sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A251 plus row mutation W169F reconstructed after offset check against RCSB 4XS6/PDB numbering. and applied mutation signature W169F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W169F, at pH 8.5, temperature not specified in the publication


enzyme_display_name: NADH-dependent peroxiredoxin

organism: Salmonella enterica subsp. enterica serovar Typhimurium

source_db: brenda

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB reviewed accession P0A251 plus row mutation T43S reconstructed after offset check against RCSB 4XS6/PDB numbering.

sequence_variant_note: Mutation signature T43S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

smiles: OO

mutation_type: substitution

proof_lines: mutant enzyme T43S, at pH 8.5, temperature not specified in the publication

data_origin: experimental

enzyme: NADH-dependent peroxiredoxin

source: brenda


mutation_signature: Unknown

sequence_source: UniProtKB reviewed accession P0A251.

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

proof_lines: wild type enzyme, at pH 8.5, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession P0A251 plus row mutation T43V reconstructed after offset check against RCSB 4XS6/PDB numbering.

sequence_variant_note: Mutation signature T43V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme T43V, at pH 8.5, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession P0A251 plus row mutation E49Q reconstructed after offset check against RCSB 4XS6/PDB numbering.

sequence_variant_note: Mutation signature E49Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme E49Q, at pH 8.5, temperature not specified in the publication


enzyme_display_name: inositol-polyphosphate 5-phosphatase

organism: Bos taurus

substrate_name: H2O; D-myo-Inositol 1,4,5-trisphosphate

kcat_over_km_display: Not reported

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

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

proof_lines:
37°C
particulate enzyme
pH 7.4, 37°C

enzyme: inositol-polyphosphate 5-phosphatase

substrate: H2O; D-myo-Inositol 1,4,5-trisphosphate


organism: Arabidopsis thaliana

substrate_name: D-myo-Inositol 1,4,5-trisphosphate; H2O

kcat_display: Not reported

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

sequence_source: UniProtKB reviewed accession O80560 (IP5PC_ARATH) via rest.uniprot.org

substrate: D-myo-Inositol 1,4,5-trisphosphate; H2O


sequence_source: UniProtKB reviewed accession Q9SKB7 (IP5PE_ARATH) via rest.uniprot.org


sequence_source: UniProtKB reviewed accession Q9SYK4 (IP5PD_ARATH) via rest.uniprot.org


organism: Canis lupus familiaris

sequence_source: UniProtKB reviewed accession Q29467 (I5P1_CANLF) via rest.uniprot.org


enzyme_display_name: cathepsin G

organism: Oryctolagus cuniculus

substrate_name: succinyl-Ala-Ala-Pro-Leu-p-nitroanilide

enzyme: cathepsin G

substrate: succinyl-Ala-Ala-Pro-Leu-p-nitroanilide


organism: Rattus norvegicus

sequence_source: UniProtKB:P17977 reviewed exact EC+organism lookup


enzyme_display_name: meprin B

organism: Mus musculus

substrate_name: glucagon

sequence_source: UniProtKB:Q61847 reviewed exact EC+organism lookup

enzyme: meprin B

substrate: glucagon


substrate_name: alpha-MSH

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q61847 canonical sequence with K185Y reconstructed by direct residue substitution and applied mutation signature K185Y to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 37°C, mutant K185Y
pH 7.5, 37°C, 500 mM NaCl, mutant K185Y
pH 7.5, 37°C, 150 mM NaCl, mutant K185Y

substrate: alpha-MSH


substrate_name: villin

sequence_source: UniProtKB:P28826 reviewed exact EC+organism lookup

substrate: villin


organism: Homo sapiens

verification_status: verified

sequence_source: UniProtKB reviewed accession P55212 (CASP6_HUMAN) from direct exact EC 3.4.22.59 plus Homo sapiens lookup.

column_label: Table II; row/segment Caspase-6; metric/detail Ac-VEID-pNA Km; raw 30 micromolar; normalized 0.03 mM.

raw_value_unit_evidence: Table II; Caspase-6; Ac-VEID-pNA Km: 30 micromolar.

table_label: Table II

status: verified


sequence_source: UniProtKB:P55212 direct REST lookup on 2026-06-18

proof_lines: in 50 mM HEPES (pH 7.0), 25 mM MgSO4, 0.5 mM EGTA, 5 mM glutathione, 0.01% (v/v) Triton X-100 containing 0.1% (w/v) bovine gamma-globulin, at 22°C


substrate_name: Lamin A; H2O

substrate: Lamin A; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P55212 direct REST lookup on 2026-06-18 and applied mutation signature K36A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K36A, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P55212 direct REST lookup on 2026-06-18 and applied mutation signature H287A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H287A, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C


source_db: oed

verification_status: unverified

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB:P55212 direct REST lookup on 2026-06-18 and applied mutation signature E244A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E244A, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C


proof_lines: wild type enzyme, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P55212 direct REST lookup on 2026-06-18 and applied mutation signature E244A/H287A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E244A/H287A, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P55212 direct REST lookup on 2026-06-18 and applied mutation signature R44K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P55212 direct REST lookup on 2026-06-18 and applied mutation signature R42A/R43A/R44A to reconstruct the assayed variant sequence.


proof_lines: pH 7.5, 37°C, mutant enzyme R42A/R43A/R44A


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from UniProt P55212 canonical sequence reconstructed with selected mutation signature and applied mutation signature A34E to reconstruct the assayed variant sequence.

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProt P55212 canonical sequence reconstructed with selected mutation signature and applied mutation signature E35K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P55212 canonical sequence reconstructed with selected mutation signature and applied mutation signature A109T to reconstruct the assayed variant sequence.


sequence_source: UniProt P55212 canonical sequence reconstructed with selected mutation signature


sequence_variant_note: Resolved canonical sequence from UniProt P55212 canonical sequence reconstructed with selected mutation signature and applied mutation signature L200A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P55212 canonical sequence reconstructed with selected mutation signature and applied mutation signature T182S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P55212 canonical sequence reconstructed with selected mutation signature and applied mutation signature K284A to reconstruct the assayed variant sequence.


enzyme_display_name: NADH peroxidase

organism: Enterococcus faecalis

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:P37062 direct FASTA check 2026-06-18 and applied mutation signature H10A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 278.15 K; cofactor NADH

enzyme: NADH peroxidase


enzyme_display_name: D-histidine 2-aminobutanoyltransferase

organism: Staphylococcus aureus

substrate_name: D-histidine

source_license: CC BY 4.0; CC BY-NC-ND 4.0

sequence_source: UniProtKB:A0A0H3JXA8 direct REST/FASTA check 2026-06-18

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

proof_lines: pH 8.0, 22°C, recombinant His-tagged enzyme

source_databases_merged: brenda skid

enzyme: D-histidine 2-aminobutanoyltransferase

substrate: D-histidine


substrate_name: NADH; H2O2

assay_conditions_summary: cofactor NADH

substrate: NADH; H2O2


organism: Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)

substrate_name: beta-HBP (at pH 7.5 and 25 degrees Celsius)

source_db: uniprot

proof_lines: kcat is 22 sec(-1) and 5.9 sec(-1) with beta-HBP and alpha-HBP as substrate, respectively. Thus, the enzyme displays 150-fold more efficiency towards the beta- than the alpha-anomer (PubMed:20050615).

source: uniprot


organism: Escherichia coli (strain K12)

proof_lines: kcat is 35.7 sec(-1) and 4.6 sec(-1) with beta-HBP and alpha-HBP as substrate, respectively. Thus, the enzyme displays 100-fold more efficiency towards the beta- than the alpha-anomer (PubMed:20050615, PubMed:31449400). kcat is 0.51 sec(-1)

substrate: beta-HBP (at pH 7.5 and 25 degrees Celsius)


organism: Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)

proof_lines: kcat is 18 sec(-1) and 4.4 sec(-1) with beta-HBP and alpha-HBP as substrate, respectively. Thus, the enzyme displays 18-fold more efficiency towards the beta- than the alpha-anomer (PubMed:20050615).


substrate_name: a DEVD peptide

proof_lines: kcat is 0.51 sec(-1) for a DEVD peptide.

substrate: a DEVD peptide


sequence_variant_note: Resolved canonical sequence from UniProt P55210 REST/FASTA direct check plus selected source accession evidence and applied mutation signature S37A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P55210 REST/FASTA direct check plus selected source accession evidence and applied mutation signature K38A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P55210 REST/FASTA direct check plus selected source accession evidence and applied mutation signature D23A to reconstruct the assayed variant sequence.


sequence_source: UniProt P55210 REST/FASTA direct check plus selected source accession evidence

proof_lines: mutant enzyme S37A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C


proof_lines: mutant enzyme K38A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt P55210 REST/FASTA direct check plus selected source accession evidence and applied mutation signature K41A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K41A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C


proof_lines: wild type enzyme, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C

proof_lines: wild-type, pH not specified in the publication, temperature not specified in the publication

proof_lines: wild-type, value above 0.2 mM, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P55210 REST/FASTA direct check plus selected source accession evidence and applied mutation signature Y230V/W232Y/S234V/Q276D to reconstruct the assayed variant sequence.

proof_lines: Y230V/W232Y/S234V/Q276D, pH not specified in the publication, temperature not specified in the publication


proof_lines: pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt REST P55210 canonical sequence reconstructed with selected mutation signature K39A and applied mutation signature K39A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K39A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C


sequence_source: UniProt REST P55210 reviewed canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProt REST P55210 canonical sequence reconstructed with selected mutation signature K40A and applied mutation signature K40A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P55210 canonical sequence reconstructed with selected mutation signature D23A and applied mutation signature D23A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D23A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt REST P55210 canonical sequence reconstructed with selected mutation signature K41A and applied mutation signature K41A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST P55210 canonical sequence reconstructed with selected mutation signature K39A


sequence_source: UniProt REST P55210 canonical sequence reconstructed with selected mutation signature K40A

proof_lines: mutant enzyme K40A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P20933_fasta_and_sabio_rk_mutation:T257S and applied mutation signature T257S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant Thr257Ser


organism: Leptopilina heterotoma

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication, recombinant enzyme


enzyme_display_name: CoA-disulfide reductase

organism: Pyrococcus horikoshii

substrate_name: NADH; NADPH

sequence_variant_note: Resolved canonical sequence from UniProtKB:O58308 plus Y65A/Y66A/P67G/H367G reconstruction and applied mutation signature Y65A/Y66A/P67G/H367G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 348.15 K; cofactor NADPH

proof_lines: pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G

enzyme: CoA-disulfide reductase

substrate: NADH; NADPH


substrate_name: CoA-disulfide

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

substrate: CoA-disulfide


substrate_name: CoA-disulfide; H+; NADPH; CoA-disulfide; H+; NADPH; NADP+; Coenzyme A; CoA-disulfide; H+; NADH; NADH; NAD+; H+; NADPH; CoA-disulfide; NADPH; CoA-disulfide; H+; H+; 3'-Dephospho-CoA-disulfide; NADPH

assay_conditions_summary: cofactor CoA


assay_conditions_summary: 296.15 K; cofactor CoA

proof_lines: wild type enzyme, at 23°C, pH not specified in the publication

proof_lines: wild type enzyme, at 37°C, pH not specified in the publication


substrate_name: methyl methanethiolsulfonate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q2FIA5 plus Y419F reconstruction and applied mutation signature Y419F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y419F, at 23°C, pH not specified in the publication

substrate: methyl methanethiolsulfonate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q2FIA5 plus Y361F reconstruction and applied mutation signature Y361F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y361F, at 23°C, pH not specified in the publication


substrate_name: NADPH

assay_conditions_summary: pH 7.8; 310.15 K; cofactor NADPH

substrate: NADPH


substrate_name: CoA-glutathione

assay_conditions_summary: pH 7.8; 310.15 K; cofactor CoA

substrate: CoA-glutathione


organism: Thermus thermophilus

substrate_name: NADH; CoA-disulfide

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

assay_conditions_summary: pH 7.5; 315.15 K; cofactor NADH

proof_lines:
pH 7.5, 42°C
Raw SKiD Env: Temp=42°C, pH=7.5

substrate: NADH; CoA-disulfide


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9BXR0 plus V161C reconstruction and applied mutation signature V161C to reconstruct the assayed variant sequence.


substrate_name: queuine

substrate: queuine


sequence_source: UniProtKB:Q9BXR0 plus V161C reconstruction


substrate_name: queuine; 7-aminomethyl-7-carbaguanine

proof_lines:
pH 7.3, 37°C, wild-type
pH 7.3, 37°C, wild-type enzyme

substrate: queuine; 7-aminomethyl-7-carbaguanine


substrate_name: guanine34 in tRNAAsp; queuine

proof_lines:
at pH 7.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.3

substrate: guanine34 in tRNAAsp; queuine


enzyme_display_name: 3-hydroxybenzoate 6-monooxygenase

organism: Aquipseudomonas alcaligenes

sequence_source: UniProtKB:Q9F131 direct accession lookup

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

assay_conditions_summary: pH 7.5; 296.15 K; cofactor NADPH

proof_lines: pH 7.5, 23°C, recombinant enzyme, cofactor NADH

proof_lines: pH 7.5, 23°C, recombinant enzyme, cofactor NADPH

enzyme: 3-hydroxybenzoate 6-monooxygenase


organism: Corynebacterium glutamicum

sequence_source: UniProtKB:Q8NLB6 direct accession lookup

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: recombinant enzyme, with NADH, pH 7.5, 25°C


organism: Rhodococcus jostii

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0SFK6 direct accession lookup and applied mutation signature Y105F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q0SFK6 direct accession lookup

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


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines: pH 8, 25°C, enzyme immobilized onto surface-functionalized electrospun polycaprolactone (PCL) fibers


organism: Bacillus anthracis

substrate_name: H+; CoA-disulfide; NADH

sequence_source: UniProtKB:A0A6L7H7X4 direct accession lookup from source accession Q81UT5

assay_conditions_summary: cofactor NADP+

substrate: H+; CoA-disulfide; NADH


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


substrate_name: CoA-disulfide; H+; NADH

km_display: Not reported

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: CoA-disulfide reductase(Enzyme) mutant Y425F

substrate: CoA-disulfide; H+; NADH


substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: NADH; H+; CoA-disulfide

proof_lines: SABIO-RK modifier species: CoA-disulfide reductase(Enzyme) mutant Y367F

substrate: NADH; H+; CoA-disulfide


sequence_source: UniProtKB:O58308 direct accession lookup

assay_conditions_summary: pH 7.5; 348.15 K; cofactor CoA


assay_conditions_summary: pH 7.5; 348.15 K; cofactor NADH


proof_lines: pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, wild-type enzyme

proof_lines: pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, mutant enzyme Y65A/Y66A/P67G/H367G


sequence_source: UniProtKB reviewed accession Q9JMA2 direct lookup; selected BRENDA source supplied Q9JMA2.

proof_lines: recombinant enzyme whose subunits are produced separately and combined in a molar ratio of 1:1 for kinetic measurements, pH and temperature not specified in the publication


organism: Zymomonas mobilis

substrate_name: guanine34 in tRNA

substrate: guanine34 in tRNA


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


enzyme_display_name: N(4)-acetylcytidine amidohydrolase

organism: Escherichia coli

sequence_source: UniProtKB reviewed accession P67603 direct lookup; selected source supplied P67603.

enzyme: N(4)-acetylcytidine amidohydrolase


assay_conditions_summary: pH 8; 295.15 K; buffer 50 mM potassium phosphate

column_label: Table 2 (Catalytic parameters of YqfB with a C-terminal His6 tag), substrate row '7' = N4-isobutyryl-2′-deoxycytidine; column 'Km (M)' = (1.9 ± 0.08) × 10^-3; column 'kcat (s-1)' = 75 ± 3; column 'Ki (M)' = (1.60 ± 0.02) × 10^-3; column 'kcat/Km (M−1 s−1)' = (3.75 ± 0.06) × 10^4

normalized_value_unit_evidence: Km: printed Table 2 cell 1.9 x 10^-3 M; 1 M is 1000 mM, so 1.9 x 10^-3 x 1000 = 1.9 mM; the exported value is 1.9 mM. kcat: printed Table 2 cell 75 s^-1; already in s^-1, no conversion; the exported value is 75.0 s^(-1). kcat/Km: printed Table 2 cell 3.75 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.75 x 10^4 / 1000 = 37.5 s^-1 mM^-1; the exported kcat_over_km 39.473684210526315 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (75.0 / 1.9), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 2, Table 2 body row for substrate 7 (N4-isobutyryl-2′-deoxycytidine), YqfB with a C-terminal His6 tag: Km = 1.9 x 10^-3 M; kcat = 75 s^-1; printed kcat/Km = 3.75 x 10^4 M^-1 s^-1.

table_label: Table 2: Catalytic parameters of YqfB with a C-terminal His6 tag (Scientific Reports 2020)


column_label: Table 2 (Catalytic parameters of YqfB with a C-terminal His6 tag), substrate row '2' = N4-acetyl-5-fluorocytosine; column 'Km (M)' = (2.1 ± 0.2) × 10^-3; column 'kcat (s-1)' = 90 ± 7; column 'Ki (M)' = (4 ± 4) × 10^-3; column 'kcat/Km (M−1 s−1)' = (4.0 ± 0.3) × 10^4

normalized_value_unit_evidence: Km: printed Table 2 cell 2.1 x 10^-3 M; 1 M is 1000 mM, so 2.1 x 10^-3 x 1000 = 2.1 mM; the exported value is 2.1 mM. kcat: printed Table 2 cell 90 s^-1; already in s^-1, no conversion; the exported value is 90.0 s^(-1). kcat/Km: printed Table 2 cell 4.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.0 x 10^4 / 1000 = 40.0 s^-1 mM^-1; the exported kcat_over_km 42.857142857142854 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (90.0 / 2.1), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 2, Table 2 body row for substrate 2 (N4-acetyl-5-fluorocytosine), YqfB with a C-terminal His6 tag: Km = 2.1 x 10^-3 M; kcat = 90 s^-1; printed kcat/Km = 4.0 x 10^4 M^-1 s^-1.


column_label: Table 2 (Catalytic parameters of YqfB with a C-terminal His6 tag), substrate row '6' = N4-acetyl-2′-deoxycytidine; column 'Km (M)' = (4.00 ± 0.04) × 10^-4; column 'kcat (s-1)' = 101 ± 1; column 'Ki (M)' = N.D.; column 'kcat/Km (M−1 s−1)' = (2.30 ± 0.02) × 10^5

normalized_value_unit_evidence: Km: printed Table 2 cell 4.00 x 10^-4 M; 1 M is 1000 mM, so 4.00 x 10^-4 x 1000 = 0.4 mM; the exported value is 0.4 mM. kcat: printed Table 2 cell 101 s^-1; already in s^-1, no conversion; the exported value is 101.0 s^(-1). kcat/Km: printed Table 2 cell 2.30 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.30 x 10^5 / 1000 = 230.0 s^-1 mM^-1; the exported kcat_over_km 252.5 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (101.0 / 0.4), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 2, Table 2 body row for substrate 6 (N4-acetyl-2′-deoxycytidine), YqfB with a C-terminal His6 tag: Km = 4.00 x 10^-4 M; kcat = 101 s^-1; printed kcat/Km = 2.30 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P67603 canonical sequence and selected source mutation E74A. and applied mutation signature E74A to reconstruct the assayed variant sequence.


substrate_name: capecitabine

column_label: Table 2 (Catalytic parameters of YqfB with a C-terminal His6 tag), substrate row '28' = Capecitabine; column 'Km (M)' = (7.0 ± 0.2) × 10^-4; column 'kcat (s-1)' = 0.016 ± 0.003; column 'Ki (M)' = N.D.; column 'kcat/Km (M−1 s−1)' = 22 ± 0.1

normalized_value_unit_evidence: Km: printed Table 2 cell 7.0 x 10^-4 M; 1 M is 1000 mM, so 7.0 x 10^-4 x 1000 = 0.7 mM; the exported value is 0.7 mM. kcat: printed Table 2 cell 0.016 s^-1; already in s^-1, no conversion; the exported value is 0.016 s^(-1). kcat/Km: printed Table 2 cell 22 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 22 / 1000 = 0.022 s^-1 mM^-1; the exported kcat_over_km 0.02285714285714286 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (0.016 / 0.7), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 2, Table 2 body row for substrate 28 (Capecitabine), YqfB with a C-terminal His6 tag: Km = 7.0 x 10^-4 M; kcat = 0.016 s^-1; printed kcat/Km = 22 M^-1 s^-1.

substrate: capecitabine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P67603 and applied mutation signature H70A to reconstruct the assayed variant sequence.

column_label: Table 3 (Rate constants for YqfB mutants), YqfB row 'H70A' with substrate row '3' = N4-acetylcytidine; column 'Km (M)' = (5.0 ± 0.02) × 10^-5; column 'kcat (s−1)' = 23 ± 0.029; column 'Ki (M)' = (2.0 ± 0.01) × 10^-4; column 'kcat/Km (M−1 s−1)' = (4.0 ± 0.02) × 10^5

normalized_value_unit_evidence: Km: printed Table 3 cell 5.0 x 10^-5 M; 1 M is 1000 mM, so 5.0 x 10^-5 x 1000 = 0.05 mM; the exported value is 0.05 mM. kcat: printed Table 3 cell 23 s^-1; already in s^-1, no conversion; the exported value is 23.0 s^(-1). kcat/Km: printed Table 3 cell 4.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.0 x 10^5 / 1000 = 400.0 s^-1 mM^-1; the exported kcat_over_km 460.0 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (23.0 / 0.05), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, Table 3 body row for YqfB H70A with substrate 3 (N4-acetylcytidine): Km = 5.0 x 10^-5 M; kcat = 23 s^-1; printed kcat/Km = 4.0 x 10^5 M^-1 s^-1.

table_label: Table 3: Rate constants for YqfB mutants (Scientific Reports 2020)


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P67603 canonical sequence and selected source mutation Y89A. and applied mutation signature Y89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P67603 and applied mutation signature E74A to reconstruct the assayed variant sequence.

column_label: Table 3 (Rate constants for YqfB mutants), YqfB row 'E74A' with substrate row '1' = N4-acetylcytosine; column 'Km (M)' = (3.0 ± 0.02) × 10^-4; column 'kcat (s−1)' = 0.22 ± 0.001; column 'Ki (M)' = N.D.; column 'kcat/Km (M−1 s−1)' = (7.0 ± 0.04) × 10^2

normalized_value_unit_evidence: Km: printed Table 3 cell 3.0 x 10^-4 M; 1 M is 1000 mM, so 3.0 x 10^-4 x 1000 = 0.3 mM; the exported value is 0.3 mM. kcat: printed Table 3 cell 0.22 s^-1; already in s^-1, no conversion; the exported value is 0.22 s^(-1). kcat/Km: printed Table 3 cell 7.0 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.0 x 10^2 / 1000 = 0.7000000000000001 s^-1 mM^-1; the exported kcat_over_km 0.7333333333333334 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (0.22 / 0.3), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, Table 3 body row for YqfB E74A with substrate 1 (N4-acetylcytosine): Km = 3.0 x 10^-4 M; kcat = 0.22 s^-1; printed kcat/Km = 7.0 x 10^2 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P67603 and applied mutation signature D27A to reconstruct the assayed variant sequence.

column_label: Table 3 (Rate constants for YqfB mutants), YqfB row 'D27A' with substrate row '3' = N4-acetylcytidine; column 'Km (M)' = (2.9 ± 0.11) × 10^-4; column 'kcat (s−1)' = 300 ± 16.; column 'Ki (M)' = (4.0 ± 0.2) × 10^-4; column 'kcat/Km (M−1 s−1)' = (1.2 ± 0.01) × 10^6

normalized_value_unit_evidence: Km: printed Table 3 cell 2.9 x 10^-4 M; 1 M is 1000 mM, so 2.9 x 10^-4 x 1000 = 0.29 mM; the exported value is 0.29 mM. kcat: printed Table 3 cell 300 s^-1; already in s^-1, no conversion; the exported value is 300.0 s^(-1). kcat/Km: printed Table 3 cell 1.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^6 / 1000 = 1200.0 s^-1 mM^-1; the exported kcat_over_km 1034.4827586206898 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (300.0 / 0.29), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, Table 3 body row for YqfB D27A with substrate 3 (N4-acetylcytidine): Km = 2.9 x 10^-4 M; kcat = 300 s^-1; printed kcat/Km = 1.2 x 10^6 M^-1 s^-1.


proof_lines: recombinant C-terminally His6-tagged enzyme, at pH 8.0 and 22°C

proof_lines: recombinant N-terminally His6-tagged enzyme, at pH 8.0 and 22°C


substrate_name: 3-hydroxybenzoate (with NAD as cosubstrate)

assay_conditions_summary: cofactor NADPH


organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)


organism: Polaromonas naphthalenivorans (strain CJ2)


organism: Rattus norvegicus


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

proof_lines: kcat is 1.11 sec(-1) with CoA persulfide as substrate (in the presence of NADH). kcat is 1.50 sec(-1) with CoA persulfide as substrate (in the presence of NADPH). kcat is 1.07 sec(-1) with NADH as substrate (in the presence of CoA persulfid


organism: Homo sapiens

substrate_name: tRNA(Tyr)

proof_lines: kcat is 0.0056 sec(-1) with tRNA(Tyr) as substrate and 0.00586 sec(-1) with guanine as substrate.

substrate: tRNA(Tyr)


organism: Mus musculus

proof_lines: kcat is 0.0065 sec(-1) with tRNA(Tyr) as substrate.


organism: Escherichia coli (strain K12)

column_label: Table 2 (Catalytic parameters of YqfB with a C-terminal His6 tag), substrate row '3' = N4-acetylcytidine; column 'Km (M)' = (6.2 ± 0.1) × 10^-5; column 'kcat (s-1)' = 157 ± 1; column 'Ki (M)' = (1.3 ± 0.2) × 10^-4; column 'kcat/Km (M−1 s−1)' = (2.2 ± 0.1) × 10^6

normalized_value_unit_evidence: Km: printed Table 2 cell 6.2 x 10^-5 M; 1 M is 1000 mM, so 6.2 x 10^-5 x 1000 = 0.062 mM; the exported value is 0.062 mM. kcat: printed Table 2 cell 157 s^-1; already in s^-1, no conversion; the exported value is 157.0 s^(-1). kcat/Km: printed Table 2 cell 2.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.2 x 10^6 / 1000 = 2200.0 s^-1 mM^-1; the export carries no kcat_over_km field for this row, so the printed cell is recorded as evidence only and no ratio is written.

raw_value_unit_evidence: Table 2, Table 2 body row for substrate 3 (N4-acetylcytidine), YqfB with a C-terminal His6 tag: Km = 6.2 x 10^-5 M; kcat = 157 s^-1; printed kcat/Km = 2.2 x 10^6 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P67603 canonical sequence and selected source mutation H70A and applied mutation signature H70A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P67603 and applied mutation signature Y89A to reconstruct the assayed variant sequence.

column_label: Table 3 (Rate constants for YqfB mutants), YqfB row 'Y89A' with substrate row '3' = N4-acetylcytidine; column 'Km (M)' = (2.2 ± 0.06) × 10^-3; column 'kcat (s−1)' = 40 ± 1.3; column 'Ki (M)' = N.D.; column 'kcat/Km (M−1 s−1)' = (1.9 ± 0.09) × 10^4

normalized_value_unit_evidence: Km: printed Table 3 cell 2.2 x 10^-3 M; 1 M is 1000 mM, so 2.2 x 10^-3 x 1000 = 2.2 mM; the exported value is 2.2 mM. kcat: printed Table 3 cell 40 s^-1; already in s^-1, no conversion; the exported value is 40.0 s^(-1). kcat/Km: printed Table 3 cell 1.9 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^4 / 1000 = 19.0 s^-1 mM^-1; the exported kcat_over_km 18.18181818181818 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (40.0 / 2.2), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, Table 3 body row for YqfB Y89A with substrate 3 (N4-acetylcytidine): Km = 2.2 x 10^-3 M; kcat = 40 s^-1; printed kcat/Km = 1.9 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P67603 canonical sequence and selected source mutation D27A and applied mutation signature D27A to reconstruct the assayed variant sequence.


column_label: Table 3 (Rate constants for YqfB mutants), YqfB row 'E74A' with substrate row '3' = N4-acetylcytidine; column 'Km (M)' = (2.0 ± 0.03) × 10^-6; column 'kcat (s−1)' = (7.0 ± 0.06) × 10^-2; column 'Ki (M)' = (3.0 ± 2.8) × 10^-7; column 'kcat/Km (M−1 s−1)' = (3.0 ± 0.05) × 10^4

normalized_value_unit_evidence: Km: printed Table 3 cell 2.0 x 10^-6 M; 1 M is 1000 mM, so 2.0 x 10^-6 x 1000 = 0.002 mM; the exported value is 0.002 mM. kcat: printed Table 3 cell 7.0 x 10^-2 s^-1; already in s^-1, no conversion; the exported value is 0.07 s^(-1). kcat/Km: printed Table 3 cell 3.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.0 x 10^4 / 1000 = 30.0 s^-1 mM^-1; the exported kcat_over_km 35.0 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (0.07 / 0.002), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, Table 3 body row for YqfB E74A with substrate 3 (N4-acetylcytidine): Km = 2.0 x 10^-6 M; kcat = 7.0 x 10^-2 s^-1; printed kcat/Km = 3.0 x 10^4 M^-1 s^-1.


sequence_source: UniProtKB P67603 direct REST check


column_label: Table 2: Catalytic parameters of YqfB with a C-terminal His6 tag. Substrate row '3a' (compound 3 = N4-acetylcytidine; footnote a: the recombinant wild-type YqfB); column 'Km (M)' = 7.0 x 10^-5; column 'kcat (s-1)' = 196; column 'Ki (M)' = 7.7 x 10^-5; column 'kcat/Km (M-1 s-1)' = 2.8 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 7.0 x 10^-5 M; 1 M = 1000 mM, so 7.0 x 10^-5 M = 0.07 mM, which is the exported value. kcat: printed Table 2 cell 196 s^-1; already in s^-1, no conversion; the exported value is 196.0 s^(-1). kcat/Km: printed Table 2 cell 2.8 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the cell is 2800.0 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Table 2, substrate row '3a' (compound 3 = N4-acetylcytidine; footnote a: the recombinant wild-type YqfB): Km = 7.0 x 10^-5 M; kcat = 196 s^-1; Ki = 7.7 x 10^-5 M; printed kcat/Km = 2.8 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row 3a (compound 3 = N4-acetylcytidine), footnote a: the recombinant wild-type YqfB


organism: Asobara tabida

sequence_source: UniProtKB D0V0N4 direct REST check

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication, recombinant enzyme


sequence_source: UniProtKB P20933 direct REST check


proof_lines: recombinant wild-type enzyme, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P20933 canonical sequence and selected source mutation S72A and applied mutation signature S72A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant Ser72Ala


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P20933 canonical sequence and selected source mutation T224S and applied mutation signature T224S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: N4-(beta-N-acetylglucosaminyl)-L-asparaginase(Enzyme) mutant Thr224Ser


enzyme_display_name: 2-isopropylmalate synthase

organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WQB3 and applied mutation signature R97A to reconstruct the assayed variant sequence.

smiles: CC(C)C(=O)C(=O)O

enzyme: 2-isopropylmalate synthase


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WQB3 and applied mutation signature D444A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WQB3 and applied mutation signature D444Y to reconstruct the assayed variant sequence.


organism: Neisseria meningitidis

substrate_name: pyruvate

proof_lines: apparent value, full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C

substrate: pyruvate


organism: Solanum lycopersicum

proof_lines: isoform IPMS3, pH and temperature not specified in the publication


proof_lines: isoform IPMS1, pH and temperature not specified in the publication


organism: Thermus thermophilus

substrate_name: acetyl-CoA

assay_conditions_summary: pH 8; 323.15 K; cofactor CoA

substrate: acetyl-CoA


enzyme_display_name: methylthioalkylmalate synthase

organism: Arabidopsis thaliana

assay_conditions_summary: pH 8.5; 305.15 K; cofactor CoA

enzyme: methylthioalkylmalate synthase


smiles: CSCCCCCCCC(=O)C(=O)O


smiles: CSCCCCCCC(=O)C(=O)O

assay_conditions_summary: pH 8; 305.15 K; cofactor CoA

column_label: Table III (Kinetic parameters for various 2-oxo acids with recombinant MAM3), substrate row '8-Methylthio-2-oxooctanoic acid (/C7 glucosinolates)'; column 'Km (uM)' = 253; column 'Vmax (nmol min^-1 mg^-1)' = 364; column 'kcat (s^-1)' = 0.3; column 'kcat/Km (M^-1 s^-1)' = 1,280.

normalized_value_unit_evidence: Km: printed Table III cell 253 in the column headed 'Km (uM)'; 253 / 1000 = 0.253 mM; the exported value is 0.253 mM. kcat: printed Table III cell 0.3 in the column headed 'kcat (s^-1)'; s^-1 is already the canonical turnover unit, so no unit conversion applies; the exported value is 0.3 s^(-1). kcat/Km: printed Table III cell 1,280 in the column headed 'kcat/Km (M^-1 s^-1)'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1280 / 1000 = 1.28 s^-1 mM^-1; the exported value is 1.1857707509881423 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, substrate row '8-Methylthio-2-oxooctanoic acid (/C7 glucosinolates)': Km = 253 uM; kcat = 0.3 s^-1; printed kcat/Km = 1,280 M^-1 s^-1.

table_label: Table III. Kinetic parameters for various 2-oxo acids with recombinant MAM3 (Plant Physiology 2007, 144:60-71)


smiles: CC(=O)C(=O)O

column_label: Table III (Kinetic parameters for various 2-oxo acids with recombinant MAM3), substrate row 'Pyruvate'; column 'Km (uM)' = 8,600; column 'Vmax (nmol min^-1 mg^-1)' = 191; column 'kcat (s^-1)' = 0.17; column 'kcat/Km (M^-1 s^-1)' = 23.

normalized_value_unit_evidence: Km: printed Table III cell 8,600 in the column headed 'Km (uM)'; 8600 / 1000 = 8.6 mM; the exported value is 8.6 mM. kcat: printed Table III cell 0.17 in the column headed 'kcat (s^-1)'; s^-1 is already the canonical turnover unit, so no unit conversion applies; the exported value is 0.17 s^(-1). kcat/Km: printed Table III cell 23 in the column headed 'kcat/Km (M^-1 s^-1)'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 23 / 1000 = 0.023 s^-1 mM^-1; the exported value is 0.01976744186046512 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, substrate row 'Pyruvate': Km = 8,600 uM; kcat = 0.17 s^-1; printed kcat/Km = 23 M^-1 s^-1.

row_label: Table III, substrate row 'Pyruvate'


smiles: CSCCCC(=O)C(=O)O


enzyme_display_name: polynucleotide 5'-hydroxyl-kinase

organism: Pyrococcus horikoshii

substrate_name: 5'-OH DNA

sequence_source: UniProtKB:O57936 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot)

enzyme: polynucleotide 5'-hydroxyl-kinase

substrate: 5'-OH DNA


organism: Tequatrovirus T4

sequence_source: UniProtKB:P06855 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot)


enzyme_display_name: fluoroacetyl-CoA thioesterase

organism: Streptantibioticus cattleyicolor

substrate_name: fluoroacetyl-CoA

sequence_source: UniProtKB:Q1EMV2 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot)

assay_conditions_summary: pH 7.6; 298.15 K; cofactor CoA

proof_lines: wild-type, 25°C, pH not specified in the publication

proof_lines: wild type protein, pH not specified in the publication, 25°C

proof_lines: wild type enzyme, with acetyl-CoA as substrate, at pH 7.6, temperature not specified in the publication

enzyme: fluoroacetyl-CoA thioesterase

substrate: fluoroacetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1EMV2 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot) and applied mutation signature E50A to reconstruct the assayed variant sequence.

assay_conditions_summary: 298.15 K; cofactor CoA

proof_lines: mutant E50A, 25°C, pH not specified in the publication

proof_lines: E50A mutant protein, pH not specified in the publication, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1EMV2 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot) and applied mutation signature T42S to reconstruct the assayed variant sequence.

proof_lines: mutant T42S, 25°C, pH not specified in the publication

proof_lines: T42S mutant protein, pH not specified in the publication, 25°C


substrate_name: Unknown

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1EMV2 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot) and applied mutation signature F36A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; cofactor CoA

proof_lines: mutant enzyme F36A, with acetyl-CoA as substrate, at pH 7.6, temperature not specified in the publication

proof_lines: mutant enzyme F36A, with fluoroacetyl-CoA as substrate, at pH 7.6, temperature not specified in the publication

substrate: Unknown


organism: Streptomyces cattleya

source_db: skid

source_license: CC BY-NC-ND 4.0

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

source: skid


organism: Bordetella bronchiseptica

substrate_name: D-fructose 1,6-bisphosphate

sequence_source: UniProtKB:Q7WG29 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot)

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: D-fructose 1,6-bisphosphate


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB:P63228 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot) and applied mutation signature C92A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P63228 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot) and applied mutation signature C107A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P63228 and applied mutation signature K137A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic constants for E. coli GmhB mutant catalyzed hydrolysis of the alpha and/or beta anomer of D-glycerol-D-manno-heptose-1,7-bisphosphate in 50 mM Tris-HCl (pH 7.5, 25 C) containing 1 mM MgCl2), GmhB row 'K137A' with Substrate anomer 'beta'; column 'kcat (sec-1)' = 28.0; column 'Km (uM)' = 39; column 'kcat/Km (M-1 s-1)' = 7 x 10^5. Table 2 carries exactly these three numeric columns.

normalized_value_unit_evidence: kcat: printed Table 2 cell 28.0 sec-1; 1 sec-1 is 1 s^(-1), so no unit conversion applies; the paper value is 28.0 s^(-1). Km: printed Table 2 cell 39 uM; 1 uM is 0.001 mM, so 39 / 1000 = 0.039 mM; the paper value is 0.039 mM. kcat/Km: printed Table 2 cell 7 x 10^5 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 7 x 10^5 / 1000 = 700.0 s^-1 mM^-1; the paper value is 700.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, GmhB row 'K137A', substrate anomer beta: the kcat (sec-1) cell reads 28.0, the Km (uM) cell reads 39, and the printed kcat/Km (M-1 s-1) cell reads 7 x 10^5.

table_label: Table 2: Steady-state kinetic constants for E. coli GmhB mutant catalyzed hydrolysis of the alpha and/or beta anomer of D-glycerol-D-manno-heptose-1,7-bisphosphate in 50 mM Tris-HCl (pH 7.5, 25 C) containing 1 mM MgCl2 (Biochemistry 2010, 49(6):1082-1092)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P63228 and applied mutation signature C109A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic constants for E. coli GmhB mutant catalyzed hydrolysis of the alpha and/or beta anomer of D-glycerol-D-manno-heptose-1,7-bisphosphate in 50 mM Tris-HCl (pH 7.5, 25 C) containing 1 mM MgCl2), GmhB row 'C109A' with Substrate anomer 'beta'; column 'kcat (sec-1)' = 0.34; column 'Km (uM)' = 68; column 'kcat/Km (M-1 s-1)' = 5 x 10^3. Table 2 carries exactly these three numeric columns.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.34 sec-1; 1 sec-1 is 1 s^(-1), so no unit conversion applies; the paper value is 0.34 s^(-1). Km: printed Table 2 cell 68 uM; 1 uM is 0.001 mM, so 68 / 1000 = 0.068 mM; the paper value is 0.068 mM. kcat/Km: printed Table 2 cell 5 x 10^3 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 5 x 10^3 / 1000 = 5.0 s^-1 mM^-1; the paper value is 5.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, GmhB row 'C109A', substrate anomer beta: the kcat (sec-1) cell reads 0.34, the Km (uM) cell reads 68, and the printed kcat/Km (M-1 s-1) cell reads 5 x 10^3.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P63228 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot) and applied mutation signature R110A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P63228 REST direct exact-accession lookup, reviewed=UniProtKB reviewed (Swiss-Prot)


substrate_name: Propanoyl-CoA

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

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

substrate: Propanoyl-CoA


substrate_name: crotonoyl-CoA

substrate: crotonoyl-CoA


smiles: CCC(=O)C(=O)O


substrate_name: alpha-ketoisovalerate

sequence_variant_note: Resolved canonical sequence from UniProtKB P9WQB3 FASTA direct lookup, 2026-06-18 and applied mutation signature Y169F to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor CoA

substrate: alpha-ketoisovalerate


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WQB3 FASTA direct lookup, 2026-06-18 and applied mutation signature Y410F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WQB3 FASTA direct lookup, 2026-06-18 and applied mutation signature E218A to reconstruct the assayed variant sequence.

proof_lines: mutant E218A, enzyme displays substrate activation, unactivated form

proof_lines: mutant E218A, enzyme displays substrate activation, activated form


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WQB3 FASTA direct lookup, 2026-06-18 and applied mutation signature H379A to reconstruct the assayed variant sequence.

proof_lines: mutant H379A, enzyme displays substrate activation, unactivated form

proof_lines: mutant H379A, enzyme displays substrate activation, activated form


sequence_source: UniProtKB P9WQB3 FASTA direct lookup, 2026-06-18


proof_lines:
wild type enzyme, at pH 7.5 and 25°C
wild-type


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WQB3 FASTA direct lookup, 2026-06-18 and applied mutation signature D444A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WQB3 FASTA direct lookup, 2026-06-18 and applied mutation signature D444R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P9WQB3 FASTA direct lookup, 2026-06-18 and applied mutation signature D444Y to reconstruct the assayed variant sequence.


organism: Bifidobacterium longum

substrate_name: galacto-N-biose

sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 direct REST lookup; selected source row exact accession and applied mutation signature V162T to reconstruct the assayed variant sequence.

substrate: galacto-N-biose


sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 direct REST lookup; selected source row exact accession and applied mutation signature P161S/S336A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 direct REST lookup; selected BRENDA source row exact accession and applied mutation signature V162T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:E8MF13 direct REST lookup; selected source row exact accession

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:E8MF13 direct REST lookup; selected BRENDA source row exact accession and applied mutation signature P161S to reconstruct the assayed variant sequence.


substrate_name: lacto-N-biose I

sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 direct REST lookup; selected source row exact accession and applied mutation signature S336A to reconstruct the assayed variant sequence.

substrate: lacto-N-biose I


sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 direct REST lookup; selected BRENDA source row exact accession and applied mutation signature P161S/S336A to reconstruct the assayed variant sequence.


organism: Clostridium perfringens

substrate_name: Phosphate; Lacto-N-biose

sequence_source: UniProtKB:A0A0H2YRA5 direct REST lookup; selected SABIO-RK source row exact accession

substrate: Phosphate; Lacto-N-biose


organism: Cutibacterium acnes


substrate_name: N-acetyl-D-galactosamine

assay_conditions_summary: pH 7; 310.15 K; buffer 100 mM MOPS

substrate: N-acetyl-D-galactosamine


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


organism: Lachnoclostridium phytofermentans

sequence_source: UniProtKB:A9KIW5 direct canonical sequence lookup

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


sequence_source: UniProtKB:A9KQ75 direct canonical sequence lookup


organism: Vibrio vulnificus

sequence_source: UniProtKB:A0A3Q0KZS1 direct accession sequence lookup

proof_lines: with beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine as cosubstrate, in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C

proof_lines: with beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine as cosubstrate, in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C


enzyme_display_name: [myosin light-chain] kinase

organism: Dictyostelium discoideum

substrate_name: myosin

sequence_source: UniProtKB:P25323 direct canonical sequence lookup

proof_lines:
myosin from Dictyostelium
22°C, pH 7.5

enzyme: [myosin light-chain] kinase

substrate: myosin


organism: Gallus gallus

substrate_name: [non-muscle heavy meromyosin IIB]

sequence_source: UniProtKB:P11799 direct canonical sequence lookup

substrate: [non-muscle heavy meromyosin IIB]


organism: Homo sapiens

substrate_name: Myosin light chain; ATP

sequence_source: UniProtKB:Q15746 direct canonical sequence lookup

assay_conditions_summary: cofactor ATP

substrate: Myosin light chain; ATP


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: myosin-light-chain kinase(Enzyme) mutant A1491S N-terminal FLAG-tagged


organism: Mus musculus

sequence_source: UniProtKB:Q3UIZ8 direct canonical sequence lookup


substrate_name: myosin light chain

sequence_source: UniProtKB:Q6PDN3 direct canonical sequence lookup

substrate: myosin light chain


organism: Oryctolagus cuniculus

substrate_name: ATP; Myosin light chain

sequence_source: UniProtKB:P29294 direct canonical sequence lookup

substrate: ATP; Myosin light chain


organism: Acetivibrio thermocellus

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


organism: Bacteriophage T4

substrate_name: 5'-Dephospho-DNA; ATP

proof_lines: SABIO-RK modifier species: polynucleotide 5'-hydroxyl-kinase(Enzyme) mutant pseT 1,47

substrate: 5'-Dephospho-DNA; ATP


substrate_name: ATP; 5'-Dephospho-DNA

sequence_source: UniProtKB:P06855 direct canonical sequence lookup

substrate: ATP; 5'-Dephospho-DNA


organism: Caenorhabditis elegans

sequence_source: UniProtKB:P52874 direct accession sequence lookup

proof_lines: pH and temperature not specified in the publication


organism: Arabidopsis thaliana

sequence_source: UniProtKB REST direct lookup for Q9C550; reviewed entry LEU12_ARATH; canonical sequence length 631.


substrate_name: acetyl-CoA

sequence_source: UniProtKB REST direct lookup for Q9LPR4; reviewed entry LEU11_ARATH; canonical sequence length 631.

substrate: acetyl-CoA


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB REST direct lookup for Q58595; reviewed entry LEU1_METJA; canonical sequence length 518.

assay_conditions_summary: pH 7.8; 310.15 K; cofactor CoA


organism: Mycobacterium tuberculosis


substrate_name: alpha-Ketovaline

substrate: alpha-Ketovaline


substrate_name: Acetyl-CoA

substrate: Acetyl-CoA


substrate_name: K+

substrate: K+


substrate_name: Na+

substrate: Na+


substrate_name: Li+

substrate: Li+


substrate_name: Rb+

substrate: Rb+


substrate_name: alpha-Ketovaline; Acetyl-CoA; H2O

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

sequence_source: UniProtKB REST direct lookup for P9WQB3; reviewed entry LEU1_MYCTU; canonical sequence length 644.

proof_lines: full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C

source_databases_merged: sabio_rk brenda skid

substrate: alpha-Ketovaline; Acetyl-CoA; H2O


sequence_variant_note: Resolved canonical sequence from UniProt:O95989 and applied mutation signature R45A to reconstruct the assayed variant sequence.

proof_lines: mutant R45A, pH 7.2, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt:O95989 and applied mutation signature H42A to reconstruct the assayed variant sequence.

proof_lines: mutant H42A, pH 7.2, temperature not specified in the publication


organism: Saccharomyces cerevisiae


substrate_name: 5-PP-InsP5; H2O

substrate: 5-PP-InsP5; H2O


substrate_name: H2O; 5-PP-InsP5

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) wildtype N-terminal truncated (116-281)

substrate: H2O; 5-PP-InsP5


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature R252A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant R252A


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature R216A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant R216A


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature H219A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant H219A


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature E185A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant E185A


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature N215A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant N215A


column_label: Table 1 (Kinetic parameters for Siw14-mediated dephosphorylation of naturally occurring PP-InsPs), enzyme row 'Siw14' with substrate '5-InsP7'; column 'Km (uM)' = 10.4; column 'Kcat (s^-1)' = 1.31; column 'Kcat/Km (10^6 M^-1 s^-1)' = 0.125.

normalized_value_unit_evidence: kcat: printed Table 1, row Siw14 with substrate 5-InsP7 cell 1.31 s-1; the printed unit s-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 1.31 s^(-1); the exported value is 1.31 s^(-1). Km: printed Table 1, row Siw14 with substrate 5-InsP7 cell 10.4 uM; 10.4 / 1000 = 0.0104 mM, and this pass writes that printed cell as the paper value; the exported value is 0.0101 mM, which the printed Table 1 cell for this enzyme and substrate replaces. kcat/Km: printed Table 1, row Siw14 with substrate 5-InsP7 cell 0.125 in a column headed in units of 10^6 M^-1 s^-1, that is 0.125 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 125000 / 1000 = 125 s^-1 mM^-1; the catalog identity stores no catalytic-efficiency value, so this printed cell is carried as evidence only.

raw_value_unit_evidence: Table 1, row Siw14 with substrate 5-InsP7: Km = 10.4 uM; kcat = 1.31 s-1; printed kcat/Km = 0.125 in a column headed in units of 10^6 M^-1 s^-1, that is 0.125 x 10^6 M^-1 s^-1.

row_label: Table 1, enzyme row 'Siw14' with substrate '5-InsP7'

table_label: Table 1: Kinetic parameters for Siw14-mediated dephosphorylation of naturally occurring PP-InsPs (J. Biol. Chem. (2018) 293(18) 6905-6914)


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature N183A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant N183A


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature K184A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant K184A


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature K250A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant K250A


sequence_variant_note: Resolved canonical sequence from UniProt:P53965 and applied mutation signature K218A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: diphosphoinositol-polyphosphate diphosphatase(Enzyme) mutant K218A


organism: Schizosaccharomyces pombe

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


organism: Escherichia coli

sequence_source: UniProtKB REST:P63228

proof_lines:
pH 8.0, wild-type enzyme
pH 7.5, 25°C, wild-type


organism: Mesorhizobium loti

sequence_source: UniProtKB REST:Q98I56


column_label: Table 2: Steady-state kinetic constants for hydrolysis of D-glycero-D-manno-heptose-1α,7-bisphosphate and D-glycero-D-manno-heptose-1β,7-bisphosphate by the selected D-glycero-D-manno-heptose-1,7-bisphosphate phosphatases (GmbBs). Table 2, enzyme source row 'M. loti', anomer column 'alpha'; column 'kcat (s-1)' = 4.4; column 'Km (uM)' = 58; column 'kcat/Km M-1 s-1' = 7.6 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.4 s^-1; already in s^-1, no conversion; the exported value is 4.4 s^(-1). Km: printed Table 2 cell 58 uM; 58 / 1000 = 0.058 mM; the exported value is 0.58 mM. kcat/Km: printed Table 2 cell 7.6 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 = 0.001 mM^-1 s^-1, so 76000.0 x 0.001 = 76.0 s^-1 mM^-1; the exported value is 7.586206896551725 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Table 2, enzyme source row 'M. loti', anomer column 'alpha': kcat = 4.4 s^-1; Km = 58 uM; printed kcat/Km = 7.6 x 10^4 M^-1 s^-1.


enzyme_display_name: dCMP deaminase

organism: Geobacillus thermodenitrificans

substrate_name: dCMP

proof_lines: in absence of dCTP, pH and temperature not specified in the publication

proof_lines: in presence of dCTP, pH and temperature not specified in the publication

enzyme: dCMP deaminase

substrate: dCMP


substrate_name: dCMP; H2O

sequence_source: UniProtKB REST:P32321

substrate: dCMP; H2O


organism: Paramecium bursaria Chlorella virus 1

substrate_name: dCTP

sequence_source: UniProtKB REST:O41078

proof_lines: pH 9.5, 42°C, in presence of 0.1 mM dCTP

substrate: dCTP


sequence_source: UniProtKB REST:O95989

proof_lines: pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProtKB REST:Q9NZJ9


column_label: Retained publisher HTML Table II, hDIPP2alpha row: Km 4.2 +/- 0.4; Kcat 0.15 +/- 0.01; Kcat/Km 360 x 10^5; k-1 2000 +/- 400.

normalized_value_unit_evidence: Kcat is 0.15 s^-1; Km 4.2 nM normalizes to 0.0000042 mM; independently printed Kcat/Km 360 x 10^5 M^-1 s^-1 normalizes to 36000 s^-1 mM^-1.

raw_value_unit_evidence: Table II hDIPP2alpha row: Km 4.2 +/- 0.4 nM; Kcat 0.15 +/- 0.01 s^-1; independently printed Kcat/Km 360 x 10^5 M^-1 s^-1; k-1 2000 +/- 400 s^-1.

table_label: Table II. Comparison of the catalytic properties of hDIPP isoforms with PP-InsP5 as substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST:O95989 and applied mutation signature H42A/R45A to reconstruct the assayed variant sequence.

proof_lines: mutant H42A/R45A, pH 7.2, temperature not specified in the publication


proof_lines: wild-type, pH 7.2, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST:O95989 and applied mutation signature R41A to reconstruct the assayed variant sequence.

proof_lines: mutant R41A, pH 7.2, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST:O95989 and applied mutation signature K18A to reconstruct the assayed variant sequence.

proof_lines: mutant K18A, pH 7.2, temperature not specified in the publication


enzyme_display_name: thiol S-methyltransferase

substrate_name: NCS-

sequence_source: UniProtKB:Q0WP12 canonical sequence REST JSON/TSV direct lookup

proof_lines: wild type protein, pH not specified in the publication, temperature not specified in the publication

enzyme: thiol S-methyltransferase

substrate: NCS-


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0WP12 canonical sequence plus selected-record mutation signature Y172F and applied mutation signature Y172F to reconstruct the assayed variant sequence.

proof_lines: Y172F mutant protein, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0WP12 canonical sequence plus selected-record mutation signature V23C and applied mutation signature V23C to reconstruct the assayed variant sequence.

proof_lines: V23C mutant protein, pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProtKB:Q9H8H3 canonical sequence REST JSON/TSV direct lookup

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


sequence_source: UniProtKB:Q6UX53 canonical sequence REST JSON/TSV direct lookup


organism: Phaeodactylum tricornutum

substrate_name: SH-

sequence_source: UniProtKB:B7FWR0 canonical sequence REST JSON/TSV direct lookup

substrate: SH-


organism: Raphanus sativus

substrate_name: thiocyanate

sequence_source: UniProtKB:C6L2E7 canonical sequence REST JSON/TSV direct lookup

proof_lines: pH 7.0, 30°C, purified recombinant enzyme

substrate: thiocyanate


enzyme_display_name: bile acid-CoA:amino acid N-acyltransferase

organism: Homo sapiens

substrate_name: Choloyl-CoA; Glycine

sequence_source: UniProtKB:Q14032 canonical sequence REST JSON/TSV direct lookup

assay_conditions_summary: pH 8.4; 310.15 K; cofactor CoA

substrate: Choloyl-CoA; Glycine


substrate_name: Glycine; Choloyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14032 canonical sequence plus selected-record mutation signature C235S and applied mutation signature C235S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bile acid-CoA:amino acid N-acyltransferase(Enzyme) mutant C235S

substrate: Glycine; Choloyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14032 canonical sequence plus selected-record mutation signature H362Q and applied mutation signature H362Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bile acid-CoA:amino acid N-acyltransferase(Enzyme) mutant H362Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14032 canonical sequence plus selected-record mutation signature D328A and applied mutation signature D328A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bile acid-CoA:amino acid N-acyltransferase(Enzyme) mutant D328A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14032 canonical sequence plus selected-record mutation signature C235A and applied mutation signature C235A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bile acid-CoA:amino acid N-acyltransferase(Enzyme) mutant C235A


organism: Mus musculus

substrate_name: Choloyl-CoA; Taurine

sequence_source: UniProtKB:Q91X34 canonical sequence REST JSON/TSV direct lookup

enzyme: bile acid-CoA:amino acid N-acyltransferase

substrate: Choloyl-CoA; Taurine


organism: Rattus norvegicus

sequence_source: UniProtKB:Q63276 canonical sequence REST JSON/TSV direct lookup


sequence_source: UniProtKB:Q9FN52 canonical sequence REST JSON/TSV direct lookup

smiles: CSCCCCC(=O)C(=O)O


enzyme_display_name: juvenile-hormone esterase

organism: Manduca sexta

substrate_name: juvenile hormone III

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9GPG0 and applied mutation signature T314V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; buffer 50 mM sodium phosphate pH 7.4

column_label: Table 1: Kinetic properties of the Manduca sexta juvenile hormone esterase and its two substrate-binding-pocket point mutants for JH III and saturated JH III (Biochemistry 2010, 49(17):3733-3742); printed column heads Enzyme | Substrate | Vmax (nmol min^-1 mg^-1) | KM (nM) | kcat (s^-1) | kcat/KM (M^-1 s^-1).; this label names the enzyme forms generically so that it carries only the enzyme-form label of the cited row. Table 1, enzyme row T314V, substrate column JH III; column Vmax (nmol min^-1 mg^-1) = 4370 ± 180; column KM (nM) = 86 ± 11; column kcat (s^-1) = 4.5; column kcat/KM (M^-1 s^-1) = 5.3 x 10^7. captured primary segment: T314V | JH III | Vmax 4370 ± 180 nmol min^-1 mg^-1 | KM 86 ± 11 nM | kcat 4.5 s^-1 | kcat/KM 5.3 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 86 nM; 1 nM is 1/1000000 mM, so 86 / 1000000 = 0.000086 mM; the exported value is 0.000086 mM. kcat: printed Table 1 kcat cell 4.5 s^-1; the column is already in s^-1 and no unit conversion applies; the exported value is 4.5 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 5.3 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.3 x 10^7 / 1000 = 53000.0 s^-1 mM^-1. Quotient disclosure for this row: 4.5 / 0.000086 = 52325.58139534883 s^-1 mM^-1 is the value the export carries for kcat_over_km, while the paper prints its own efficiency cell 5.3 x 10^7 M^-1 s^-1 = 53000.0 s^-1 mM^-1 for the same row; the printed cell is outside the interval that the two significant digits of the table would give for that quotient, so the printed cell is carried as the paper side of this row.

raw_value_unit_evidence: Table 1, enzyme row T314V, substrate JH III: KM = 86 nM; kcat = 4.5 s^-1; printed kcat/KM = 5.3 x 10^7 M^-1 s^-1.

enzyme: juvenile-hormone esterase

substrate: juvenile hormone III


substrate_name: Alpha-naphthyl acetate

sequence_source: UniProtKB Q9GPG0 canonical sequence.

substrate: Alpha-naphthyl acetate


organism: Tenebrio molitor

substrate_name: methyl 1-heptylthioacetothioate

sequence_source: UniProtKB Q8WRD8 canonical sequence.

substrate: methyl 1-heptylthioacetothioate


organism: Tribolium castaneum

sequence_source: UniProtKB D6WMZ8 canonical sequence; source accession D7US45 resolves as a secondary accession.

proof_lines: pH and temperature not specified in the publication


sequence_source: UniProtKB P63228 canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P63228 canonical sequence; C107A reconstructed after direct residue check. and applied mutation signature C107A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 25°C, mutant enzyme C107A
pH 8.0, mutant enzyme C107A


sequence_source: UniProtKB P63228 canonical sequence; C107A reconstructed after direct residue check.


sequence_variant_note: Resolved canonical sequence from UniProtKB P63228 canonical sequence; C109A reconstructed after direct residue check. and applied mutation signature C109A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P63228 and applied mutation signature K137A to reconstruct the assayed variant sequence.

row_label: Table 2, GmhB row 'K137A', substrate anomer beta


sequence_variant_note: Resolved canonical sequence from UniProtKB P63228 canonical sequence; C92A reconstructed after direct residue check. and applied mutation signature C92A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P63228 canonical sequence; C109A reconstructed after direct residue check.


sequence_variant_note: Resolved canonical sequence from UniProtKB P63228 canonical sequence; R110A reconstructed after direct residue check. and applied mutation signature R110A to reconstruct the assayed variant sequence.


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


substrate_name: D-fructose 1,6-bisphosphate

column_label: Table 1: Steady-state kinetic constants for E. coli GMHB catalyzed hydrolysis of phosphate esters in 50 mM Tris-HCl (pH 7.5, 25 °C) containing 1 mM MgCl2. Table 1, substrate row 'fructose 1,6-bisphosphate', E. coli GmhB; column 'kcat (sec-1)' = 0.039; column 'Km (uM)' = 1501; column 'kcat/Km (M-1 sec-1)' = 3 x 10^1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.039 s^-1; already in s^-1, no conversion; the exported value is 0.039 s^(-1). Km: printed Table 1 cell 1501 uM; 1501 / 1000 = 1.501 mM; the exported value is 1.5 mM. kcat/Km: printed Table 1 cell 3 x 10^1 M^-1 s^-1; 1 M^-1 s^-1 = 0.001 mM^-1 s^-1, so 30.0 x 0.001 = 0.03 s^-1 mM^-1; the exported value is 0.026 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Table 1, substrate row 'fructose 1,6-bisphosphate', E. coli GmhB: kcat = 0.039 s^-1; Km = 1501 uM; printed kcat/Km = 3 x 10^1 M^-1 s^-1.

substrate: D-fructose 1,6-bisphosphate


proof_lines:
pH 7.5, 25°C
pH 7.5, 25°C, Ki(slope)
pH 7.5, 25°C, Ki(intercept)


substrate_name: D-sedoheptulose 1,7-bisphosphate

substrate: D-sedoheptulose 1,7-bisphosphate


enzyme_display_name: inositol-trisphosphate 3-kinase

sequence_source: UniProtKB:P17105 direct accession lookup

enzyme: inositol-trisphosphate 3-kinase


organism: Arabidopsis thaliana

substrate_name: CDP-1,2-diacylglycerol; myo-Inositol

sequence_source: UniProtKB:Q8LBA6 direct accession lookup

substrate: CDP-1,2-diacylglycerol; myo-Inositol


substrate_name: myo-Inositol; CDP-1,2-diacylglycerol

sequence_source: UniProtKB:P70500 direct accession lookup

substrate: myo-Inositol; CDP-1,2-diacylglycerol


sequence_source: UniProtKB:P06197 direct accession lookup


organism: Bombyx mori

sequence_source: UniProtKB:D2KWC2 direct accession lookup


organism: Drosophila melanogaster

sequence_source: UniProtKB:A1ZA98 direct accession lookup

proof_lines:
racemic juvenile hormone III
10R isomer of juvenile hormone III
10S isomer of juvenile hormone III


substrate_name: saturated juvenile hormone III

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9GPG0 and applied mutation signature F259I to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic properties of the Manduca sexta juvenile hormone esterase and its two substrate-binding-pocket point mutants for JH III and saturated JH III (Biochemistry 2010, 49(17):3733-3742); printed column heads Enzyme | Substrate | Vmax (nmol min^-1 mg^-1) | KM (nM) | kcat (s^-1) | kcat/KM (M^-1 s^-1).; this label names the enzyme forms generically so that it carries only the enzyme-form label of the cited row. Table 1, enzyme row F259I, substrate column saturated JH III; column Vmax (nmol min^-1 mg^-1) = 3000 ± 150; column KM (nM) = 641 ± 84; column kcat (s^-1) = 3.1; column kcat/KM (M^-1 s^-1) = 4.8 x 10^6. captured primary segment: F259I | saturated JH III | Vmax 3000 ± 150 nmol min^-1 mg^-1 | KM 641 ± 84 nM | kcat 3.1 s^-1 | kcat/KM 4.8 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 641 nM; 1 nM is 1/1000000 mM, so 641 / 1000000 = 0.000641 mM; the exported value is 0.000641 mM. kcat: printed Table 1 kcat cell 3.1 s^-1; the column is already in s^-1 and no unit conversion applies; the exported value is 3.1 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 4.8 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.8 x 10^6 / 1000 = 4800.0 s^-1 mM^-1. Quotient disclosure for this row: 3.1 / 0.000641 = 4836.19344773791 s^-1 mM^-1, which is the exported kcat_over_km, and that quotient written to the two significant digits of the table is the printed cell 4.8 x 10^6 M^-1 s^-1.

raw_value_unit_evidence: Table 1, enzyme row F259I, substrate saturated JH III: KM = 641 nM; kcat = 3.1 s^-1; printed kcat/KM = 4.8 x 10^6 M^-1 s^-1.

substrate: saturated juvenile hormone III


sequence_source: UniProtKB:Q9GPG0 direct accession lookup


column_label: Table 1: Kinetic properties of the Manduca sexta juvenile hormone esterase and its two substrate-binding-pocket point mutants for JH III and saturated JH III (Biochemistry 2010, 49(17):3733-3742); printed column heads Enzyme | Substrate | Vmax (nmol min^-1 mg^-1) | KM (nM) | kcat (s^-1) | kcat/KM (M^-1 s^-1).; this label names the enzyme forms generically so that it carries only the enzyme-form label of the cited row. Table 1, enzyme row MsJHE, substrate column saturated JH III; column Vmax (nmol min^-1 mg^-1) = 630 ± 40; column KM (nM) = 46 ± 10; column kcat (s^-1) = 0.7; column kcat/KM (M^-1 s^-1) = 1.4 x 10^7. captured primary segment: MsJHE | saturated JH III | Vmax 630 ± 40 nmol min^-1 mg^-1 | KM 46 ± 10 nM | kcat 0.7 s^-1 | kcat/KM 1.4 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 46 nM; 1 nM is 1/1000000 mM, so 46 / 1000000 = 0.000046 mM; the exported value is 0.000046 mM. kcat: printed Table 1 kcat cell 0.7 s^-1; the column is already in s^-1 and no unit conversion applies; the exported value is 0.7 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 1.4 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^7 / 1000 = 14000.0 s^-1 mM^-1. Quotient disclosure for this row: 0.7 / 0.000046 = 15217.391304347826 s^-1 mM^-1 is the value the export carries for kcat_over_km, while the paper prints its own efficiency cell 1.4 x 10^7 M^-1 s^-1 = 14000.0 s^-1 mM^-1 for the same row; the printed cell is outside the interval that the two significant digits of the table would give for that quotient, so the printed cell is carried as the paper side of this row.

raw_value_unit_evidence: Table 1, enzyme row MsJHE, substrate saturated JH III: KM = 46 nM; kcat = 0.7 s^-1; printed kcat/KM = 1.4 x 10^7 M^-1 s^-1.


column_label: Table 1: Kinetic properties of the Manduca sexta juvenile hormone esterase and its two substrate-binding-pocket point mutants for JH III and saturated JH III (Biochemistry 2010, 49(17):3733-3742); printed column heads Enzyme | Substrate | Vmax (nmol min^-1 mg^-1) | KM (nM) | kcat (s^-1) | kcat/KM (M^-1 s^-1).; this label names the enzyme forms generically so that it carries only the enzyme-form label of the cited row. Table 1, enzyme row F259I, substrate column JH III; column Vmax (nmol min^-1 mg^-1) = 3850 ± 210; column KM (nM) = 101 ± 17; column kcat (s^-1) = 4.0; column kcat/KM (M^-1 s^-1) = 4.0 x 10^7. captured primary segment: F259I | JH III | Vmax 3850 ± 210 nmol min^-1 mg^-1 | KM 101 ± 17 nM | kcat 4.0 s^-1 | kcat/KM 4.0 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 101 nM; 1 nM is 1/1000000 mM, so 101 / 1000000 = 0.000101 mM; the exported value is 0.000101 mM. kcat: printed Table 1 kcat cell 4.0 s^-1; the column is already in s^-1 and no unit conversion applies; the exported value is 4.0 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 4.0 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.0 x 10^7 / 1000 = 40000.0 s^-1 mM^-1. Quotient disclosure for this row: 4.0 / 0.000101 = 39603.960396039605 s^-1 mM^-1, which is the exported kcat_over_km, and that quotient written to the two significant digits of the table is the printed cell 4.0 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: Table 1, enzyme row F259I, substrate JH III: KM = 101 nM; kcat = 4.0 s^-1; printed kcat/KM = 4.0 x 10^7 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9GPG0 direct accession lookup and applied mutation signature F259I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: mutant F259I, at 30°C in 50 mM sodium phosphate buffer, pH 7.4, containing 1 mg/mL of bovine serum albumin


column_label: Table 1: Kinetic properties of the Manduca sexta juvenile hormone esterase and its two substrate-binding-pocket point mutants for JH III and saturated JH III (Biochemistry 2010, 49(17):3733-3742); printed column heads Enzyme | Substrate | Vmax (nmol min^-1 mg^-1) | KM (nM) | kcat (s^-1) | kcat/KM (M^-1 s^-1).; this label names the enzyme forms generically so that it carries only the enzyme-form label of the cited row. Table 1, enzyme row MsJHE, substrate column JH III; column Vmax (nmol min^-1 mg^-1) = 630 ± 30; column KM (nM) = 30 ± 5; column kcat (s^-1) = 0.7; column kcat/KM (M^-1 s^-1) = 2.2 x 10^7. captured primary segment: MsJHE | JH III | Vmax 630 ± 30 nmol min^-1 mg^-1 | KM 30 ± 5 nM | kcat 0.7 s^-1 | kcat/KM 2.2 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 KM cell 30 nM; 1 nM is 1/1000000 mM, so 30 / 1000000 = 0.00003 mM; the exported value is 0.00003 mM. kcat: printed Table 1 kcat cell 0.7 s^-1; the column is already in s^-1 and no unit conversion applies; the exported value is 0.7 s^(-1). kcat/Km: printed Table 1 kcat/KM cell 2.2 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.2 x 10^7 / 1000 = 22000.0 s^-1 mM^-1. Quotient disclosure for this row: 0.7 / 0.00003 = 23333.333333333332 s^-1 mM^-1 is the value the export carries for kcat_over_km, while the paper prints its own efficiency cell 2.2 x 10^7 M^-1 s^-1 = 22000.0 s^-1 mM^-1 for the same row; the printed cell is outside the interval that the two significant digits of the table would give for that quotient, so the printed cell is carried as the paper side of this row.

raw_value_unit_evidence: Table 1, enzyme row MsJHE, substrate JH III: KM = 30 nM; kcat = 0.7 s^-1; printed kcat/KM = 2.2 x 10^7 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9GPG0 direct accession lookup and applied mutation signature T314V to reconstruct the assayed variant sequence.

proof_lines: mutant T314V, at 30°C in 50 mM sodium phosphate buffer, pH 7.4, containing 1 mg/mL of bovine serum albumin


proof_lines: wild-type, at 30°C in 50 mM sodium phosphate buffer, pH 7.4, containing 1 mg/mL of bovine serum albumin


sequence_source: UniProtKB:Q9FN52 direct accession lookup (UniProtKB reviewed (Swiss-Prot); organism=Arabidopsis thaliana; protein=Methylthioalkylmalate synthase 3, chloroplastic; EC=2.3.3.17).


smiles: CSCCC(=O)C(=O)O

column_label: Table III (Kinetic parameters for various 2-oxo acids with recombinant MAM3), substrate row '4-Methylthio-2-oxobutanoic acid (/C3 glucosinolates)'; column 'Km (uM)' = 932; column 'Vmax (nmol min^-1 mg^-1)' = 1,448; column 'kcat (s^-1)' = 1.3; column 'kcat/Km (M^-1 s^-1)' = 1,380.

normalized_value_unit_evidence: Km: printed Table III cell 932 in the column headed 'Km (uM)'; 932 / 1000 = 0.932 mM; the exported value is 0.932 mM. kcat: printed Table III cell 1.3 in the column headed 'kcat (s^-1)'; s^-1 is already the canonical turnover unit, so no unit conversion applies; the exported value is 1.3 s^(-1). kcat/Km: printed Table III cell 1,380 in the column headed 'kcat/Km (M^-1 s^-1)'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1380 / 1000 = 1.38 s^-1 mM^-1; the exported value is 1.3948497854077253 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, substrate row '4-Methylthio-2-oxobutanoic acid (/C3 glucosinolates)': Km = 932 uM; kcat = 1.3 s^-1; printed kcat/Km = 1,380 M^-1 s^-1.


organism: Brassica juncea

substrate_name: acetyl-CoA

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

substrate: acetyl-CoA


sequence_source: UniProtKB:C5J4P1 direct accession lookup (UniProtKB unreviewed (TrEMBL); organism=Brassica juncea; protein=methylthioalkylmalate synthase; EC=2.3.3.17).


enzyme_display_name: cinnamate beta-D-glucosyltransferase

organism: Fragaria vesca

substrate_name: gallate

sequence_source: UniProtKB:A0A2U9N624 direct accession lookup (UniProtKB unreviewed (TrEMBL); organism=Fragaria vesca; protein=Glycosyltransferase; EC=2.4.1.-).

enzyme: cinnamate beta-D-glucosyltransferase

substrate: gallate


substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Fragaria x ananassa

substrate_name: sinapate

substrate: sinapate


substrate_name: vanillate

substrate: vanillate


sequence_source: UniProtKB:Q2V6K1 direct accession lookup (UniProtKB reviewed (Swiss-Prot); organism=Fragaria ananassa; protein=Putative UDP-glucose glucosyltransferase; EC=2.4.1.-).


sequence_source: UniProtKB:Q66PF4 direct accession lookup (UniProtKB reviewed (Swiss-Prot); organism=Fragaria ananassa; protein=Cinnamate beta-D-glucosyltransferase; EC=2.4.1.177).

proof_lines:
recombinant enzyme, pH 7.0, 30°C
with cinnamic acid


substrate_name: syringate

substrate: syringate


assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
pH 8.0, 30°C, isoenzyme Bju.IPMS1-B2
pH 8.0, 30°C, isoenzyme Bju.IPMS1-A1
pH 8.0, 30°C, isoenzyme Bju.IPMS1-A2


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines:
isoform Leu9, at pH 7.5 and 30°C
isoform Leu4, at pH 7.5 and 30°C
with respect to acetyl-CoA


organism: Unknown

substrate_name: Unknown

substrate: Unknown


substrate_name: ATP

substrate: ATP


substrate_name: myo-inositol

substrate: myo-inositol


enzyme_display_name: cysteine desulfurase

organism: Synechocystis sp.

substrate_name: L-selenocysteine

proof_lines:
pH 7.5, 37°C, isoenzyme SsCsd1
pH 7.5, 37°C, isoenzyme SsCsd2

enzyme: cysteine desulfurase

substrate: L-selenocysteine


substrate_name: dCMP

substrate: dCMP


substrate_name: diphosphoinositol pentakisphosphate

proof_lines:
isoenzyme hDIPP1
isoenzyme hDIPP2alpha
isoenzyme hDIPP2beta

substrate: diphosphoinositol pentakisphosphate


substrate_name: KSCN

substrate: KSCN


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: gliotoxin

substrate: gliotoxin


substrate_name: taurine toward choloyl-CoA

substrate: taurine toward choloyl-CoA


organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)


substrate_name: 4-methylthio-2-oxobutanoic acid

substrate: 4-methylthio-2-oxobutanoic acid


substrate_name: L-Cysteine; Acceptor

sequence_source: UniProtKB REST accession Q93WX6, release 2026_02

substrate: L-Cysteine; Acceptor


sequence_source: UniProtKB REST accession O49543, release 2026_02


organism: Azotobacter vinelandii

substrate_name: L-cysteine

assay_conditions_summary: pH 8

substrate: L-cysteine


substrate_name: L-Cysteine

mutation_signature: Δ1

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

mutation_type: deletion

proof_lines: SABIO-RK modifier species: cysteine desulfurase(Enzyme) mutant Nfs1 delta1-53/Isd11/IscU

substrate: L-Cysteine


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P77444 plus direct mutation reconstruction and applied mutation signature E96A to reconstruct the assayed variant sequence.

proof_lines: mutant E96A, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P77444 plus direct mutation reconstruction and applied mutation signature H55A to reconstruct the assayed variant sequence.

proof_lines: mutant H55A, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P77444 plus direct mutation reconstruction and applied mutation signature E250A to reconstruct the assayed variant sequence.

proof_lines: mutant E250A, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P77444 plus direct mutation reconstruction and applied mutation signature R92A to reconstruct the assayed variant sequence.

proof_lines: mutant R92A, pH 8.0, temperature not specified in the publication


sequence_source: UniProtKB REST accession P77444, release 2026_02

proof_lines: wild-type, pH 8.0, temperature not specified in the publication


sequence_source: UniProtKB REST accession P0A6B7, release 2026_02


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB REST accession P9WQ71, release 2026_02


organism: Nostoc sp. PCC 7120 = FACHB-418

proof_lines: absence of Anabaena sulfur acceptor E, pH 7.4, temperature not specified in the publication

proof_lines: presence of Anabaena sulfur acceptor E, pH 7.4, temperature not specified in the publication


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: ATP using 24-mer 5'-OH DNA as substrate

substrate: ATP using 24-mer 5'-OH DNA as substrate


organism: Arabidopsis thaliana


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: myo-inositol (at pH 9.0 and 37 degrees Celsius)

assay_conditions_summary: pH 9


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: CDP-diacylglycerol

substrate: CDP-diacylglycerol


substrate_name: L-Cysteine (at 37 degrees Celsius and pH 7.9)


substrate_name: Unknown


organism: Escherichia coli (strain K12)

substrate_name: L-cysteine sulfinate

substrate: L-cysteine sulfinate


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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: L-cysteine (at pH 7.5 and 37 degrees Celsius)

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


organism: African swine fever virus (strain Badajoz 1971 Vero-adapted)


substrate_name: polyphosphate

substrate: polyphosphate


organism: Homo sapiens


enzyme_display_name: glycogen(starch) synthase

organism: Unknown

substrate_name: UDP-glucose

enzyme: glycogen(starch) synthase

substrate: UDP-glucose


organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

proof_lines: kcat for encapulated enzyme is 67 sec(-1), for unencapsulated enzyme is 10 sec(-1).

substrate: Unknown


organism: Tribolium castaneum

substrate_name: juvenile hormone (JH) III

substrate: juvenile hormone (JH) III


organism: Streptantibioticus cattleyicolor

substrate_name: fluoroacetyl-CoA (at pH 8 and 25 degrees Celsius)

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: kcat is 390 sec(-1) with fluoroacetyl-CoA as substrate and 0.06 sec(-1) with acetyl-CoA (at pH 7.6 and 25 degrees Celsius, PubMed:20836570). kcat is 0.044 sec(-1) with fluoroacetyl-CoA as substrate (PubMed:20430898).


substrate_name: 5-diphosphoinositol pentakisphosphate

proof_lines: kcat is 0.0025 sec(-1) with 5-diphosphoinositol pentakisphosphate as substrate (PubMed:26828065). kcat is 1.31 sec(-1) with 5-diphosphoinositol pentakisphosphate as substrate, 0.77 sec(-1) with 5-diphosphoinositol tetrakisphosphate as subst

substrate: 5-diphosphoinositol pentakisphosphate


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

proof_lines: kcat is 2 sec(-1) for Ap6A. kcat is 1.7 sec(-1) for Ap5A.


substrate_name: inorganic diphosphate (pyrophosphate) (at 37 degrees Celsius and at pH 5)

assay_conditions_summary: pH 5

proof_lines: kcat is 0.44 sec(-1) with inorganic diphosphate (pyrophosphate) as substrate (at 37 degrees Celsius and at pH 5) (PubMed:37772819). kcat is 1.24 sec(-1) with p-nitrophenylphosphate as substrate (at 37 degrees Celsius and at pH 5) (PubMed:37


organism: Rattus norvegicus

substrate_name: D-myo-Inositol 1,4,5-trisphosphate; ATP

proof_lines: recombinant enzyme IP3K-C fragment comprising calmodulin binding domain and catalytic domain

proof_lines: recombinant enzyme IP3K-C fragment comprising catalytic domain

substrate: D-myo-Inositol 1,4,5-trisphosphate; ATP


substrate_name: Inositol 2,4,5-trisphosphate; ATP

substrate: Inositol 2,4,5-trisphosphate; ATP


enzyme_display_name: fructose-6-phosphate phosphoketolase

organism: Bifidobacterium breve

substrate_name: D-fructose 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:D6PAH1 canonical sequence with validated S440A substitution from selected BRENDA note and applied mutation signature S440A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S440A, pH and temperature not specified in the publication

enzyme: fructose-6-phosphate phosphoketolase

substrate: D-fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:D6PAH1 canonical sequence with validated Y501F substitution from selected BRENDA note and applied mutation signature Y501F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y501F, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:D6PAH1 canonical sequence with validated Q321A substitution from selected BRENDA note and applied mutation signature Q321A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q321A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:D6PAH1 canonical sequence with validated H548A substitution from selected BRENDA note and applied mutation signature H548A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H548A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:D6PAH1 canonical sequence with validated H142A substitution from selected BRENDA note and applied mutation signature H142A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H142A, pH and temperature not specified in the publication


sequence_source: UniProtKB:D6PAH1 exact accession lookup

proof_lines: wild type enzyme, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:D6PAH1 canonical sequence with validated H142N substitution from selected BRENDA note and applied mutation signature H142N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H142N, pH and temperature not specified in the publication


organism: Lactobacillus plantarum

substrate_name: D-Fructose 6-phosphate; Phosphate

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: fructose-6-phosphate phosphoketolase(Enzyme) wildtype delta 1-7 truncated, N-terminal His-tag

substrate: D-Fructose 6-phosphate; Phosphate


organism: Lactococcus lactis subsp. lactis

substrate_name: D-Fructose 6-phosphate

sequence_source: UniProtKB:Q9CFH4 exact accession lookup

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

substrate: D-Fructose 6-phosphate


substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


substrate_name: D-Xylulose 5-phosphate

substrate: D-Xylulose 5-phosphate


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9HY13 exact accession lookup


organism: Oryctolagus cuniculus

substrate_name: MLC (isoform Smooth-muscle at 22 degrees Celsius)


substrate_name: 1D-myo-inositol 1,4,5-trisphosphate

substrate: 1D-myo-inositol 1,4,5-trisphosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Arabidopsis thaliana

substrate_name: 4-methylthio-2-oxobutanoic acid

substrate: 4-methylthio-2-oxobutanoic acid


organism: Caenorhabditis elegans

substrate_name: UDP-glucose (at 30 degrees Celsius)

substrate: UDP-glucose (at 30 degrees Celsius)


substrate_name: UDP-alpha-D-glucose (UDPG) (in the absence of glucose-6-phosphate) (poorly and non-phosphorylated state)

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


organism: Mus musculus


substrate_name: UDP-alpha-D-glucose (UDPG) (in the absence of glucose-6-phosphate) (poorly or non-phosphorylated state)


organism: Trichomonas vaginalis (strain ATCC PRA-98 / G3)

substrate_name: UDP-glucose

assay_conditions_summary: cofactor ADP


organism: Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)

substrate_name: lacto-N-biose

substrate: lacto-N-biose


organism: Homo sapiens

substrate_name: MLC (isoform 1 at 22 degrees Celsius)

substrate: MLC (isoform 1 at 22 degrees Celsius)


organism: Cyanophora paradoxa

substrate_name: ADP-glucose / UDP-glucose

sequence_source: UniProtKB:A8V967 live REST lookup; unreviewed A8V967_CYAPA canonical sequence

assay_conditions_summary: pH 7.5; 308.15 K; cofactor ADP

substrate: ADP-glucose / UDP-glucose


substrate_name: Unknown

sequence_source: UniProtKB:P13807 live REST lookup; reviewed Swiss-Prot GYS1_HUMAN canonical sequence


organism: Fragaria x ananassa


substrate: UDP-glucose


organism: Rubus idaeus

substrate_name: gallate / UDP-glucose

sequence_source: UniProtKB:A0A2U9N6D2 live REST lookup; unreviewed A0A2U9N6D2_RUBID canonical sequence

substrate: gallate / UDP-glucose


substrate_name: gallate

substrate: gallate


organism: Bifidobacterium longum

substrate_name: lacto-N-biose I / galacto-N-biose / alpha-D-galactose 1-phosphate / phosphate

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

sequence_source: UniProtKB:E8MF13 live REST lookup; reviewed Swiss-Prot LNPA_BIFL2 canonical sequence

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


substrate_name: lacto-N-biose I / galacto-N-biose / alpha-D-galactose 1-phosphate

proof_lines: wild type enzyme, using N-acetyl-D-glucosamine as cosubstrate


substrate_name: alpha-D-galactose 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 canonical sequence with selected row mutation Y362F reconstructed after residue check and applied mutation signature Y362F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y362F, using N-acetyl-D-glucosamine as cosubstrate

substrate: alpha-D-galactose 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 canonical sequence with selected row mutation N166A reconstructed after residue check and applied mutation signature N166A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N166A, using N-acetyl-D-glucosamine as cosubstrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 canonical sequence with selected row mutation F364N reconstructed after residue check and applied mutation signature F364N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F364N, using N-acetyl-D-glucosamine as cosubstrate


substrate_name: galacto-N-biose / lacto-N-biose I

sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 canonical sequence with selected row mutation S336A reconstructed after residue check and applied mutation signature S336A to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 30°C, mutant S336A
pH 7.5, 30°C, mutants S336A and

substrate: galacto-N-biose / lacto-N-biose I


substrate_name: galacto-N-biose

sequence_variant_note: Resolved canonical sequence from UniProtKB:E8MF13 canonical sequence with selected row mutation P161S reconstructed after residue check and applied mutation signature P161S to reconstruct the assayed variant sequence.

substrate: galacto-N-biose


substrate_name: lacto-N-biose I

sequence_source: UniProtKB:E8MF13 canonical sequence with selected row mutation P161S reconstructed after residue check

substrate: lacto-N-biose I


organism: Gallus gallus

substrate_name: Inositol 2,4,5-trisphosphate / ATP

sequence_source: UniProtKB:Q9YH86 live REST lookup; unreviewed Q9YH86_CHICK canonical sequence

substrate: Inositol 2,4,5-trisphosphate / ATP


enzyme_display_name: mycothione reductase

organism: Unknown

substrate_name: NADPH

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

assay_conditions_summary: cofactor NADPH

enzyme: mycothione reductase

substrate: NADPH


substrate_name: a neolactoside nLc4Cer(d18:1(4E))

substrate: a neolactoside nLc4Cer(d18:1(4E))