substrate_name: H2O; Uridine 3'-phosphate

substrate: H2O; Uridine 3'-phosphate


enzyme_display_name: Deleted entry

organism: Enterococcus faecalis

substrate_name: NADH; H+; O2

kcat_display: Not reported

km_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

ki_unit: mM

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

mutation_type: substitution

assay_conditions_summary: cofactor NADH

proof_lines: SABIO-RK modifier species: Procion Yellow H-E4R

enzyme: Deleted entry

substrate: NADH; H+; O2


organism: Saccharomyces cerevisiae

substrate_name: Hexacyanoferrate(III); NADH

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

km_unit: mM

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

substrate: Hexacyanoferrate(III); NADH

status: unverified


substrate_name: NADH; Hexacyanoferrate(III)

substrate: NADH; Hexacyanoferrate(III)


organism: Thermus thermophilus

substrate_name: FAD; NADH

sequence_source: UniProtKB

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

substrate: FAD; NADH


organism: Bos taurus

substrate_name: Ubiquinone; NADH

substrate: Ubiquinone; NADH


organism: Clostridium thermohydrosulfuricum

substrate_name: NADH; O2; H+

substrate: NADH; O2; H+


organism: Homo sapiens

substrate_name: Ferricytochrome c; NADH; H+

substrate: Ferricytochrome c; NADH; H+


organism: Lactococcus lactis subsp. lactis


organism: Rattus norvegicus

substrate_name: NADH; Ubiquinone

substrate: NADH; Ubiquinone


organism: Treponema hyodysenteriae

substrate_name: NADH; H+; Acceptor

sequence_source: UniProtKB Q59917; direct UniProt record references PMID 8491717

substrate: NADH; H+; Acceptor


enzyme_display_name: Transferred entry: 7.1.1.9

substrate_name: Ferrocytochrome c; O2

enzyme: Transferred entry: 7.1.1.9

substrate: Ferrocytochrome c; O2


organism: Bacillus subtilis


substrate_name: O2; Ferrocytochrome c

substrate: O2; Ferrocytochrome c


substrate_name: Ferrocytochrome c

source_db: oed

source_license: CC BY 4.0

substrate: Ferrocytochrome c

source: oed


kcat_over_km_origin: calculated

data_origin: experimental


substrate_name: NADH; Aquacob(III)alamin; H+

substrate: NADH; Aquacob(III)alamin; H+


substrate_name: NADH; H+; Aquacob(III)alamin

assay_conditions_summary: cofactor NADPH

substrate: NADH; H+; Aquacob(III)alamin


substrate_name: H+; Aquacob(III)alamin; NADH

proof_lines: SABIO-RK modifier species: aquacobalamin reductase(Enzyme) mutant cblC

substrate: H+; Aquacob(III)alamin; NADH


substrate_name: Aquacob(III)alamin; H+; NADH

assay_conditions_summary: cofactor NAD+

substrate: Aquacob(III)alamin; H+; NADH


enzyme_display_name: DNA helicase

source_db: uniprot

enzyme: DNA helicase

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

substrate: peptide TSAVLQSGFRK-NH(2)


organism: Escherichia coli

substrate_name: H2O; ATP

proof_lines: SABIO-RK modifier species: DNA helicase(Enzyme) mutant uvrD252

substrate: H2O; ATP


substrate_name: ATP; H2O

substrate: ATP; H2O


proof_lines: SABIO-RK modifier species: DNA helicase(Enzyme) mutant 167-641, N-terminal His6-tagged


enzyme_display_name: [tau protein] kinase

organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

enzyme: [tau protein] kinase


substrate_name: alpha-casein

proof_lines: Maximal velocity nearly identical for the reactions with alpha-casein and PER2 peptide.

substrate: alpha-casein


organism: Trypanosoma brucei

substrate_name: Peptide; ATP

substrate: Peptide; ATP


organism: Roseovarius nubinhibens

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB reviewed (Swiss-Prot) accession A3SI50

assay_conditions_summary: pH 9; 313.15 K; cofactor FAD

source: skid


proof_lines: All kinetic experiments are done with 10 mm Tris-HCl, 0.01% Triton X-100, and 10 mm DTT and at pH 8.5.


organism: Mus musculus

substrate_name: histone H4K20me1 peptide

substrate: histone H4K20me1 peptide


substrate_name: histone octamer

substrate: histone octamer


enzyme_display_name: Transferred entry: 3.13.2.1

substrate_name: H2O; S-Adenosyl-L-homocysteine

proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C112S

enzyme: Transferred entry: 3.13.2.1

substrate: H2O; S-Adenosyl-L-homocysteine


proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C78S


proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C112A


organism: Thermotoga maritima

substrate_name: S-Adenosyl-L-homocysteine; H2O

substrate: S-Adenosyl-L-homocysteine; H2O


organism: Beta vulgaris


organism: Mesocricetus auratus


substrate_name: Homocysteine; Adenosine

substrate: Homocysteine; Adenosine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C421S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C421S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C113D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C113D


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C113S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C113S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C421D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C421D


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C195D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C195D


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C195S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C195S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C78A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteinase(Enzyme) mutant C78A


enzyme_display_name: laccase

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

enzyme: laccase


substrate_name: sinapate

sequence_variant_note: Mutation signature R416A matches the mutant residue at offset +0 and the reference residue at offset +13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: sinapate


enzyme_display_name: thymidylate synthase

organism: Lactobacillus casei

sequence_source: UniProtKB P00469 canonical protein sequence reconstructed with mutation R23S

sequence_variant_note: Mutation signature R23S matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

enzyme: thymidylate synthase


substrate_name: dUMP

sequence_source: UniProtKB P00469 canonical protein sequence reconstructed with mutation R179P

sequence_variant_note: Mutation signature R179P matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: dUMP


sequence_source: UniProtKB P00469 canonical protein sequence reconstructed with mutation R179W

sequence_variant_note: Mutation signature R179W matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P00469 canonical protein sequence reconstructed with mutation R179H

sequence_variant_note: Mutation signature R179H matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P00469 canonical protein sequence reconstructed with mutation R218K


sequence_source: UniProtKB P00469 canonical protein sequence reconstructed with mutation R178A

sequence_variant_note: Mutation signature R178A matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P00469 canonical protein sequence reconstructed with mutation R23N

sequence_variant_note: Mutation signature R23N matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P00469 canonical protein sequence reconstructed with mutation R23Q

sequence_variant_note: Mutation signature R23Q matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: Bacteriophage T4

sequence_source: UniProtKB P00471 FASTA direct check; reviewed entry TYSY_BPT4, Enterobacteria phage T4, EC 2.1.1.45; variant sequence reconstructed by applying R137K


sequence_source: UniProtKB P00471 FASTA direct check; reviewed entry TYSY_BPT4, Enterobacteria phage T4, EC 2.1.1.45

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_source: UniProtKB P00471 FASTA direct check; reviewed entry TYSY_BPT4, Enterobacteria phage T4, EC 2.1.1.45; variant sequence reconstructed by applying C156S


sequence_source: UniProtKB P00471 FASTA direct check; reviewed entry TYSY_BPT4, Enterobacteria phage T4, EC 2.1.1.45; variant sequence reconstructed by applying P155A


sequence_source: UniProtKB P00471 FASTA direct check; reviewed entry TYSY_BPT4, Enterobacteria phage T4, EC 2.1.1.45; variant sequence reconstructed by applying K49R


sequence_source: UniProt:P00471 canonical wild-type sequence


sequence_source: UniProt:P00471 canonical sequence reconstructed with selected-batch mutation P155A


sequence_source: UniProt:P00471 canonical sequence reconstructed with selected-batch mutation K48R


sequence_source: UniProt:P0A886 canonical sequence reconstructed with selected-batch mutation G257K

sequence_variant_note: Mutation signature G257K matches the mutant residue at offset +0 and the reference residue at offset -6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProt:P0A886 canonical sequence reconstructed with selected-batch mutation G23K/E86K


sequence_source: UniProt:P0A886 canonical wild-type sequence


sequence_source: UniProt:P0A886 canonical sequence reconstructed with selected-batch mutation E86K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence direct REST check plus row mutation_signature R179D reconstruction and applied mutation signature R179D to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179G to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 3.2, column 'Km (uM)' sub-column 'THF' = 28, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.14. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 3.2 s^-1, already in s^-1, so no unit conversion applies and the value stays 3.2 s^(-1). Km: printed 28 uM; 1 uM is 0.001 mM, so 28 / 1000 = 0.028 mM. kcat/Km: printed 0.14 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.14 x 1000 = 140 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row G (R179G): printed kcat = 3.2 s^-1, printed Km in the 'THF' sub-column = 28 uM, printed kcat/Km in the 'THF' sub-column = 0.14 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row G (R179G), dTMP formation with CH2H4folate varied

table_label: Table I: Kinetic and binding constants for L.casei TS R23 and R178 mutants (Protein Engineering 2000, 13(8):557-563); the printed table continues with the Residue 179 and Residue 218 blocks under the same column heads

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence direct REST check plus row mutation_signature R23A reconstruction and applied mutation signature R23A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence direct REST check plus row mutation_signature R23Y reconstruction and applied mutation signature R23Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00469 canonical sequence direct REST check plus row mutation_signature R23A reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence direct REST check plus row mutation_signature R179G reconstruction and applied mutation signature R179G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence direct REST check plus row mutation_signature R23I reconstruction and applied mutation signature R23I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence direct REST check plus row mutation_signature R23P reconstruction and applied mutation signature R23P to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P0A886 direct REST lookup (https://rest.uniprot.org/uniprotkb/P0A886.json)

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


organism: Homo sapiens

sequence_source: UniProtKB P04818 direct REST lookup (https://rest.uniprot.org/uniprotkb/P04818.json)


sequence_source: UniProtKB P00469 direct REST lookup (https://rest.uniprot.org/uniprotkb/P00469.json)

sequence_variant_note: Mutation signature R179L matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature R23D matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00471 canonical sequence reconstructed with H157V after direct residue check


sequence_source: UniProtKB:P00471 canonical sequence reconstructed with K48R after direct residue check


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence retrieved by direct lookup; reconstructed substitution R179V and applied mutation signature R179V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence retrieved by direct lookup; reconstructed substitution R179H and applied mutation signature R179H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence retrieved by direct lookup; reconstructed substitution R23K and applied mutation signature R23K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence retrieved by direct lookup; reconstructed substitution R23F and applied mutation signature R23F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence retrieved by direct lookup; reconstructed substitution R178C and applied mutation signature R178C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence retrieved by direct lookup; reconstructed substitution R179G and applied mutation signature R179G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179Q to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 2.3, column 'Km (uM)' sub-column 'THF' = 27, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.07. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 2.3 s^-1, already in s^-1, so no unit conversion applies and the value stays 2.3 s^(-1). Km: printed 27 uM; 1 uM is 0.001 mM, so 27 / 1000 = 0.027 mM. kcat/Km: printed 0.07 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.07 x 1000 = 70 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row Q (R179Q): printed kcat = 2.3 s^-1, printed Km in the 'THF' sub-column = 27 uM, printed kcat/Km in the 'THF' sub-column = 0.07 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row Q (R179Q), dTMP formation with CH2H4folate varied


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence retrieved by direct lookup; reconstructed substitution R23V and applied mutation signature R23V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 plus row-specific substitution reconstruction and applied mutation signature R23G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 plus row-specific substitution reconstruction and applied mutation signature R23Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 plus row-specific substitution reconstruction and applied mutation signature R178S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 plus row-specific substitution reconstruction and applied mutation signature R23V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 plus row-specific substitution reconstruction and applied mutation signature R178A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 plus row-specific substitution reconstruction and applied mutation signature R179C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 plus row-specific substitution reconstruction and applied mutation signature R23N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 plus row-specific substitution reconstruction and applied mutation signature R179P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P00469 plus direct single-substitution reconstruction and applied mutation signature R23K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P00469 plus direct single-substitution reconstruction and applied mutation signature R23S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P00469 plus direct single-substitution reconstruction and applied mutation signature R23E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P00469 plus direct single-substitution reconstruction and applied mutation signature R179L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P00469 plus direct single-substitution reconstruction and applied mutation signature R178K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P00469 plus direct single-substitution reconstruction and applied mutation signature R179K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P00469 plus direct single-substitution reconstruction and applied mutation signature R23D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179S to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 2.3, column 'Km (uM)' sub-column 'THF' = 19, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.089. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 2.3 s^-1, already in s^-1, so no unit conversion applies and the value stays 2.3 s^(-1). Km: printed 19 uM; 1 uM is 0.001 mM, so 19 / 1000 = 0.019 mM. kcat/Km: printed 0.089 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.089 x 1000 = 89 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row S (R179S): printed kcat = 2.3 s^-1, printed Km in the 'THF' sub-column = 19 uM, printed kcat/Km in the 'THF' sub-column = 0.089 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row S (R179S), dTMP formation with CH2H4folate varied


sequence_source: UniProtKB:P00469 canonical sequence with row-specific R218K substitution reconstructed after residue-coordinate check

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_source: UniProtKB:P00469 canonical sequence with row-specific R23S substitution reconstructed after residue-coordinate check

sequence_variant_note: Mutation signature R23S matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence with row-specific R179S substitution reconstructed after residue-coordinate check

sequence_variant_note: Mutation signature R179S matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence with row-specific R179W substitution reconstructed after residue-coordinate check

sequence_variant_note: Mutation signature R179W matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence with row-specific R23D substitution reconstructed after residue-coordinate check

sequence_variant_note: Mutation signature R23D matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence with row-specific R23L substitution reconstructed after residue-coordinate check

sequence_variant_note: Mutation signature R23L matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence with row-specific R23K substitution reconstructed after residue-coordinate check

sequence_variant_note: Mutation signature R23K matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence with row-specific R23F substitution reconstructed after residue-coordinate check

sequence_variant_note: Mutation signature R23F matches the mutant residue at offset +0 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179D to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 1.9, column 'Km (uM)' sub-column 'THF' = 37, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.057. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 1.9 s^-1, already in s^-1, so no unit conversion applies and the value stays 1.9 s^(-1). Km: printed 37 uM; 1 uM is 0.001 mM, so 37 / 1000 = 0.037 mM. kcat/Km: printed 0.057 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.057 x 1000 = 57 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row D (R179D): printed kcat = 1.9 s^-1, printed Km in the 'THF' sub-column = 37 uM, printed kcat/Km in the 'THF' sub-column = 0.057 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row D (R179D), dTMP formation with CH2H4folate varied


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R179W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179F to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 1.4, column 'Km (uM)' sub-column 'THF' = 31, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.032. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 1.4 s^-1, already in s^-1, so no unit conversion applies and the value stays 1.4 s^(-1). Km: printed 31 uM; 1 uM is 0.001 mM, so 31 / 1000 = 0.031 mM. kcat/Km: printed 0.032 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.032 x 1000 = 32 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row F (R179F): printed kcat = 1.4 s^-1, printed Km in the 'THF' sub-column = 31 uM, printed kcat/Km in the 'THF' sub-column = 0.032 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row F (R179F), dTMP formation with CH2H4folate varied


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R23E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R23P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179C to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 2.6, column 'Km (uM)' sub-column 'THF' = 26, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.073. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 2.6 s^-1, already in s^-1, so no unit conversion applies and the value stays 2.6 s^(-1). Km: printed 26 uM; 1 uM is 0.001 mM, so 26 / 1000 = 0.026 mM. kcat/Km: printed 0.073 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.073 x 1000 = 73 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row C (R179C): printed kcat = 2.6 s^-1, printed Km in the 'THF' sub-column = 26 uM, printed kcat/Km in the 'THF' sub-column = 0.073 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row C (R179C), dTMP formation with CH2H4folate varied


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179V to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 1.9, column 'Km (uM)' sub-column 'THF' = 42, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.033. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 1.9 s^-1, already in s^-1, so no unit conversion applies and the value stays 1.9 s^(-1). Km: printed 42 uM; 1 uM is 0.001 mM, so 42 / 1000 = 0.042 mM. kcat/Km: printed 0.033 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.033 x 1000 = 33 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row V (R179V): printed kcat = 1.9 s^-1, printed Km in the 'THF' sub-column = 42 uM, printed kcat/Km in the 'THF' sub-column = 0.033 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row V (R179V), dTMP formation with CH2H4folate varied


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R23G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469; local single-substitution reconstruction and applied mutation signature R23E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469; local single-substitution reconstruction and applied mutation signature R23V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469; local single-substitution reconstruction and applied mutation signature R23G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469; local single-substitution reconstruction and applied mutation signature R179Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469; local single-substitution reconstruction and applied mutation signature R179S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469; local single-substitution reconstruction and applied mutation signature R179V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469; local single-substitution reconstruction and applied mutation signature R179A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469; local single-substitution reconstruction and applied mutation signature R23L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 REST FASTA checked 2026-05-23; R179Q applied to the canonical thymidylate synthase sequence. and applied mutation signature R179Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 REST FASTA checked 2026-05-23; R23L applied to the canonical thymidylate synthase sequence. and applied mutation signature R23L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179M to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 2.5, column 'Km (uM)' sub-column 'THF' = 35, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.051. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 2.5 s^-1, already in s^-1, so no unit conversion applies and the value stays 2.5 s^(-1). Km: printed 35 uM; 1 uM is 0.001 mM, so 35 / 1000 = 0.035 mM. kcat/Km: printed 0.051 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.051 x 1000 = 51 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row M (R179M): printed kcat = 2.5 s^-1, printed Km in the 'THF' sub-column = 35 uM, printed kcat/Km in the 'THF' sub-column = 0.051 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row M (R179M), dTMP formation with CH2H4folate varied


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 REST FASTA checked 2026-05-23; R179T applied to the canonical thymidylate synthase sequence. and applied mutation signature R179T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 REST FASTA checked 2026-05-23; R23N applied to the canonical thymidylate synthase sequence. and applied mutation signature R23N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179H to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 2.6, column 'Km (uM)' sub-column 'THF' = 48, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.04. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 2.6 s^-1, already in s^-1, so no unit conversion applies and the value stays 2.6 s^(-1). Km: printed 48 uM; 1 uM is 0.001 mM, so 48 / 1000 = 0.048 mM. kcat/Km: printed 0.04 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.04 x 1000 = 40 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row H (R179H): printed kcat = 2.6 s^-1, printed Km in the 'THF' sub-column = 48 uM, printed kcat/Km in the 'THF' sub-column = 0.04 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row H (R179H), dTMP formation with CH2H4folate varied


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 REST FASTA checked 2026-05-23; R23Y applied to the canonical thymidylate synthase sequence. and applied mutation signature R23Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 REST FASTA checked 2026-05-23; R178C applied to the canonical thymidylate synthase sequence. and applied mutation signature R178C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00469 canonical sequence reconstructed with V316G using PMID:1627545 mutation context

sequence_variant_note: Mutation signature V316G matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence reconstructed with V316Y using PMID:1627545 mutation context

sequence_variant_note: Mutation signature V316Y matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence reconstructed with V316T using PMID:1627545 mutation context

sequence_variant_note: Mutation signature V316T matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence reconstructed with V316W using PMID:1627545 mutation context

sequence_variant_note: Mutation signature V316W matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence reconstructed with V316C using PMID:1627545 mutation context

sequence_variant_note: Mutation signature V316C matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence reconstructed with V316F using PMID:1627545 mutation context

sequence_variant_note: Mutation signature V316F matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P00469 canonical sequence reconstructed with V316K using PMID:1627545 mutation context

sequence_variant_note: Mutation signature V316K matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProtKB P00469 canonical sequence fetched by REST/FASTA on 2026-05-23 plus PMID 1627545 Val316 mutation context.

sequence_variant_note: Mutation signature V316H matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature V316A matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature V316R matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature V316I matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature V316P matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature V316L matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature V316E matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316E to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row E (V316E); column 'k_cat (s^-1)' = 0.15; column 'K_m (uM), dUMP sub-column' = 2.5; column 'k_cat/K_m (s^-1 uM^-1), dUMP sub-column' = 0.060.

normalized_value_unit_evidence: kcat: printed Table I cell 0.15 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.15 s^(-1). Km: printed Table I cell 2.5 uM; 2.5 / 1000 = 0.0025 mM. kcat/Km: printed Table I cell 0.060 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.060 x 1000 = 60.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row E (V316E), dTMP formation, dUMP axis: k_cat = 0.15 s^-1; K_m = 2.5 uM; printed k_cat/K_m = 0.060 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row E (V316E), dTMP formation, dUMP axis


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence reconstructed with PMID:1627545 V316E substitution and applied mutation signature V316E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316M to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row M (V316M); column 'k_cat (s^-1)' = 0.65; column 'K_m (uM), dUMP sub-column' = 2.5; column 'k_cat/K_m (s^-1 uM^-1), dUMP sub-column' = 0.26.

normalized_value_unit_evidence: kcat: printed Table I cell 0.65 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.65 s^(-1). Km: printed Table I cell 2.5 uM; 2.5 / 1000 = 0.0025 mM. kcat/Km: printed Table I cell 0.26 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.26 x 1000 = 260.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row M (V316M), dTMP formation, dUMP axis: k_cat = 0.65 s^-1; K_m = 2.5 uM; printed k_cat/K_m = 0.26 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row M (V316M), dTMP formation, dUMP axis


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316S to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row S (V316S); column 'k_cat (s^-1)' = 0.54; column 'K_m (uM), dUMP sub-column' = 1.7; column 'k_cat/K_m (s^-1 uM^-1), dUMP sub-column' = 0.32.

normalized_value_unit_evidence: kcat: printed Table I cell 0.54 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.54 s^(-1). Km: printed Table I cell 1.7 uM; 1.7 / 1000 = 0.0017 mM. kcat/Km: printed Table I cell 0.32 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.32 x 1000 = 320.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row S (V316S), dTMP formation, dUMP axis: k_cat = 0.54 s^-1; K_m = 1.7 uM; printed k_cat/K_m = 0.32 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row S (V316S), dTMP formation, dUMP axis


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence reconstructed with PMID:1627545 V316S substitution and applied mutation signature V316S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316R to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row R (V316R); column 'k_cat (s^-1)' = 0.020; column 'K_m (uM), dUMP sub-column' = 1.5; column 'k_cat/K_m (s^-1 uM^-1), dUMP sub-column' = 0.014.

normalized_value_unit_evidence: kcat: printed Table I cell 0.020 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.02 s^(-1). Km: printed Table I cell 1.5 uM; 1.5 / 1000 = 0.0015 mM. kcat/Km: printed Table I cell 0.014 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.014 x 1000 = 14.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row R (V316R), dTMP formation, dUMP axis: k_cat = 0.020 s^-1; K_m = 1.5 uM; printed k_cat/K_m = 0.014 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row R (V316R), dTMP formation, dUMP axis


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316L to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row L (V316L); column 'k_cat (s^-1)' = 1.3; column 'K_m (uM), dUMP sub-column' = 1.7; column 'k_cat/K_m (s^-1 uM^-1), dUMP sub-column' = 0.81.

normalized_value_unit_evidence: kcat: printed Table I cell 1.3 s^-1; already in s^-1, no unit conversion applies; the paper value is 1.3 s^(-1). Km: printed Table I cell 1.7 uM; 1.7 / 1000 = 0.0017 mM. kcat/Km: printed Table I cell 0.81 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.81 x 1000 = 810.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row L (V316L), dTMP formation, dUMP axis: k_cat = 1.3 s^-1; K_m = 1.7 uM; printed k_cat/K_m = 0.81 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row L (V316L), dTMP formation, dUMP axis


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence reconstructed with PMID:1627545 V316N substitution and applied mutation signature V316N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewed row-specific V316I reconstruction and applied mutation signature V316I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316C to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row C (V316C); column 'k_cat (s^-1)' = 1.1; column 'K_m (uM), CH2H4folate sub-column' = 77; column 'k_cat/K_m (s^-1 uM^-1), CH2H4folate sub-column' = 0.015.

normalized_value_unit_evidence: kcat: printed Table I cell 1.1 s^-1; already in s^-1, no unit conversion applies; the paper value is 1.1 s^(-1). Km: printed Table I cell 77 uM; 77 / 1000 = 0.077 mM. kcat/Km: printed Table I cell 0.015 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.015 x 1000 = 15.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row C (V316C), dTMP formation, CH2H4folate axis: k_cat = 1.1 s^-1; K_m = 77 uM; printed k_cat/K_m = 0.015 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row C (V316C), dTMP formation, CH2H4folate axis


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewed row-specific R179E reconstruction and applied mutation signature R179E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewed row-specific R179K reconstruction and applied mutation signature R179K to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00469 canonical sequence with reviewed row-specific R179K reconstruction


sequence_source: UniProtKB:P00469 canonical sequence with reviewed row-specific R179E reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewed row-specific R179T reconstruction and applied mutation signature R179T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewed row-specific R179A reconstruction and applied mutation signature R179A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 direct FASTA; row-specific R23Q substitution reconstructed after residue check and applied mutation signature R23Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 direct FASTA; row-specific R179M substitution reconstructed after residue check and applied mutation signature R179M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 direct FASTA; row-specific R23A substitution reconstructed after residue check and applied mutation signature R23A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature R179L to reconstruct the assayed variant sequence.

column_label: Table I column group 'dTMP formation', column 'kcat (s-1)a' = 2.3, column 'Km (uM)' sub-column 'THF' = 51, column 'kcat/Km (s-1 uM-1)' sub-column 'THF' = 0.033. The printed Table I line for this mutant also carries the other dTMP-formation sub-column, and where the paper measured them the PLP-binding Kd sub-columns and the BrdUMP dehalogenation columns.

normalized_value_unit_evidence: kcat: printed 2.3 s^-1, already in s^-1, so no unit conversion applies and the value stays 2.3 s^(-1). Km: printed 51 uM; 1 uM is 0.001 mM, so 51 / 1000 = 0.051 mM. kcat/Km: printed 0.033 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.033 x 1000 = 33 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, Residue 179 block, mutant row L (R179L): printed kcat = 2.3 s^-1, printed Km in the 'THF' sub-column = 51 uM, printed kcat/Km in the 'THF' sub-column = 0.033 s^-1 uM^-1.

row_label: Table I, Residue 179 block, mutant row L (R179L), dTMP formation with CH2H4folate varied


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 direct FASTA; row-specific R179F substitution reconstructed after residue check and applied mutation signature R179F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 direct FASTA; row-specific R178K substitution reconstructed after residue check and applied mutation signature R178K to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P00469 direct FASTA; row-specific R179M substitution reconstructed after residue check


sequence_source: UniProtKB reviewed accession P00469 direct FASTA; row-specific R179F substitution reconstructed after residue check


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316K to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row K (V316K); column 'k_cat (s^-1)' = 0.12; column 'K_m (uM), dUMP sub-column' = 1.2; column 'k_cat/K_m (s^-1 uM^-1), dUMP sub-column' = 0.099.

normalized_value_unit_evidence: kcat: printed Table I cell 0.12 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.12 s^(-1). Km: printed Table I cell 1.2 uM; 1.2 / 1000 = 0.0012 mM. kcat/Km: printed Table I cell 0.099 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.099 x 1000 = 99.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row K (V316K), dTMP formation, dUMP axis: k_cat = 0.12 s^-1; K_m = 1.2 uM; printed k_cat/K_m = 0.099 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row K (V316K), dTMP formation, dUMP axis


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 plus direct V316 substitution reconstruction and applied mutation signature V316Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316N to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row N (V316N); column 'k_cat (s^-1)' = 0.39; column 'K_m (uM), dUMP sub-column' = 1.4; column 'k_cat/K_m (s^-1 uM^-1), dUMP sub-column' = 0.27.

normalized_value_unit_evidence: kcat: printed Table I cell 0.39 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.39 s^(-1). Km: printed Table I cell 1.4 uM; 1.4 / 1000 = 0.0014 mM. kcat/Km: printed Table I cell 0.27 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.27 x 1000 = 270.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row N (V316N), dTMP formation, dUMP axis: k_cat = 0.39 s^-1; K_m = 1.4 uM; printed k_cat/K_m = 0.27 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row N (V316N), dTMP formation, dUMP axis


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 plus direct V316 substitution reconstruction and applied mutation signature V316S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 plus direct V316 substitution reconstruction and applied mutation signature V316M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 plus direct V316 substitution reconstruction and applied mutation signature V316T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00469 and applied mutation signature V316P to reconstruct the assayed variant sequence.

column_label: Table I: Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS (Biochemistry 1992, 31, 6032-6038); decoded printed column heads residue 316 | Thy- media | k_cat (s^-1) | K_m (uM) for CH2H4folate and dUMP | k_cat/K_m (s^-1 uM^-1) for CH2H4folate and dUMP | BrdUMP dehalogenation k_cat (s^-1) and K_m (uM), residue 316 row P (V316P); column 'k_cat (s^-1)' = 0.60; column 'K_m (uM), dUMP sub-column' = 4.2; column 'k_cat/K_m (s^-1 uM^-1), dUMP sub-column' = 0.14.

normalized_value_unit_evidence: kcat: printed Table I cell 0.60 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.6 s^(-1). Km: printed Table I cell 4.2 uM; 4.2 / 1000 = 0.0042 mM. kcat/Km: printed Table I cell 0.14 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.14 x 1000 = 140.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, residue 316 row P (V316P), dTMP formation, dUMP axis: k_cat = 0.60 s^-1; K_m = 4.2 uM; printed k_cat/K_m = 0.14 s^-1 uM^-1.

row_label: Table I. Steady-State Kinetic Constants for Val 316 Mutants of L. casei TS, residue 316 row P (V316P), dTMP formation, dUMP axis


sequence_source: UniProtKB:P00469 plus direct V316 substitution reconstruction


sequence_source: Reconstructed from UniProtKB P00469 canonical sequence by applying V316H; UniProt checked directly on 2026-05-23.

sequence_variant_note: Mutation signature V316H matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProtKB P00469 canonical sequence by applying V316G; UniProt checked directly on 2026-05-23.

sequence_variant_note: Mutation signature V316G matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProtKB P00469 canonical sequence by applying V316Q; UniProt checked directly on 2026-05-23.

sequence_variant_note: Mutation signature V316Q matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProtKB P00469 canonical sequence by applying V316W; UniProt checked directly on 2026-05-23.

sequence_variant_note: Mutation signature V316W matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProtKB P00469 canonical sequence by applying V316F; UniProt checked directly on 2026-05-23.

sequence_variant_note: Mutation signature V316F matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProtKB P00469 canonical sequence by applying V316A; UniProt checked directly on 2026-05-23.

sequence_variant_note: Mutation signature V316A matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProtKB P00469 canonical sequence by applying V316K; UniProt checked directly on 2026-05-23.

sequence_variant_note: Mutation signature V316K matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 (TYSY_LACCA), REST lookup 2026-05-23; R178S reconstructed from the canonical sequence after confirming residue 178 is R. and applied mutation signature R178S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 (TYSY_LACCA), REST lookup 2026-05-23; R179C reconstructed from the canonical sequence after confirming residue 179 is R. and applied mutation signature R179C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P00469 (TYSY_LACCA), REST lookup 2026-05-23.

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 (TYSY_LACCA), REST lookup 2026-05-23; N229D reconstructed from the canonical sequence after confirming residue 229 is N. and applied mutation signature N229D to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P00469 (TYSY_LACCA), REST lookup 2026-05-23; N229D reconstructed from the canonical sequence after confirming residue 229 is N.


substrate_name: dCMP

substrate: dCMP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00469 (TYSY_LACCA), REST lookup 2026-05-23; V316A reconstructed from the canonical sequence after confirming residue 316 is V. and applied mutation signature V316A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewer-applied W82Y reconstruction and applied mutation signature W82Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewer-applied W82A reconstruction and applied mutation signature W82A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewer-applied W82L reconstruction and applied mutation signature W82L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewer-applied W82D reconstruction and applied mutation signature W82D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewer-applied W82S reconstruction and applied mutation signature W82S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00469 canonical sequence with reviewer-applied W82S reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00469 canonical sequence with reviewer-applied W82H reconstruction and applied mutation signature W82H to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00469 canonical sequence with reviewer-applied W82H reconstruction


organism: Leishmania major

sequence_source: UniProtKB:P07382 FASTA retrieved during exact accession lookup


sequence_source: UniProtKB:P07382 FASTA plus PMID 8144647 M53R mutation reconstruction

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


organism: Trypanosoma cruzi

sequence_source: UniProtKB:Q27793 FASTA retrieved during exact accession lookup


sequence_source: UniProtKB:P00469 REST/FASTA direct check on 2026-05-23; W82G reconstructed from the canonical P00469 sequence after confirming residue 82 is W.


sequence_source: UniProtKB:P00469 REST/FASTA direct check on 2026-05-23; W82V reconstructed from the canonical P00469 sequence after confirming residue 82 is W.


sequence_source: UniProtKB:P00469 REST/FASTA direct check on 2026-05-23; W82F reconstructed from the canonical P00469 sequence after confirming residue 82 is W.


sequence_source: UniProtKB:P00469 REST/FASTA direct check on 2026-05-23; W82H reconstructed from the canonical P00469 sequence after confirming residue 82 is W.


sequence_source: UniProtKB:P00469 REST/FASTA direct check on 2026-05-23.


sequence_source: UniProtKB:P00469 REST/FASTA direct check on 2026-05-23; W82M reconstructed from the canonical P00469 sequence after confirming residue 82 is W.


sequence_source: UniProtKB:P00469 REST/FASTA direct check on 2026-05-23; W82Y reconstructed from the canonical P00469 sequence after confirming residue 82 is W.


enzyme_display_name: phospholipase A2

organism: Bos taurus

assay_conditions_summary: pH 4

enzyme: phospholipase A2


organism: Agaricus placomyces

substrate_name: hydroquinone

sequence: DVIGPQAQVTLANQD

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

substrate: hydroquinone


organism: Bacillus stratosphericus

substrate_name: ABTS

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

substrate: ABTS


organism: Cerrena unicolor

substrate_name: syringaldazine

sequence: AIGPVADLH

wild_type_sequence: AIGPVADLH

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

substrate: syringaldazine


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature W82A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature W82F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature W82R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature W82N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature W82M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature W82S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature W82L to reconstruct the assayed variant sequence.


organism: Bothrops bilineatus smaragdinus

substrate_name: 4-nitro-3-octanoyloxy-benzoic acid

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

substrate: 4-nitro-3-octanoyloxy-benzoic acid


organism: Crotalus durissus ruruima

substrate_name: 4-nitro-3-(octanoyloxy)-benzoic acid

substrate: 4-nitro-3-(octanoyloxy)-benzoic acid


organism: Trametes hirsuta

substrate_name: ABTS (at pH 6.0 and 50 degrees Celsius)

assay_conditions_summary: pH 6

proof_lines: kcat is 129.37 sec(-1) for ABTS oxidation (at pH 6.0 and 50 degrees Celsius).

substrate: ABTS (at pH 6.0 and 50 degrees Celsius)


organism: Anopheles gambiae

proof_lines: kcat is 1571 min(-1) with hydroquinone as substrate (PubMed:22479493). kcat is 306 min(-1) with catechol as substrate (PubMed:22479493). kcat is 93 min(-1) with DOPA as substrate (PubMed:22479493). kcat is 274 min(-1) with dopamine as subst


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 16.8 sec(-1) with ABTS as substrate (PubMed:11884407). kcat is 322 sec(-1) with ABTS as substrate (PubMed:18307408). kcat is 144 sec(-1) with ABTS as substrate (PubMed:22481612). kcat is 3.7 sec(-1) with SGZ as substrate (PubMed:118


organism: Fomitopsis schrenkii

substrate_name: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) (at pH 3.0 and 30 degrees Celsius)

assay_conditions_summary: pH 3

proof_lines: kcat is 409 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate (at pH 3.0 and 30 degrees Celsius). kcat is 23.1 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate (at p


proof_lines: kcat is 315 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate (at pH 3.0 and 30 degrees Celsius). kcat is 42.6 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate (at p

substrate: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) (at pH 3.0 and 30 degrees Celsius)


organism: Ganoderma australe

substrate_name: ABTS (at pH 6.0 and 55 degrees Celsius)

proof_lines: kcat is 273 sec(-1) for ABTS oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 259 sec(-1) for catechol oxidation (at pH 6.0 and 55 degrees Celsius) (PubMed:34467865). kcat is 237 sec(-1) for 2,6-dimethylphenol oxidati

substrate: ABTS (at pH 6.0 and 55 degrees Celsius)


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

proof_lines: kcat is 9.9 sec(-1) with 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid as substrate. kcat is 21.7 sec(-1) with syringaldazine as substrate. Optimal activity at 200 mM salt, with 65% activity at 1 M NaCl.


enzyme_display_name: anthranilate phosphoribosyltransferase

organism: Saccharolobus solfataricus

substrate_name: anthranilate

sequence_variant_note: Resolved canonical sequence from UniProt P50384 canonical sequence with selected OED mutation signature applied and applied mutation signature I36E/M47D/D83G/F149S to reconstruct the assayed variant sequence.

enzyme: anthranilate phosphoribosyltransferase

substrate: anthranilate


sequence_variant_note: Resolved canonical sequence from UniProt P50384 canonical sequence with selected OED mutation signature applied and applied mutation signature I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P50384 canonical sequence with selected OED mutation signature applied and applied mutation signature I36E/M47D/D83G/N109S/F149S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P50384 canonical sequence with selected OED mutation signature applied and applied mutation signature I36E/M47D/D83G/F149S/L320M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P50384 canonical sequence with selected OED mutation signature applied and applied mutation signature I36E/M47D/D83G/F149S/F193S to reconstruct the assayed variant sequence.


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProt P50384 canonical sequence with selected OED mutation signature applied

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


sequence_variant_note: Resolved canonical sequence from UniProt P50384 canonical sequence with selected OED mutation signature applied and applied mutation signature I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M to reconstruct the assayed variant sequence.


sequence_source: direct UniProtKB REST lookup for reviewed accession P50384; matches identity reuse cache accession:P50384

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.2
Raw SKiD Env: Temp=87°C, pH=-----
Raw SKiD Env: Temp=60°C, pH=-----


organism: Sulfolobus solfataricus

substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_source: reconstructed from direct UniProtKB P50384 canonical sequence after validating source mutation signature D223N against the canonical residues (D223N)

sequence_variant_note: Mutation signature D223N matches the mutant residue at offset +0 and the reference residue at offset -14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate


substrate_name: Anthranilate

sequence_source: reconstructed from direct UniProtKB P50384 canonical sequence after validating source mutation signature K106Q against the canonical residues (K106Q)

sequence_variant_note: Mutation signature K106Q matches the mutant residue at offset +0 and the reference residue at offset +9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: Anthranilate


sequence_source: reconstructed from direct UniProtKB P50384 canonical sequence after validating source mutation signature H107A against the canonical residues (H107A)

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_source: reconstructed from direct UniProtKB P50384 canonical sequence after validating source mutation signature R164A/H154A against the canonical residues (R164A, H154A)


sequence_source: reconstructed from direct UniProtKB P50384 canonical sequence after validating source mutation signature E224Q against the canonical residues (E224Q)

sequence_variant_note: Mutation signature E224Q matches the mutant residue at offset +0 and the reference residue at offset -5; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I36E/M47D/D83G/F149S/I169T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I36E/M47D/T77I/D83G/F149S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I36E/M47D/D83G/F149S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I36E/M47D/D83G/F149S/L320M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P50384 canonical sequence with H107A/P178A applied after direct residue check and applied mutation signature H107A/P178A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P50384 canonical sequence with R164A applied after direct residue check and applied mutation signature R164A to reconstruct the assayed variant sequence.


organism: Thermococcus kodakarensis

sequence_source: UniProtKB:Q9YGB4 canonical sequence from direct accession lookup

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


organism: Escherichia coli (strain K12)

substrate_name: chorismate (at pH 7.5)

substrate: chorismate (at pH 7.5)


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: magnesium (at 60 degrees Celsius and at pH 7.5)


organism: Escherichia coli

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, P444G


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant P444A

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, P444A


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D439A, P444A

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, D439A, P444A


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant D439A

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, D439A


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant P444L

proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant deletion aa367-416, P444L


proof_lines: SABIO-RK modifier species: laccase(Enzyme) mutant P444I


organism: Marinomonas mediterranea

sequence_source: UniProtKB:Q9KJB8 direct accession lookup on 2026-05-24


organism: Thermus thermophilus

sequence_source: UniProtKB exact accession lookup Q72HW2, retrieved 2026-05-24


organism: Trametes versicolor

substrate_name: Methyl syringate; O2

sequence_source: UniProtKB Q12718 direct REST accession check

substrate: Methyl syringate; O2


organism: Bacillus pumilus

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


organism: Bacillus tequilensis


organism: Carica papaya


organism: Klebsiella pneumoniae


organism: Sporothrix carnis


organism: Streptomyces griseorubens


organism: Thielavia sp.


organism: Pleurotus ostreatus


organism: Trametes hirsuta

substrate_name: O2; 2,6-Dimethoxyphenol

substrate: O2; 2,6-Dimethoxyphenol


organism: Trametes polyzona


organism: Trametes sp.


substrate_name: O2; Syringic acid

substrate: O2; Syringic acid


enzyme_display_name: pyruvate kinase

organism: Homo sapiens

sequence_source: UniProtKB:P14618 canonical sequence retrieved by exact accession lookup.

enzyme: pyruvate kinase


organism: Arabidopsis thaliana

substrate_name: Phosphoenolpyruvate; ADP

substrate: Phosphoenolpyruvate; ADP


organism: Corynebacterium glutamicum

substrate_name: ADP; Phosphoenolpyruvate

sequence_source: UniProtKB:Q46078 direct accession lookup on 2026-05-24

substrate: ADP; Phosphoenolpyruvate


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB exact accession P52489 REST lookup (2026-05-24)


organism: Bos taurus

assay_conditions_summary: cofactor ADP


organism: Brassica napus


organism: Plasmodium falciparum


organism: Rattus norvegicus


sequence_variant_note: Resolved canonical sequence from UniProt P00549 canonical sequence with validated row-specific substitution T298A applied at offset 0. and applied mutation signature T298A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme Pyk1 T298A


sequence_source: UniProt P00549 canonical sequence checked, but selected mutation numbering did not validate against that canonical sequence.

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme PYK1 S384P


sequence_source: UniProt P00549 canonical sequence from direct accession lookup; no mutation signature is present in the selected source snapshots.


organism: Ricinus communis


organism: Spinacia oleracea


organism: Streptococcus mutans


organism: Toxoplasma gondii


organism: Trypanosoma brucei


enzyme_display_name: beta-galactosidase

substrate_name: H2O; p-Nitrophenyl-beta-D-galactoside

sequence_source: UniProtKB:Q9SCV8 canonical sequence, direct lookup 2026-05-24

enzyme: beta-galactosidase

substrate: H2O; p-Nitrophenyl-beta-D-galactoside


organism: Arthrobacter sp.

substrate_name: o-Nitrophenyl-beta-D-galactoside; H2O

sequence_source: UniProtKB:Q7WTU5 canonical sequence, direct lookup 2026-05-24

substrate: o-Nitrophenyl-beta-D-galactoside; H2O


organism: Aspergillus niger

substrate_name: H2O; Lactose

sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24

substrate: H2O; Lactose


sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24, with selected-batch mutation signature Y304F/Y355H/N357G/W806F applied

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Y304F/Y355H/N357G/W806F His6-tagged


sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24, with selected-batch mutation signature W806F applied

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W806F His6-tagged


sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24, with selected-batch mutation signature W806S applied

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W806S His6-tagged


substrate_name: Lactose; H2O

sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24, with selected-batch mutation signature Y304F/Y355H/N357G applied

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Y304F/Y355H/N357G His6-tagged

substrate: Lactose; H2O


sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24, with selected-batch mutation signature Y304F applied

sequence_variant_note: Mutation signature Y304F matches the mutant residue at offset +0 and the reference residue at offset -10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Y304F His6-tagged


organism: Escherichia coli

substrate_name: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540F


substrate_name: o-Nitrophenyl beta-D-galactopyranoside 6-phosphate; H2O

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540N


substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357F

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357N


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357L


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357D


sequence_source: UniProtKB:P16278 direct lookup 2026-05-24


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant I-cell disease


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461K and applied mutation signature E461K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461Q and applied mutation signature E461Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461D and applied mutation signature E461D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461G and applied mutation signature E461G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461G


sequence_source: UniProtKB:P06864 canonical context only

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant psi epg0

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg a


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461H and applied mutation signature E461H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461H


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature H540E and applied mutation signature H540E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540E

substrate: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate


organism: Kluyveromyces lactis

sequence_source: UniProtKB:P00723 direct accession lookup (2026-05-24)


organism: Lactobacillus casei


organism: Lactobacillus delbrueckii subsp. bulgaricus

sequence_source: UniProtKB:P0C1Y0 direct accession lookup (2026-05-24)


sequence_source: UniProtKB:P0C1Y0 canonical sequence retained as context only (2026-05-24)

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0C1Y0 direct lookup plus L317F reconstruction (2026-05-24) and applied mutation signature L317F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant L317F


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant P429S


sequence_source: UniProtKB:P00722 canonical sequence from REST lookup; context only, not a row-specific variant sequence

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999F


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999Y


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant G794A


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201E-


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201N-


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201F-


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg ab

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg_b

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg_a


substrate_name: p-Nitrophenyl-beta-D-galactoside; H2O

substrate: p-Nitrophenyl-beta-D-galactoside; H2O


organism: Bifidobacterium bifidum


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391K


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391E


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391F


sequence_source: UniProtKB P00722 FASTA direct lookup on 2026-05-24; reviewed E. coli K-12 lacZ beta-galactosidase canonical sequence.


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999G


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999L


enzyme_display_name: Beta-galactosidase

organism: Trichoderma reesei

sequence_source: UniProtKB Q70SY0 FASTA

unit: lgwedgeoneswedgeone

enzyme: Beta-galactosidase


sequence_source: UniProtKB A2QAN3 canonical sequence with UniProt mutagenesis feature Y304A applied; direct lookup 2026-05-24.

sequence_variant_note: Mutation signature Y304A matches the mutant residue at offset +0 and the reference residue at offset -10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Y304A His6-tagged


organism: Aspergillus oryzae

sequence_source: UniProtKB Q2UCU3 canonical sequence; direct lookup 2026-05-24.


organism: Bacillus coagulans

sequence_source: UniProtKB A0A1L1XWG1 canonical sequence; direct lookup 2026-05-24.


organism: Bacillus subtilis

sequence_source: UniProtKB O31529 canonical sequence with UniProt mutagenesis feature E145A applied; direct lookup 2026-05-24.

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E145A


sequence_source: UniProtKB O31529 canonical sequence; direct lookup 2026-05-24.


organism: Bacteroides ovatus

sequence_source: UniProtKB A7LXS9 canonical sequence; direct lookup 2026-05-24.


organism: Lactococcus lactis subsp. lactis


organism: Mus musculus


organism: Pantoea agglomerans

column_label: PMID 17336932 characterization paragraph, Bga/oNPGal segment, Km = 0.06 mM and Vmax = 0.43 mM/min.

raw_value_unit_evidence: The Km and Vmax values for oNPGal were calculated as 0.06 mM and 0.43 mM/min, respectively.

row_label: Bga beta-galactosidase with oNPGal substrate

table_label: Characterization of the enzyme paragraph


organism: Pediococcus pentosaceus


organism: Raphanus sativus


organism: Streptococcus thermophilus


organism: Sulfolobus solfataricus

verification_status: verified

column_label: Table label: Table 3. Kinetic constuntsfor S. solfataricus 8-galactosiduse (Wiley ePDF text layer; caption OCR-mangled from 'Kinetic constants for S. solfataricus beta-galactosidase'). Row: P-NpCal. Columns read: K m (mM) cell 0.225, k cat (min^-1) cell 5700, k cat / K m (min^-1 mM^-1) cell 25333. metric: Km; raw value: 0.225; raw unit: mM; normalized value: 0.225 mM; metric: kcat; raw value: 5700; raw unit: min^-1; normalized value: 95.0 s^(-1); assay condition: Purified Sulfolobus solfataricus beta-galactosidase; Km values determined by Lineweaver-Burk plots of data from assays carried out at 75 deg C for p-NpGal (this row's substrate), as described in Experimental Procedures.

normalized_value_unit_evidence: Table 3 row P-NpCal: Km 0.225 mM = 0.225 mM (already in export units); kcat 5700 min^-1 = 5700/60 = 95.0 s^(-1) (1 min^-1 = 1/60 s^-1), an exact conversion. In the ePDF text layer the Greek beta renders variously as '8', 'P' or 'B', the substrate o-nitrophenyl-beta-D-galactoside row is rendered 'P-NpCal' (paper's p-NpGal), the kcat column header renders as 'k,,,' with unit 'min-l', and the kcat/Km column header renders as 'k C a t i K ,' with unit 'min-' x mM-'.

raw_value_unit_evidence: Table 3. Kinetic constuntsfor S. solfataricus 8-galactosiduse (Wiley ePDF text layer; caption OCR-mangled from 'Kinetic constants for S. solfataricus beta-galactosidase') | metric header row: Substrate K , k,,, k C a t i K , | units row: mM min-l min-' x mM-' | row: P-NpCal 0.225 5700 25333 | cells read: K m = 0.225 mM; k cat = 5700 min^-1; k cat / K m = 25333 min^-1 mM^-1. In the ePDF text layer the Greek beta renders variously as '8', 'P' or 'B', the substrate o-nitrophenyl-beta-D-galactoside row is rendered 'P-NpCal' (paper's p-NpGal), the kcat column header renders as 'k,,,' with unit 'min-l', and the kcat/Km column header renders as 'k C a t i K ,' with unit 'min-' x mM-'.

row_label: P-NpCal

status: verified


organism: Rattus norvegicus


organism: Escherichia coli


organism: Homo sapiens


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Lac- Gal d


organism: Oryctolagus cuniculus


organism: Pseudarthrobacter oxydans


enzyme_display_name: beta-lactamase

organism: Aeromonas hydrophila

substrate_name: H2O; Imipenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N116H/N220G

enzyme: beta-lactamase

substrate: H2O; Imipenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N220G


organism: Enterobacter cloacae

substrate_name: H2O; Cefotaxime

sequence_source: UniProtKB:P05364 direct REST lookup on 2026-05-24

substrate: H2O; Cefotaxime


substrate_name: Nitrocefin; H2O

sequence_source: UniProt REST exact accession lookup on 2026-05-24 for P13661

substrate: Nitrocefin; H2O


substrate_name: H2O; Cephaloridine

sequence_source: UniProt REST exact accession lookup on 2026-05-24 for P00811

substrate: H2O; Cephaloridine


substrate_name: H2O; Ampicillin

sequence_source: UniProtKB:P62593 direct accession lookup on 2026-05-24

substrate: H2O; Ampicillin


organism: Klebsiella pneumoniae

sequence_source: UniProtKB:C7C422 canonical sequence


organism: Serratia marcescens

substrate_name: Ampicillin; H2O

sequence_source: UniProtKB:P52699 canonical FASTA checked 2026-05-24

substrate: Ampicillin; H2O


organism: Shewanella algae

substrate_name: H2O; Penicillin G

sequence_source: UniProtKB:Q6VCW0 canonical FASTA checked 2026-05-24

substrate: H2O; Penicillin G


organism: Shewanella frigidimarina

substrate_name: H2O; Amoxicillin

sequence_source: UniProtKB:Q53BU0 canonical FASTA checked 2026-05-24

substrate: H2O; Amoxicillin


organism: Shewanella livingstonensis

substrate_name: Amoxicillin; H2O

sequence_source: UniProtKB:Q53BU1 canonical FASTA checked 2026-05-24

substrate: Amoxicillin; H2O


organism: Pseudomonas putida

sequence_source: UniProtKB direct lookup: https://rest.uniprot.org/uniprotkb/Q8GCU7.json (2026-05-24)


organism: Mycobacterium tuberculosis

substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


organism: Pseudomonas aeruginosa

substrate_name: H2O; Carbenicillin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant R234K

substrate: H2O; Carbenicillin


substrate_name: Penicillin G; H2O

sequence_source: UniProtKB Q3SAW3 direct accession lookup, active entry accessed 2026-05-24

substrate: Penicillin G; H2O


organism: Stenotrophomonas maltophilia

sequence_source: UniProtKB:P52700 direct REST FASTA/JSON lookup


substrate_name: H2O; Biapenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120N

substrate: H2O; Biapenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120C


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120S


organism: Aeromonas sobria

substrate_name: Imipenem; H2O

substrate: Imipenem; H2O


substrate_name: Cefdinir; H2O

substrate: Cefdinir; H2O


substrate_name: H2O; Cefdinir

substrate: H2O; Cefdinir


enzyme_display_name: carboxylesterase

substrate_name: p-Nitrophenyl acetate; H2O

column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-1'; substrate row 'pNPA'; column 'Km(uM)' = 27; column 'kcat(min-1)' = 1020; column 'kcat/Km(uM-1 min1)' = 38.

normalized_value_unit_evidence: Km: printed Table 5 cell 27 uM; 27 / 1000 = 0.027 mM; the exported value is 0.00000001105833 mM. kcat: printed Table 5 cell 1020 min^-1; 1020 / 60 = 17.0 s^(-1); the exported value is 17.0 s^(-1). kcat/Km: printed Table 5 cell 38 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 38 x 1000 / 60 = 633.3333333333334 s^-1 mM^-1; the catalog carries no catalytic-efficiency value for this row, so the printed cell is kept as paper evidence only.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-1', substrate row 'pNPA': Km = 27 uM; kcat = 1020 min^-1; printed kcat/Km = 38 uM^-1 min^-1.

table_label: Table 5: Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates (Arch Biochem Biophys 2006;445(1):115-123)

enzyme: carboxylesterase

substrate: p-Nitrophenyl acetate; H2O


proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant p.Asp260fs


sequence_source: UniProtKB:P23141 with direct G143E substitution reconstruction

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant p.Gly143Glu


organism: Lactobacillus casei

substrate_name: H2O; p-Nitrophenyl acetate

substrate: H2O; p-Nitrophenyl acetate


organism: Lactococcus lactis subsp. cremoris


substrate_name: Tripropionin; H2O

substrate: Tripropionin; H2O


substrate_name: H2O; 1-R,S-cis-Permethrin

substrate: H2O; 1-R,S-cis-Permethrin


substrate_name: p-Nitrophenyl butyrate; H2O

substrate: p-Nitrophenyl butyrate; H2O


organism: Actinidia eriantha

substrate_name: H2O; 4-Methylumbelliferyl acetate

sequence_source: UniProtKB:Q0ZPV7 direct accession lookup

substrate: H2O; 4-Methylumbelliferyl acetate


organism: Alicyclobacillus acidocaldarius

substrate_name: p-Nitrophenyl dodecanoate; H2O

sequence_source: UniProtKB:Q7M0L6 checked; 19-residue accession cannot validate residue-numbered variant

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant M211S/R215L

substrate: p-Nitrophenyl dodecanoate; H2O


substrate_name: H2O; p-Nitrophenyl dodecanoate

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant M211S

substrate: H2O; p-Nitrophenyl dodecanoate


proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant R215L


sequence_source: UniProtKB:Q7M0L6 checked; 19-residue accession not accepted as full enzyme sequence


substrate_name: Triacetin; H2O

sequence_source: UniProtKB:Q7SIG1 direct accession lookup

substrate: Triacetin; H2O


organism: Arabidopsis thaliana

substrate_name: H2O; Methyl indole-3-acetate

sequence_source: UniProtKB:Q9SG92 direct accession lookup

substrate: H2O; Methyl indole-3-acetate


organism: Archaeoglobus fulgidus

sequence_source: UniProtKB:O28558 direct accession lookup


substrate_name: H2O; p-Nitrophenyl butyrate

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant chimer EstA-EstP

substrate: H2O; p-Nitrophenyl butyrate


proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant chimer EstP-EstA


organism: Rattus norvegicus

substrate_name: H2O; All-trans-Retinyl palmitate

substrate: H2O; All-trans-Retinyl palmitate


organism: Rhizomucor miehei


organism: Sus scrofa

substrate_name: H2O; 5'-L-Phenylalanyl-floxuridine

substrate: H2O; 5'-L-Phenylalanyl-floxuridine


organism: Thermomyces lanuginosus


organism: Aspergillus niger

sequence_source: UniProtKB accession Q6ED33 direct REST lookup


organism: Bacillus sp.

sequence_source: UniProtKB accession Q6DV85 direct REST lookup


sequence_source: UniProtKB accession Q6DV84 direct REST lookup


organism: Bacillus subtilis


organism: Cavia porcellus


organism: Escherichia coli


organism: Felis silvestris catus

sequence_source: UniProtKB accession Q8I034 direct REST lookup


organism: Geobacillus stearothermophilus

substrate_name: H2O; p-Nitrophenyl caproate

sequence_source: UniProtKB accession Q06174 direct REST lookup

substrate: H2O; p-Nitrophenyl caproate


substrate_name: p-Nitrophenyl caproate; H2O

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant M211V

substrate: p-Nitrophenyl caproate; H2O


substrate_name: p-Nitrophenyl octanoate; H2O

substrate: p-Nitrophenyl octanoate; H2O


proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant M211T


substrate_name: H2O; p-Nitrophenyl octanoate

substrate: H2O; p-Nitrophenyl octanoate


organism: Geobacillus thermoleovorans

substrate_name: p-Nitrophenyl laurate; H2O

unit: moldivs

substrate: p-Nitrophenyl laurate; H2O


organism: Homo sapiens

substrate_name: Irinotecan; H2O

substrate: Irinotecan; H2O


substrate_name: H2O; Irinotecan

substrate: H2O; Irinotecan


substrate_name: Capecitabine; H2O

substrate: Capecitabine; H2O


substrate_name: H2O; Tripropionin

substrate: H2O; Tripropionin


substrate_name: p-Nitrophenyl acetate; H2O

substrate: p-Nitrophenyl acetate; H2O


organism: Salmo salar

substrate_name: H2O; Trioleoylglycerol

substrate: H2O; Trioleoylglycerol