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


organism: Homo sapiens

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

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

data_origin: experimental

status: unverified

source: oed


source_db: brenda

kcat_over_km_display: Not reported

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

source: brenda


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.

mutation_type: substitution

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


kcat_display: Not reported

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

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


organism: Staphylococcus aureus

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

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

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

source_databases_merged: brenda skid

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


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


organism: Mus musculus

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


verification_status: corrected

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)

status: corrected


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)

source_db: uniprot

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

assay_conditions_summary: cofactor NADPH

source: uniprot


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


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)


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


organism: Escherichia coli (strain K12)

verification_status: verified

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.

status: verified


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


organism: Homo sapiens

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

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

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 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: 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


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

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


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


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

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 UniProtKB Q9GPG0 canonical sequence; T314V reconstructed after direct residue check. and applied mutation signature T314V to reconstruct the assayed variant sequence.

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

substrate: saturated juvenile hormone III


sequence_source: UniProtKB:Q9GPG0 direct accession lookup


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


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))


organism: Pasteurella multocida

substrate_name: 4-methylumbelliferyl beta-lactoside

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q15KI8 direct REST lookup 2026-06-18 and applied mutation signature M144H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 310.15 K; buffer Tris-HCl

proof_lines: mutant enzyme M144H, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: mutant enzyme M144H, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: mutant enzyme M144H, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

substrate: 4-methylumbelliferyl beta-lactoside


substrate_name: CMP-N-acetyl-beta-neuraminate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q15KI8 and applied mutation signature H311A to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row H311A; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 1.8 mM; kcat cell = 2.1 s^-1; kcat/Km cell = 1.1 s^-1 mM^-1; author manuscript page 17 (PDF page 17). captured primary segment: CMP-Neu5Ac | PmST1 H311A, the H311A single mutant of Pasteurella multocida sialyltransferase 1 | Table 1, enzyme row H311A: Km 1.8 mM | kcat 2.1 s^-1 | kcat/Km printed cell 1.1 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 1.8 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 1.8 mM. kcat: printed cell 2.1 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 2.1 s^(-1). kcat/Km: printed cell 1.1 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 1.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row H311A: Km = 1.8 mM; kcat = 2.1 s^-1; printed kcat/Km = 1.1 s^-1 mM^-1.

row_label: Table 1, enzyme row H311A

table_label: Table 1 (Apparent kinetics of the CMP-Neu5Ac hydrolysis activity of WT PmST1 and mutants), printed column heads enzyme | Km (mM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1)

substrate: CMP-N-acetyl-beta-neuraminate


sequence_source: UniProtKB:Q15KI8 direct REST lookup 2026-06-18


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q15KI8 direct REST lookup 2026-06-18 and applied mutation signature H311A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H311A, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C


substrate_name: 4-methylumbelliferyl beta-Lewis x

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q15KI8 and applied mutation signature M144H to reconstruct the assayed variant sequence.

column_label: Table 2, acceptor row LexbMU, M144H column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 8.1 mM; kcat cell = 8.4 s^-1; kcat/Km cell = 1.0 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LexβMU | PmST1 M144H, the M144H single mutant of Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LexβMU, M144H column block: Km 8.1 mM | kcat 8.4 s^-1 | kcat/Km printed cell 1.0 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 8.1 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 8.1 mM. kcat: printed cell 8.4 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 8.4 s^(-1). kcat/Km: printed cell 1.0 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 1.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LexbMU, M144H column block: Km = 8.1 mM; kcat = 8.4 s^-1; printed kcat/Km = 1.0 s^-1 mM^-1.

table_label: Table 2 (Apparent kinetics of the alpha2-3-sialyltransferase activity of WT PmST1 and mutants), printed column blocks Km (mM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1), each block split into the sub-columns WT | M144D | M144H

substrate: 4-methylumbelliferyl beta-Lewis x


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q15KI8 and applied mutation signature D141A to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row D141A; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 1.4 mM; kcat cell = 2.5 x 10^-2 s^-1; kcat/Km cell = 1.8 x 10^-2 s^-1 mM^-1; author manuscript page 17 (PDF page 17). captured primary segment: CMP-Neu5Ac | PmST1 D141A, the D141A single mutant of Pasteurella multocida sialyltransferase 1 | Table 1, enzyme row D141A: Km 1.4 mM | kcat 2.5 x 10^-2 s^-1 | kcat/Km printed cell 1.8 x 10^-2 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 1.4 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 1.4 mM. kcat: printed cell 2.5 x 10^-2 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 0.025 s^(-1). kcat/Km: printed cell 1.8 x 10^-2 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 0.018 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row D141A: Km = 1.4 mM; kcat = 2.5 x 10^-2 s^-1; printed kcat/Km = 1.8 x 10^-2 s^-1 mM^-1.

row_label: Table 1, enzyme row D141A


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


organism: Photobacterium phosphoreum

sequence_source: UniProtKB:A5LHX0 direct REST lookup 2026-06-18

proof_lines:
pH 6.0, 25°C
Raw SKiD Env: Temp=25°C, pH=6


organism: Photobacterium sp. JT-ISH-224

sequence_source: UniProtKB:A8QYL0 direct REST lookup 2026-06-18


organism: Rattus norvegicus

sequence_source: UniProtKB:Q02734 direct REST lookup 2026-06-18

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: cathepsin V

sequence_source: UniProtKB:O60911 direct REST lookup 2026-06-18

enzyme: cathepsin V


proof_lines: pH 5.5, 37°C, presence of dermatan sulfate

proof_lines: pH 5.5, 37°C, presence of heparan sulfate

proof_lines: in 0.1 M sodium acetate buffer pH 5.5 containing 2.5 mM dithiothreitol and 1 mM EDTA, at 25°C


enzyme_display_name: aminodeoxyfutalosine deaminase

organism: Acidothermus cellulolyticus

sequence_source: UniProtKB:A0LRH8 direct REST lookup 2026-06-18

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'AFL', Acel0264 column group; column 'kcat (s-1)' = 6.8; column 'Km (uM)' = 6.0; column 'kcat/Km (M-1 s-1)' = 1.1 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 6.8 s^-1; already in s^-1, no unit conversion applies; normalized 6.8 s^(-1). Km: printed cell 6.0 uM; 6.0 / 1000 = 0.006 mM; normalized 0.006 mM. kcat/Km: printed cell 1.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^6 / 1000 = 1100 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row AFL, Acel0264 column group: kcat = 6.8 s^-1; Km = 6.0 uM; kcat/Km = 1.1 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row 'AFL', Acel0264 column group

table_label: Table 2: Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429 (Biochemistry 2013, 52(37))

enzyme: aminodeoxyfutalosine deaminase


sequence_source: UniProtKB:A0LRH8 reviewed canonical sequence

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'NECA', Acel0264 column group; column 'kcat (s-1)' = 0.007; column 'Km (uM)' = 61; column 'kcat/Km (M-1 s-1)' = 110.

normalized_value_unit_evidence: kcat: printed cell 0.007 s^-1; already in s^-1, no unit conversion applies; normalized 0.007 s^(-1). Km: printed cell 61 uM; 61 / 1000 = 0.061 mM; normalized 0.061 mM. kcat/Km: printed cell 110 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 110 / 1000 = 0.11 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row NECA, Acel0264 column group: kcat = 0.007 s^-1; Km = 61 uM; kcat/Km = 110 M^-1 s^-1.

row_label: Table 2, substrate row 'NECA', Acel0264 column group


organism: Deinococcus radiodurans

sequence_source: UniProtKB:Q9RW45 reviewed canonical sequence

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'AFL', Dr0824 column group; column 'kcat (s-1)' = 8.6; column 'Km (uM)' = 1.8; column 'kcat/Km (M-1 s-1)' = 4.8 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 8.6 s^-1; already in s^-1, no unit conversion applies; normalized 8.6 s^(-1). Km: printed cell 1.8 uM; 1.8 / 1000 = 0.0018 mM; normalized 0.0018 mM. kcat/Km: printed 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 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row AFL, Dr0824 column group: kcat = 8.6 s^-1; Km = 1.8 uM; kcat/Km = 4.8 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row 'AFL', Dr0824 column group


column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row '2'-deoxyadenosine', Dr0824 column group; column 'kcat (s-1)' = 0.72; column 'Km (uM)' = 37; column 'kcat/Km (M-1 s-1)' = 1.9 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.72 s^-1; already in s^-1, no unit conversion applies; normalized 0.72 s^(-1). Km: printed cell 37 uM; 37 / 1000 = 0.037 mM; normalized 0.037 mM. kcat/Km: printed 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 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row 2'-deoxyadenosine, Dr0824 column group: kcat = 0.72 s^-1; Km = 37 uM; kcat/Km = 1.9 x 10^4 M^-1 s^-1.

row_label: Table 2, substrate row '2'-deoxyadenosine', Dr0824 column group


organism: Nitratiruptor sp. SB155-2

sequence_source: UniProtKB:A6Q234 reviewed canonical sequence

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row '5'-deoxyadenosine', Nis0429 column group; column 'kcat (s-1)' = 0.017; column 'Km (uM)' = 42; column 'kcat/Km (M-1 s-1)' = 410.

normalized_value_unit_evidence: kcat: printed cell 0.017 s^-1; already in s^-1, no unit conversion applies; normalized 0.017 s^(-1). Km: printed cell 42 uM; 42 / 1000 = 0.042 mM; normalized 0.042 mM. kcat/Km: printed cell 410 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 410 / 1000 = 0.41 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row 5'-deoxyadenosine, Nis0429 column group: kcat = 0.017 s^-1; Km = 42 uM; kcat/Km = 410 M^-1 s^-1.

row_label: Table 2, substrate row '5'-deoxyadenosine', Nis0429 column group


column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'AFL', Nis0429 column group; column 'kcat (s-1)' = 1.2; column 'Km (uM)' = 0.9; column 'kcat/Km (M-1 s-1)' = 1.3 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 1.2 s^-1; already in s^-1, no unit conversion applies; normalized 1.2 s^(-1). Km: printed cell 0.9 uM; 0.9 / 1000 = 0.0009 mM; normalized 0.0009 mM. kcat/Km: printed cell 1.3 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^6 / 1000 = 1300 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row AFL, Nis0429 column group: kcat = 1.2 s^-1; Km = 0.9 uM; kcat/Km = 1.3 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row 'AFL', Nis0429 column group


organism: Streptomyces avermitilis

substrate_name: adenosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q82K09 canonical sequence with selected-batch R87M reconstruction and applied mutation signature R87M to reconstruct the assayed variant sequence.

substrate: adenosine


sequence_source: UniProtKB:Q82K09 reviewed canonical sequence

column_label: Table 2 (Kinetic Constants for Sav2595, Acel0264, Dr0824, and Nis0429), substrate row 'AFL', Sav2595 column group; column 'kcat (s-1)' = 3.8; column 'Km (uM)' = 4.8; column 'kcat/Km (M-1 s-1)' = 7.9 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 3.8 s^-1; already in s^-1, no unit conversion applies; normalized 3.8 s^(-1). Km: printed cell 4.8 uM; 4.8 / 1000 = 0.0048 mM; normalized 0.0048 mM. kcat/Km: printed cell 7.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.9 x 10^5 / 1000 = 790 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row AFL, Sav2595 column group: kcat = 3.8 s^-1; Km = 4.8 uM; kcat/Km = 7.9 x 10^5 M^-1 s^-1.

row_label: Table 2, substrate row 'AFL', Sav2595 column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q82K09 and applied mutation signature R87M to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Constants for Sav2595 mutants), variant row 'R87M', AFL column group; column 'kcat (s-1)' = 0.42; column 'Km (uM)' = 8; column 'kcat/Km (M-1 s-1)' = 5.3 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.42 s^-1; already in s^-1, no unit conversion applies; normalized 0.42 s^(-1). Km: printed cell 8 uM; 8 / 1000 = 0.008 mM; normalized 0.008 mM. kcat/Km: printed cell 5.3 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.3 x 10^4 / 1000 = 53 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row R87M, AFL column group: kcat = 0.42 s^-1; Km = 8 uM; kcat/Km = 5.3 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'R87M', AFL column group

table_label: Table 3: Kinetic Constants for Sav2595 mutants (Biochemistry 2013, 52(37))


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q82K09 and applied mutation signature R87A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Constants for Sav2595 mutants), variant row 'R87A', AFL column group; column 'kcat (s-1)' = 0.094; column 'Km (uM)' = 3.4; column 'kcat/Km (M-1 s-1)' = 2.7 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.094 s^-1; already in s^-1, no unit conversion applies; normalized 0.094 s^(-1). Km: printed cell 3.4 uM; 3.4 / 1000 = 0.0034 mM; normalized 0.0034 mM. kcat/Km: printed cell 2.7 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.7 x 10^4 / 1000 = 27 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row R87A, AFL column group: kcat = 0.094 s^-1; Km = 3.4 uM; kcat/Km = 2.7 x 10^4 M^-1 s^-1.

row_label: Table 3, variant row 'R87A', AFL column group


enzyme_display_name: 2-isopropylmalate synthase

organism: Arabidopsis thaliana

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

proof_lines: kcat is 2.3 sec(-1) with 2-oxoisovalerate as substrate (PubMed:17189332). kcat is 1.9 sec(-1) with acetyl-CoA as substrate (PubMed:17189332).

enzyme: 2-isopropylmalate synthase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 3.5 sec(-1) for 3-methyl-2-oxobutanoate and 2.1 for acetyl-CoA.


organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)

proof_lines: kcat is 13 sec(-1) for 3-methyl-2-oxobutanoate, 3.4 sec(-1) for 2-oxobutanoate, 0.027 sec(-1) for 3-methyl-2-oxopentanoate.


enzyme_display_name: methylthioalkylmalate synthase

organism: Eutrema japonicum

proof_lines: MAM1-2 is 2000 time faster than MAM1-1 to catalyze the conversion of 6-(methylsulfinyl)hexylisothiocyanate into 2-(2-methylsulfanyl)ethylmalate.

enzyme: methylthioalkylmalate synthase


proof_lines: MAM1-1 is 2000 time slower than MAM1-2 to catalyze the conversion of 6-(methylsulfinyl)hexylisothiocyanate into 2-(2-methylsulfanyl)ethylmalate.


organism: Fragaria ananassa

substrate_name: cinnamic acid

proof_lines: The kinetic constants are determined for the recombinant His(6)-tagged protein.

substrate: cinnamic acid


organism: Punica granatum

substrate_name: gallic acid (at pH 5.0 and 30 degrees Celsius)

proof_lines: kcat is 0.55 sec(-1) with gallic acid as substrate. kcat is 0.6 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 1.35 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.89 sec(-1) with caffeic acid as substrate. kcat is


proof_lines: kcat is 0.52 sec(-1) with gallic acid as substrate. kcat is 0.61 sec(-1) with 4-hydroxybenzoic acid as substrate. kcat is 0.76 sec(-1) with 3,4-dihydroxybenzoic acid as substrate. kcat is 0.64 sec(-1) with caffeic acid as substrate. kcat is

substrate: gallic acid (at pH 5.0 and 30 degrees Celsius)


organism: Mus musculus

proof_lines: Relative Vmax is 4:2:1 for Gal-beta-1,3-GlcNAc, Gal-beta-1,4-GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.


proof_lines: Relative Vmax is 2:5:1 for Gal-beta-1,3-GlcNAc, Gal-beta-1,4-GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.


proof_lines: kcat is 32 sec(-1) for CMP-N-acetyl-beta-neuraminate (alpha2,3-sialyltransferase activity) (PubMed:16351087). kcat is 47 sec(-1) for LacMU (alpha2,3-sialyltransferase activity) (PubMed:16351087). kcat is 227 sec(-1) for alpha-Neu5Ac-(2->3)-


organism: Bacillus subtilis (strain 168)

substrate_name: L-cysteine

proof_lines: In the presence of dithiothreitol, which regenerates the second reaction product SufU.S.

substrate: L-cysteine


organism: Mycobacterium tuberculosis

substrate_name: H+; Desmyoinositol mycothione; NADPH

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

proof_lines: des-myo-inositol mycothione as second substrate

substrate: H+; Desmyoinositol mycothione; NADPH


organism: Homo sapiens

proof_lines: pH and temperature not specified in the publication


organism: myxoma virus


organism: Pasteurella multocida

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M144D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M144D, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: mutant enzyme M144D, using 4-methylumbelliferyl beta-Lewis x as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C

proof_lines: mutant enzyme M144D, using 4-methylumbelliferyl beta-lactoside as cosubstrate, in Tris-HCl buffer (200 mM, pH 8.5), at 37°C


column_label: Table 2, acceptor row LacbMU, M144H column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 0.79 mM; kcat cell = 21 s^-1; kcat/Km cell = 27 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LacβMU | PmST1 M144H, the M144H single mutant of Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LacβMU, M144H column block: Km 0.79 mM | kcat 21 s^-1 | kcat/Km printed cell 27 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 0.79 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 0.79 mM. kcat: printed cell 21 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 21.0 s^(-1). kcat/Km: printed cell 27 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 27.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LacbMU, M144H column block: Km = 0.79 mM; kcat = 21 s^-1; printed kcat/Km = 27 s^-1 mM^-1.


column_label: Table 2, acceptor row LexbMU, WT column block; columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1); Km cell = 17 mM; kcat cell = 6.7 s^-1; kcat/Km cell = 0.38 s^-1 mM^-1; author manuscript page 18 (PDF page 18). captured primary segment: LexβMU | wild-type PmST1, the recombinant Pasteurella multocida sialyltransferase 1 | Table 2, acceptor row LexβMU, WT column block: Km 17 mM | kcat 6.7 s^-1 | kcat/Km printed cell 0.38 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 17 mM; the printed unit is already mM, so no unit conversion applies and the cell carries over as 17.0 mM. kcat: printed cell 6.7 s^-1; the printed turnover column is already per second, so no unit conversion applies and the cell carries over as 6.7 s^(-1). kcat/Km: printed cell 0.38 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 0.38 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, acceptor row LexbMU, WT column block: Km = 17 mM; kcat = 6.7 s^-1; printed kcat/Km = 0.38 s^-1 mM^-1.