substrate_name: N-Acetyl-L-methionine

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-acetyl-L-methionine'; column 'kcat, s-1' = 1700; column 'Km, mM' = 0.81; column 'kcat/Km, M-1 s-1' = 2.1 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1700 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 1700.0 s^(-1). Km: printed Table 3 cell 0.81 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 0.81 mM. kcat/Km: printed Table 3 cell 2.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.1 x 10^6 / 1000 = 2100.0 s^-1 mM^-1. Quotient disclosure for this cell group: 1700 / 0.81 = 2098.7654320987654 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-acetyl-L-methionine: kcat = 1700 s^-1; Km = 0.81 mM; printed kcat/Km = 2.1 x 10^6 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-acetyl-L-methionine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

substrate: N-Acetyl-L-methionine


enzyme_display_name: acetylornithine deacetylase

organism: Escherichia coli

substrate_name: N-Acetyl-DL-serine

source_db: oed

verification_status: verified

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: UniProtKB:P23908 direct lookup

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

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

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM KPi

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-acetyl-DL-serine'; column 'kcat, s-1' = 80; column 'Km, mM' = 6.7; column 'kcat/Km, M-1 s-1' = 1.2 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 80 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 80.0 s^(-1). Km: printed Table 3 cell 6.7 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 6.7 mM. kcat/Km: printed Table 3 cell 1.2 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^4 / 1000 = 12.0 s^-1 mM^-1. Quotient disclosure for this cell group: 80 / 6.7 = 11.940298507462686 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-acetyl-DL-serine: kcat = 80 s^-1; Km = 6.7 mM; printed kcat/Km = 1.2 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-acetyl-DL-serine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

table_label: Table 3: Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase (Biochemistry 2000, 39(6):1285-1293); printed column heads substrate, kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

data_origin: experimental

enzyme: acetylornithine deacetylase

substrate: N-Acetyl-DL-serine

status: verified

source: oed


verification_status: unverified

status: unverified


substrate_name: N-Acetyl-L-asparagine

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-acetyl-L-asparagine'; column 'kcat, s-1' = 92; column 'Km, mM' = 8.3; column 'kcat/Km, M-1 s-1' = 1.1 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 92 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 92.0 s^(-1). Km: printed Table 3 cell 8.3 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 8.3 mM. kcat/Km: printed Table 3 cell 1.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^4 / 1000 = 11.0 s^-1 mM^-1. Quotient disclosure for this cell group: 92 / 8.3 = 11.08433734939759 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-acetyl-L-asparagine: kcat = 92 s^-1; Km = 8.3 mM; printed kcat/Km = 1.1 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-acetyl-L-asparagine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

substrate: N-Acetyl-L-asparagine


enzyme_display_name: ATP diphosphatase

substrate_name: H2O; dATP

kcat_over_km_display: Not reported

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

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEY3 exact accession FASTA, fetched during review and applied mutation signature A141E to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: ATP diphosphatase(Enzyme) mutant A141E His-tagged

enzyme: ATP diphosphatase

substrate: H2O; dATP


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AEY3 and applied mutation signature A141E to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Ec', Enzyme cell 'E141', Mg2+ cell '5' and Substrate cell '8-oxo-dGTP'; column 'Vmax (nm/min/ug)' = 0.22 +/- 0.01; column 'kcat (min^-1)' = 6.9 +/- 0.3; column 'Km (mM)' = 0.42 +/- 0.06; column 'kcat/Km (min^-1 mM^-1)' = 17.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.9 min^-1; one min^-1 is 1/60 s^-1, so 6.9 / 60 = 0.115 s^(-1). Km: printed Table 1 cell 0.42 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.42 mM. kcat/Km: printed Table 1 cell 17 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 17 / 60 = 0.2833333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Ec, Enzyme E141, Mg2+ 5 mM, Substrate 8-oxo-dGTP: kcat cell 6.9 +/- 0.3 min^-1; Km cell 0.42 +/- 0.06 mM; printed kcat/Km cell 17 min^-1 mM^-1; Vmax cell 0.22 +/- 0.01 nm/min/ug.

table_label: Table 1: Kinetic parameters of MazG proteins analyzed in this study (J. Biol. Chem. 2010, volume 285, number 36, pages 28076-28085)

status: corrected


sequence_source: UniProtKB:P0AEY3 exact accession FASTA, fetched during review

column_label: TABLE 1, species block 'Ec', enzyme 'WT', Mg2+ 5 mM, substrate row '8-oxo-dGTP': Vmax (nm/min/ug) = 0.23 +/- 0.01; kcat (min^-1) = 7.2 +/- 0.4; Km (mM) = 0.36 +/- 0.05; kcat/km (min^-1 mM^-1) = 20.

normalized_value_unit_evidence: kcat: the printed TABLE 1 cell is 7.2 min^-1; 7.2 / 60 = 0.12 s^(-1) exactly; the exported value is 0.12 s^(-1). Km: the printed TABLE 1 cell is 0.36 mM, already the export unit; the exported value is 0.36 mM. kcat/Km: the printed TABLE 1 kcat/km cell is 20 min^-1 mM^-1; 20 / 60 = 0.3333333333333333 s^(-1)*mM^(-1); the exported value is 0.3333333333333333 s^(-1)*mM^(-1). The cited TABLE 1 row prints one further numeric column, Vmax = 0.23 +/- 0.01 nm/min/ug, a specific activity per microgram of enzyme; see row_metrics_coverage.

table_label: TABLE 1. Kinetic parameters of MazG proteins analyzed in this study


substrate_name: dUTP

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Ec', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'dUTP'; column 'Vmax (nm/min/ug)' = 1.9 +/- 0.1; column 'kcat (min^-1)' = 60.3 +/- 3.1; column 'Km (mM)' = 0.71 +/- 0.1; column 'kcat/Km (min^-1 mM^-1)' = 85.

normalized_value_unit_evidence: kcat: printed Table 1 cell 60.3 min^-1; one min^-1 is 1/60 s^-1, so 60.3 / 60 = 1.005 s^(-1). Km: printed Table 1 cell 0.71 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.71 mM. kcat/Km: printed Table 1 cell 85 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 85 / 60 = 1.4166666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Ec, Enzyme WT, Mg2+ 5 mM, Substrate dUTP: kcat cell 60.3 +/- 3.1 min^-1; Km cell 0.71 +/- 0.1 mM; printed kcat/Km cell 85 min^-1 mM^-1; Vmax cell 1.9 +/- 0.1 nm/min/ug.

substrate: dUTP


substrate_name: dATP; H2O

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Ec', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'dATP'; column 'Vmax (nm/min/ug)' = 1.9 +/- 0.1; column 'kcat (min^-1)' = 59.8 +/- 2.3; column 'Km (mM)' = 0.34 +/- 0.05; column 'kcat/Km (min^-1 mM^-1)' = 174.

normalized_value_unit_evidence: kcat: printed Table 1 cell 59.8 min^-1; one min^-1 is 1/60 s^-1, so 59.8 / 60 = 0.9966666666666666 s^(-1), carried here at the seven-significant-digit precision this export uses for the metric, 0.9966667 s^(-1). Km: printed Table 1 cell 0.34 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.34 mM. kcat/Km: printed Table 1 cell 174 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 174 / 60 = 2.9 s^(-1)*mM^(-1). Vmax: printed Table 1 cell 1.9 nm/min/ug; 1.9 nanomoles per minute per microgram is 0.0000000019 mol / 60 s / 0.000001 g = 0.00003166667 mol*s^(-1)*g^(-1).

raw_value_unit_evidence: Table 1, Species Ec, Enzyme WT, Mg2+ 5 mM, Substrate dATP: kcat cell 59.8 +/- 2.3 min^-1; Km cell 0.34 +/- 0.05 mM; printed kcat/Km cell 174 min^-1 mM^-1; Vmax cell 1.9 +/- 0.1 nm/min/ug.

substrate: dATP; H2O


substrate_name: dATP

normalized_value_unit_evidence: kcat: printed Table 1 cell 59.8 min^-1; one min^-1 is 1/60 s^-1, so 59.8 / 60 = 0.9966666666666666 s^(-1). Km: printed Table 1 cell 0.34 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.34 mM. kcat/Km: printed Table 1 cell 174 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 174 / 60 = 2.9 s^(-1)*mM^(-1).

row_label: Table 1, row with Species cell 'Ec', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'dATP'

substrate: dATP


column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Ec', Enzyme cell 'E141', Mg2+ cell '5' and Substrate cell 'dATP'; column 'Vmax (nm/min/ug)' = 1.8 +/- 0.1; column 'kcat (min^-1)' = 57.8 +/- 2.4; column 'Km (mM)' = 0.37 +/- 0.05; column 'kcat/Km (min^-1 mM^-1)' = 156.

normalized_value_unit_evidence: kcat: printed Table 1 cell 57.8 min^-1; one min^-1 is 1/60 s^-1, so 57.8 / 60 = 0.9633333333333333 s^(-1). Km: printed Table 1 cell 0.37 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.37 mM. kcat/Km: printed Table 1 cell 156 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 156 / 60 = 2.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Ec, Enzyme E141, Mg2+ 5 mM, Substrate dATP: kcat cell 57.8 +/- 2.4 min^-1; Km cell 0.37 +/- 0.05 mM; printed kcat/Km cell 156 min^-1 mM^-1; Vmax cell 1.8 +/- 0.1 nm/min/ug.


organism: Mycobacterium smegmatis

sequence_source: UniProtKB:A0R3C4 exact accession FASTA, fetched during review

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Ms', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell '8-oxo-dGTP'; column 'Vmax (nm/min/ug)' = 0.16 +/- 0.01; column 'kcat (min^-1)' = 5.9 +/- 0.2; column 'Km (mM)' = 0.16 +/- 0.02; column 'kcat/Km (min^-1 mM^-1)' = 36.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.9 min^-1; one min^-1 is 1/60 s^-1, so 5.9 / 60 = 0.09833333333333334 s^(-1). Km: printed Table 1 cell 0.16 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.16 mM. kcat/Km: printed Table 1 cell 36 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 36 / 60 = 0.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Ms, Enzyme WT, Mg2+ 5 mM, Substrate 8-oxo-dGTP: kcat cell 5.9 +/- 0.2 min^-1; Km cell 0.16 +/- 0.02 mM; printed kcat/Km cell 36 min^-1 mM^-1; Vmax cell 0.16 +/- 0.01 nm/min/ug.


substrate_name: CTP

sequence_source: UniProtKB REST A0R3C4 direct lookup on 2026-06-13

substrate: CTP


substrate_name: GTP

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Ms', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'GTP'; column 'Vmax (nm/min/ug)' = 3.1 +/- 0.2; column 'kcat (min^-1)' = 115 +/- 6.2; column 'Km (mM)' = 0.9 +/- 0.1; column 'kcat/Km (min^-1 mM^-1)' = 127.

normalized_value_unit_evidence: kcat: printed Table 1 cell 115.0 min^-1; one min^-1 is 1/60 s^-1, so 115.0 / 60 = 1.9166666666666667 s^(-1). Km: printed Table 1 cell 0.9 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.9 mM. kcat/Km: printed Table 1 cell 127 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 127 / 60 = 2.1166666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Ms, Enzyme WT, Mg2+ 5 mM, Substrate GTP: kcat cell 115 +/- 6.2 min^-1; Km cell 0.9 +/- 0.1 mM; printed kcat/Km cell 127 min^-1 mM^-1; Vmax cell 3.1 +/- 0.2 nm/min/ug.

substrate: GTP


substrate_name: H2O; GTP

sequence_source: UniProtKB REST A0R3C4 direct lookup on 2026-06-13 provides canonical context only; exact His-tagged A222E construct sequence is unresolved

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: ATP diphosphatase(Enzyme) mutant A222E His-tagged

substrate: H2O; GTP


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB REST P96379 direct lookup on 2026-06-13


column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Mt', Enzyme cell 'WT', Mg2+ cell '20' and Substrate cell 'GTP'; column 'Vmax (nm/min/ug)' = 2.3 +/- 0.2; column 'kcat (min^-1)' = 85.5 +/- 6.4; column 'Km (mM)' = 0.6 +/- 0.1; column 'kcat/Km (min^-1 mM^-1)' = 134.

normalized_value_unit_evidence: kcat: printed Table 1 cell 85.5 min^-1; one min^-1 is 1/60 s^-1, so 85.5 / 60 = 1.425 s^(-1). Km: printed Table 1 cell 0.6 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.6 mM. kcat/Km: printed Table 1 cell 134 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 134 / 60 = 2.2333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Mt, Enzyme WT, Mg2+ 20 mM, Substrate GTP: kcat cell 85.5 +/- 6.4 min^-1; Km cell 0.6 +/- 0.1 mM; printed kcat/Km cell 134 min^-1 mM^-1; Vmax cell 2.3 +/- 0.2 nm/min/ug.


column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Mt', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell '8-oxo-dGTP'; column 'Vmax (nm/min/ug)' = 0.14 +/- 0.01; column 'kcat (min^-1)' = 5.2 +/- 0.2; column 'Km (mM)' = 0.11 +/- 0.02; column 'kcat/Km (min^-1 mM^-1)' = 47.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.2 min^-1; one min^-1 is 1/60 s^-1, so 5.2 / 60 = 0.08666666666666667 s^(-1). Km: printed Table 1 cell 0.11 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.11 mM. kcat/Km: printed Table 1 cell 47 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 47 / 60 = 0.7833333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Mt, Enzyme WT, Mg2+ 5 mM, Substrate 8-oxo-dGTP: kcat cell 5.2 +/- 0.2 min^-1; Km cell 0.11 +/- 0.02 mM; printed kcat/Km cell 47 min^-1 mM^-1; Vmax cell 0.14 +/- 0.01 nm/min/ug.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P96379 and applied mutation signature A219E to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Mt', Enzyme cell 'E219', Mg2+ cell '20' and Substrate cell 'GTP'; column 'Vmax (nm/min/ug)' = 0.8 +/- 0.1; column 'kcat (min^-1)' = 30.7 +/- 3.7; column 'Km (mM)' = 1.2 +/- 0.3; column 'kcat/Km (min^-1 mM^-1)' = 29.

normalized_value_unit_evidence: kcat: printed Table 1 cell 30.7 min^-1; one min^-1 is 1/60 s^-1, so 30.7 / 60 = 0.5116666666666666 s^(-1). Km: printed Table 1 cell 1.2 mM; the printed unit is already mM, so no unit conversion applies and the value stays 1.2 mM. kcat/Km: printed Table 1 cell 29 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 29 / 60 = 0.48333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Mt, Enzyme E219, Mg2+ 20 mM, Substrate GTP: kcat cell 30.7 +/- 3.7 min^-1; Km cell 1.2 +/- 0.3 mM; printed kcat/Km cell 29 min^-1 mM^-1; Vmax cell 0.8 +/- 0.1 nm/min/ug.


substrate_name: N-Acetyl-L-cysteine

sequence_source: UniProtKB:P23908 direct REST accession check on 2026-06-13

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-acetyl-L-cysteine'; column 'kcat, s-1' = 100; column 'Km, mM' = 13; column 'kcat/Km, M-1 s-1' = 8 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 100 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 100.0 s^(-1). Km: printed Table 3 cell 13 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 13.0 mM. kcat/Km: printed Table 3 cell 8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8 x 10^3 / 1000 = 8.0 s^-1 mM^-1. Quotient disclosure for this cell group: 100 / 13 = 7.6923076923076925 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-acetyl-L-cysteine: kcat = 100 s^-1; Km = 13 mM; printed kcat/Km = 8 x 10^3 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-acetyl-L-cysteine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

substrate: N-Acetyl-L-cysteine


substrate_name: N-Acetyl-L-lysine

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-acetyl-L-lysine'; column 'kcat, s-1' = 370; column 'Km, mM' = 4.1; column 'kcat/Km, M-1 s-1' = 9.0 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 370 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 370.0 s^(-1). Km: printed Table 3 cell 4.1 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 4.1 mM. kcat/Km: printed Table 3 cell 9.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.0 x 10^4 / 1000 = 90.0 s^-1 mM^-1. Quotient disclosure for this cell group: 370 / 4.1 = 90.2439024390244 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-acetyl-L-lysine: kcat = 370 s^-1; Km = 4.1 mM; printed kcat/Km = 9.0 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-acetyl-L-lysine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

substrate: N-Acetyl-L-lysine


substrate_name: N-Formyl-L-methionine

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-formyl-L-methionine'; column 'kcat, s-1' = 1800; column 'Km, mM' = 2.0; column 'kcat/Km, M-1 s-1' = 9.0 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1800 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 1800.0 s^(-1). Km: printed Table 3 cell 2.0 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 2.0 mM. kcat/Km: printed Table 3 cell 9.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.0 x 10^5 / 1000 = 900.0 s^-1 mM^-1. Quotient disclosure for this cell group: 1800 / 2.0 = 900.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-formyl-L-methionine: kcat = 1800 s^-1; Km = 2.0 mM; printed kcat/Km = 9.0 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-formyl-L-methionine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

substrate: N-Formyl-L-methionine


substrate_name: N-Acetyl-L-alanine

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-acetyl-L-alanine'; column 'kcat, s-1' = 120; column 'Km, mM' = 1.0; column 'kcat/Km, M-1 s-1' = 1.2 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 120 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 120.0 s^(-1). Km: printed Table 3 cell 1.0 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 1.0 mM. kcat/Km: printed Table 3 cell 1.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^5 / 1000 = 120.0 s^-1 mM^-1. Quotient disclosure for this cell group: 120 / 1.0 = 120.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-acetyl-L-alanine: kcat = 120 s^-1; Km = 1.0 mM; printed kcat/Km = 1.2 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-acetyl-L-alanine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

substrate: N-Acetyl-L-alanine


substrate_name: N-Chloroacetylglycine

smiles: O=C(O)CN=C(O)CCl

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-chloroacetylglycine'; column 'kcat, s-1' = 130; column 'Km, mM' = 7.0; column 'kcat/Km, M-1 s-1' = 1.9 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 130 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 130.0 s^(-1). Km: printed Table 3 cell 7.0 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 7.0 mM. 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. Quotient disclosure for this cell group: 130 / 7.0 = 18.571428571428573 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-chloroacetylglycine: kcat = 130 s^-1; Km = 7.0 mM; printed kcat/Km = 1.9 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-chloroacetylglycine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

substrate: N-Chloroacetylglycine


substrate_name: N-Acetyl-L-leucine

column_label: Table 3 (Substrate Specificity of Purified E. coli N-Acetylorntihine Deacetylase), substrate line 'N-alpha-acetyl-L-leucine'; column 'kcat, s-1' = 420; column 'Km, mM' = 7.0; column 'kcat/Km, M-1 s-1' = 6.0 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 420 s^-1; the printed column head is kcat, s-1, so no unit conversion applies and the paper value is 420.0 s^(-1). Km: printed Table 3 cell 7.0 mM; the printed column head is Km, mM, so no unit conversion applies and the paper value is 7.0 mM. kcat/Km: printed Table 3 cell 6.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.0 x 10^4 / 1000 = 60.0 s^-1 mM^-1. Quotient disclosure for this cell group: 420 / 7.0 = 60.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate line N-alpha-acetyl-L-leucine: kcat = 420 s^-1; Km = 7.0 mM; printed kcat/Km = 6.0 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate line N-alpha-acetyl-L-leucine, printed columns kcat (s^-1), Km (mM) and kcat/Km (M^-1 s^-1)

substrate: N-Acetyl-L-leucine


substrate_name: H2O; N2-Acetyl-L-ornithine

substrate: H2O; N2-Acetyl-L-ornithine


organism: Sinorhizobium meliloti

source_db: brenda

kcat_display: Not reported

sequence_source: UniProtKB:Q92Y75 direct REST accession check on 2026-06-13

source: brenda


enzyme_display_name: phosphate acyltransferase

organism: Bacillus subtilis

substrate_name: palmitoyl-[acyl-carrier protein]

sequence_source: UniProtKB reviewed P71018 (PLSX_BACSU) direct lookup, fetched 2026-06-13

smiles: *SC(=O)CCCCCCCCCCCCCCC

enzyme: phosphate acyltransferase

substrate: palmitoyl-[acyl-carrier protein]


substrate_name: palmitoyl phosphate

smiles: CCCCCCCCCCCCCCCC(=O)OP(=O)(O)O

substrate: palmitoyl phosphate


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

substrate_name: orthophosphate

source_db: uniprot

substrate: orthophosphate

source: uniprot


organism: Escherichia coli (strain K12)


substrate_name: dATP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 8-oxo-dGTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate: 8-oxo-dGTP (at pH 9.6 and at 37 degrees Celsius in the presence of 5 mM magnesium)


substrate_name: dTTP

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Mt', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'dTTP'; column 'Vmax (nm/min/ug)' = 1.6 +/- 0.1; column 'kcat (min^-1)' = 58.4 +/- 3.9; column 'Km (mM)' = 1.3 +/- 0.2; column 'kcat/Km (min^-1 mM^-1)' = 44.

normalized_value_unit_evidence: kcat: printed Table 1 cell 58.4 min^-1; one min^-1 is 1/60 s^-1, so 58.4 / 60 = 0.9733333333333333 s^(-1). Km: printed Table 1 cell 1.3 mM; the printed unit is already mM, so no unit conversion applies and the value stays 1.3 mM. kcat/Km: printed Table 1 cell 44 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 44 / 60 = 0.7333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Mt, Enzyme WT, Mg2+ 5 mM, Substrate dTTP: kcat cell 58.4 +/- 3.9 min^-1; Km cell 1.3 +/- 0.2 mM; printed kcat/Km cell 44 min^-1 mM^-1; Vmax cell 1.6 +/- 0.1 nm/min/ug.

substrate: dTTP


substrate_name: dATP

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Mt', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'dATP'; column 'Vmax (nm/min/ug)' = 1.7 +/- 0.2; column 'kcat (min^-1)' = 60.4 +/- 7.2; column 'Km (mM)' = 1.2 +/- 0.3; column 'kcat/Km (min^-1 mM^-1)' = 52.

normalized_value_unit_evidence: kcat: printed Table 1 cell 60.4 min^-1; one min^-1 is 1/60 s^-1, so 60.4 / 60 = 1.0066666666666666 s^(-1). Km: printed Table 1 cell 1.2 mM; the printed unit is already mM, so no unit conversion applies and the value stays 1.2 mM. kcat/Km: printed Table 1 cell 52 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 52 / 60 = 0.8666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Mt, Enzyme WT, Mg2+ 5 mM, Substrate dATP: kcat cell 60.4 +/- 7.2 min^-1; Km cell 1.2 +/- 0.3 mM; printed kcat/Km cell 52 min^-1 mM^-1; Vmax cell 1.7 +/- 0.2 nm/min/ug.


substrate_name: GTP; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P96379 with A219E reconstructed from UniProt mutagenesis feature and applied mutation signature A219E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ATP diphosphatase(Enzyme) mutant A219E His-tagged

substrate: GTP; H2O


substrate_name: dGTP

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Mt', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'dGTP'; column 'Vmax (nm/min/ug)' = 1.4 +/- 0.1; column 'kcat (min^-1)' = 51.8 +/- 2.1; column 'Km (mM)' = 0.4 +/- 0.1; column 'kcat/Km (min^-1 mM^-1)' = 130.

normalized_value_unit_evidence: kcat: printed Table 1 cell 51.8 min^-1; one min^-1 is 1/60 s^-1, so 51.8 / 60 = 0.8633333333333333 s^(-1). Km: printed Table 1 cell 0.4 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.4 mM. kcat/Km: printed Table 1 cell 130 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 130 / 60 = 2.1666666666666665 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Mt, Enzyme WT, Mg2+ 5 mM, Substrate dGTP: kcat cell 51.8 +/- 2.1 min^-1; Km cell 0.4 +/- 0.1 mM; printed kcat/Km cell 130 min^-1 mM^-1; Vmax cell 1.4 +/- 0.1 nm/min/ug.

substrate: dGTP


substrate_name: ATP

assay_conditions_summary: pH 9.6; 310.15 K; cofactor ATP

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Mt', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'ATP'; column 'Vmax (nm/min/ug)' = 1.3 +/- 0.1; column 'kcat (min^-1)' = 48.4 +/- 5.1; column 'Km (mM)' = 1.6 +/- 0.3; column 'kcat/Km (min^-1 mM^-1)' = 31.

normalized_value_unit_evidence: kcat: printed Table 1 cell 48.4 min^-1; one min^-1 is 1/60 s^-1, so 48.4 / 60 = 0.8066666666666666 s^(-1). Km: printed Table 1 cell 1.6 mM; the printed unit is already mM, so no unit conversion applies and the value stays 1.6 mM. kcat/Km: printed Table 1 cell 31 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 31 / 60 = 0.5166666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Mt, Enzyme WT, Mg2+ 5 mM, Substrate ATP: kcat cell 48.4 +/- 5.1 min^-1; Km cell 1.6 +/- 0.3 mM; printed kcat/Km cell 31 min^-1 mM^-1; Vmax cell 1.3 +/- 0.1 nm/min/ug.

substrate: ATP


substrate_name: UTP

column_label: Table 1 (Kinetic parameters of MazG proteins analyzed in this study), Table 1, row with Species cell 'Mt', Enzyme cell 'WT', Mg2+ cell '5' and Substrate cell 'UTP'; column 'Vmax (nm/min/ug)' = 0.5 +/- 0.04; column 'kcat (min^-1)' = 16.8 +/- 1.5; column 'Km (mM)' = 0.6 +/- 0.2; column 'kcat/Km (min^-1 mM^-1)' = 26.

normalized_value_unit_evidence: kcat: printed Table 1 cell 16.8 min^-1; one min^-1 is 1/60 s^-1, so 16.8 / 60 = 0.28 s^(-1). Km: printed Table 1 cell 0.6 mM; the printed unit is already mM, so no unit conversion applies and the value stays 0.6 mM. kcat/Km: printed Table 1 cell 26 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 26 / 60 = 0.43333333333333335 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Species Mt, Enzyme WT, Mg2+ 5 mM, Substrate UTP: kcat cell 16.8 +/- 1.5 min^-1; Km cell 0.6 +/- 0.2 mM; printed kcat/Km cell 26 min^-1 mM^-1; Vmax cell 0.5 +/- 0.04 nm/min/ug.

substrate: UTP


substrate_name: N-alpha-acetyl-L-ornithine

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; 298.15 K; buffer 50 mM Chelex-100 treated sodium phosphate

proof_lines: in 50 mM Chelex-100 treated sodium phosphate buffer, pH 7.5, at 25°C, in the presence of Mn2+

proof_lines: in the presence of one equivalent of Zn(II), pH 7.5, 25°C

substrate: N-alpha-acetyl-L-ornithine


organism: Badhamia polycephala


organism: Mus musculus

proof_lines:
in presence of 2 mM ZnCl2
without added metal ions
in presence of ZnCl2 and CaCl2


organism: Rattus norvegicus

substrate_name: GTP

assay_conditions_summary: pH 8; cofactor ATP

proof_lines:
with 0.1 mM free Ca2+, pH 8
competitive inhibition

substrate: GTP


organism: Schistosoma mansoni

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: 37°C, pH 7.4, inhibition of ATP hydrolysis


organism: Sus scrofa

assay_conditions_summary: pH 7.3; cofactor ATP

proof_lines:
vesicle associated enzyme at pH 7.3
vesicle associated enzyme at pH 9.9


sequence_source: UniProtKB REST lookup for A0R3C4 on 2026-06-13


substrate_name: dCTP

substrate: dCTP


substrate_name: H2O; GTP

substrate: H2O; GTP


substrate: dATP


sequence_variant_note: Resolved canonical sequence from UniProtKB A0R3C4 canonical sequence reconstructed as A222E on 2026-06-13 using UniProt mutagenesis feature and PMID 20529853 Table 1 and applied mutation signature A222E to reconstruct the assayed variant sequence.


organism: Streptomyces niveus

substrate_name: menadione hydroquinol

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 canonical sequence, residue 281 E->K reconstructed during review and applied mutation signature E281K to reconstruct the assayed variant sequence.

substrate: menadione hydroquinol


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 canonical sequence, residue 281 E->D reconstructed during review and applied mutation signature E281D to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9L9F1 canonical sequence, residue 281 E->D reconstructed during review


organism: Streptomyces roseochromogenus subsp. oscitans

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

sequence_source: UniProtKB reviewed accession Q8GHB2 direct REST lookup

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

source_databases_merged: brenda skid


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


proof_lines:
pH 7.5, 30°C, wild-type
pH 7.5, 30°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9L9F1 REST FASTA checked 2026-06-14 and applied mutation signature E281M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9L9F1 REST FASTA checked 2026-06-14 and applied mutation signature E281S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9L9F1 REST FASTA checked 2026-06-14

column_label: Table 1 (Kinetic parameters of NovQ and its mutants), row 'WT NovQ'; column 'Km (uM)' = 173.7; column 'Vmax (nM min^-1)' = 278.1; column 'kcat (s^-1)' = 0.038; column 'kcat/Km (M^-1 s^-1)' = 219.

normalized_value_unit_evidence: Km: printed Table 1 cell 173.7 uM; 173.7 / 1000 = 0.1737 mM; the exported value is 0.1737 mM. kcat: printed Table 1 cell 0.038 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 0.038 s^(-1). kcat/Km: printed Table 1 cell 219 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 219 / 1000 = 0.219 s^-1 mM^-1. The quotient of the same row's two printed component cells is 0.038 / 0.1737 = 0.21876799078871617 s^-1 mM^-1, which is the exported catalytic efficiency, and the printed cell 219 M^-1 s^-1 is the nearest integer to the same quotient expressed in the printed unit, 218.7679907887162 M^-1 s^-1.

raw_value_unit_evidence: Table 1, row 'WT NovQ': Km = 173.7 uM; kcat = 0.038 s^-1; printed kcat/Km = 219 M^-1 s^-1.

row_label: Table 1, row 'WT NovQ'

table_label: Table 1: Kinetic parameters of NovQ and its mutants (Applied Microbiology and Biotechnology 2020, 104:4371-4382)


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9L9F1 REST FASTA checked 2026-06-14 and applied mutation signature E281Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9L9F1 REST FASTA checked 2026-06-14 and applied mutation signature E281A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9L9F1 REST FASTA checked 2026-06-14 and applied mutation signature E281V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P76491 reviewed FASTA checked 2026-06-14; V30A reconstructed from canonical residue V30. and applied mutation signature V30A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P76491 reviewed FASTA checked 2026-06-14; V37A reconstructed from canonical residue V37. and applied mutation signature V37A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P76491 reviewed FASTA checked 2026-06-14; E122A reconstructed from canonical residue E122. and applied mutation signature E122A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P76491 reviewed FASTA checked 2026-06-14; E122A reconstructed from canonical residue E122.


sequence_source: UniProtKB:P76491 reviewed FASTA checked 2026-06-14.

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


sequence_source: UniProtKB:P76491 reviewed FASTA checked 2026-06-14; V37A reconstructed from canonical residue V37.


sequence_source: UniProtKB:P76491 reviewed FASTA checked 2026-06-14; V30A reconstructed from canonical residue V30.


substrate_name: palmitoyl-[acyl-carrier protein]

sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 canonical sequence plus selected-record R114A mutation signature; direct residue check on 2026-06-14 and applied mutation signature R114A to reconstruct the assayed variant sequence.


substrate_name: holo-[acyl-carrier protein]

sequence_source: UniProtKB:P71018 canonical sequence direct lookup 2026-06-14

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

substrate: holo-[acyl-carrier protein]


substrate_name: phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 canonical sequence plus selected-record E236A mutation signature; direct residue check on 2026-06-14 and applied mutation signature E236A to reconstruct the assayed variant sequence.

substrate: phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 canonical sequence plus selected-record K184R mutation signature; direct residue check on 2026-06-14 and applied mutation signature K184R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 canonical sequence plus selected-record E181A mutation signature; direct residue check on 2026-06-14 and applied mutation signature E181A to reconstruct the assayed variant sequence.

substrate: palmitoyl-[acyl-carrier protein]


organism: Streptococcus pneumoniae

substrate_name: hexadecanoyl-[acyl-carrier protein]

sequence_source: UniProtKB:Q8DRN3 canonical sequence direct lookup 2026-06-14

substrate: hexadecanoyl-[acyl-carrier protein]


sequence_source: UniProtKB:Q9L9F1 canonical sequence direct lookup 2026-06-14


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9L9F1 canonical sequence plus selected-record E281R mutation signature; direct residue check on 2026-06-14 and applied mutation signature E281R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 FASTA direct lookup on 2026-06-14; row-specific E281M substitution reconstructed from the selected mutation signature after confirming canonical residue 281 is E. and applied mutation signature E281M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9L9F1 FASTA direct lookup on 2026-06-14.

normalized_value_unit_evidence: Km: printed Table 1 cell 173.7 uM; 173.7 / 1000 = 0.1737 mM; the exported value is 0.1737 mM. kcat: printed Table 1 cell 0.038 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 0.038 s^(-1). kcat/Km: printed Table 1 cell 219 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 219 / 1000 = 0.219 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 FASTA direct lookup on 2026-06-14; row-specific E281K substitution reconstructed from the selected BRENDA note after confirming canonical residue 281 is E. and applied mutation signature E281K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 FASTA direct lookup on 2026-06-14; row-specific E281S substitution reconstructed from the selected mutation signature after confirming canonical residue 281 is E. and applied mutation signature E281S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 FASTA direct lookup on 2026-06-14; row-specific E281T substitution reconstructed from the selected mutation signature after confirming canonical residue 281 is E. and applied mutation signature E281T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 FASTA direct lookup on 2026-06-14; row-specific E281T substitution reconstructed from the selected BRENDA note after confirming canonical residue 281 is E. and applied mutation signature E281T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 FASTA direct lookup on 2026-06-14; row-specific E281R substitution reconstructed from the selected BRENDA note after confirming canonical residue 281 is E. and applied mutation signature E281R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9L9F1 FASTA direct lookup on 2026-06-14; row-specific E281Q substitution reconstructed from the selected BRENDA note after confirming canonical residue 281 is E. and applied mutation signature E281Q to reconstruct the assayed variant sequence.


organism: Bacillus cereus

substrate_name: Hexa-N-acetylchitohexaose; n H2O

substrate: Hexa-N-acetylchitohexaose; n H2O


substrate_name: N,N'-Diacetylchitobiose; n H2O

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

substrate: N,N'-Diacetylchitobiose; n H2O


substrate_name: Penta-N-acetylchitopentaose; n H2O

substrate: Penta-N-acetylchitopentaose; n H2O


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


organism: Helicobacter pylori

substrate_name: Chitin; n H2O

substrate: Chitin; n H2O


substrate_name: Chitin

substrate: Chitin


organism: Mycobacterium tuberculosis

substrate_name: peptidoglycan-N-acetyl-D-glucosamine

substrate: peptidoglycan-N-acetyl-D-glucosamine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8DP63 plus direct I419G substitution and applied mutation signature I419G to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: H2O; 4-Nitrophenyl phosphate

sequence_source: UniProtKB reviewed entry P76491, retrieved 2026-06-14 from rest.uniprot.org

substrate: H2O; 4-Nitrophenyl phosphate


organism: Saccharomyces cerevisiae

substrate_name: 4-nitrophenyl phosphate

sequence_source: UniProtKB reviewed entry P53144, retrieved 2026-06-14 from rest.uniprot.org

substrate: 4-nitrophenyl phosphate


substrate_name: 5'-dTMP; 5'-dAMP; 5'-dCMP; 5'-dGMP; 4-nitrophenyl phosphate


substrate_name: H2O; 4-Nitrophenyl phosphate; dGMP; dTMP; dAMP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8DP63 FASTA/JSON via https://rest.uniprot.org/uniprotkb/Q8DP63, retrieved 2026-06-14 and applied mutation signature K304I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8DP63 FASTA/JSON via https://rest.uniprot.org/uniprotkb/Q8DP63, retrieved 2026-06-14 and applied mutation signature L302A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8DP63 FASTA/JSON via https://rest.uniprot.org/uniprotkb/Q8DP63, retrieved 2026-06-14

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


enzyme_display_name: GTP cyclohydrolase I

substrate_name: GTP

sequence_source: UniProtKB O25613 FASTA/JSON via https://rest.uniprot.org/uniprotkb/O25613, retrieved 2026-06-14

enzyme: GTP cyclohydrolase I

substrate: GTP


organism: Homo sapiens

substrate_name: AMP

substrate: AMP


organism: Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: dGMP

proof_lines: kcat is 1.2 sec(-1) with dGMP as substrate. kcat is 1.1 sec(-1) with dTMP as substrate. kcat is 1.0 sec(-1) with dAMP as substrate. kcat is 0.28 sec(-1) with dCMP as substrate.

substrate: dGMP


proof_lines: kcat is 3000 sec(-1) with GlcNAc(5) as substrate.


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

proof_lines: kcat is 0.55 sec(-1) with GlcNAc3 as substrate.


organism: Helicobacter pylori (strain ATCC 700392 / 26695)


organism: Dictyostelium discoideum


organism: Rattus norvegicus

substrate_name: Unknown

km_display: Not reported

substrate: Unknown


enzyme_display_name: GTP cyclohydrolase FolE2

organism: Bacillus subtilis

assay_conditions_summary: pH 8; buffer 100 mM HEPES, 100 mM KCl, 0.5 mM MnCl2, 1 mM DTT; cofactor MnCl2

proof_lines: isozyme GCYH-IB, in 100 mM HEPES (pH 8.0), 100 mM KCl, 0.5 mM MnCl2, 1 mM dithiothreitol, temperature not specified in the publication

enzyme: GTP cyclohydrolase FolE2


sequence_source: UniProtKB reviewed accession P76491; query lit_pubmed:15489502, organism Escherichia coli, gene yfbR


sequence_source: UniProtKB reviewed accession Q81EK9; selected source note enzyme BC1960; query lit_pubmed:15961396, organism Bacillus cereus, BC_1960


substrate_name: 4-yethylumbelliferyl acetate

sequence_source: UniProtKB reviewed accession Q8DP63; EC+organism query for Streptococcus pneumoniae EC 3.5.1.104; PMID 21501597 abstract names PgdA

substrate: 4-yethylumbelliferyl acetate


substrate_name: phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 FASTA checked 2026-06-14; variant reconstructed by applying R120A to the canonical sequence. and applied mutation signature R120A to reconstruct the assayed variant sequence.


substrate_name: palmitoyl-[acyl-carrier protein]

sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 FASTA checked 2026-06-14; variant reconstructed by applying K184A to the canonical sequence. and applied mutation signature K184A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 FASTA checked 2026-06-14; variant reconstructed by applying K233A to the canonical sequence. and applied mutation signature K233A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 FASTA checked 2026-06-14; variant reconstructed by applying N229Q to the canonical sequence. and applied mutation signature N229Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 FASTA checked 2026-06-14; variant reconstructed by applying K184Q to the canonical sequence. and applied mutation signature K184Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 FASTA checked 2026-06-14; variant reconstructed by applying E209A to the canonical sequence. and applied mutation signature E209A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 FASTA checked 2026-06-14; variant reconstructed by applying R73A to the canonical sequence. and applied mutation signature R73A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P71018 FASTA checked 2026-06-14; variant reconstructed by applying N229A to the canonical sequence. and applied mutation signature N229A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q13057 (COASY_HUMAN), direct REST lookup 2026-06-14

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


substrate_name: dephospho-CoA

substrate: dephospho-CoA


substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: diphosphate

substrate: diphosphate


substrate_name: Diphosphate; Dephospho-CoA

substrate: Diphosphate; Dephospho-CoA


sequence_source: UniProtKB reviewed accession P9WPA5 (COAD_MYCTU), direct REST lookup 2026-06-14

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: apparent value, at 25°C in 50 mM Tris (pH 8.0)


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed accession Q9I6D1 (COAD_PSEAE), direct REST lookup 2026-06-14

proof_lines:
pH 7.0, 25°C, recombinant enzyme
pH 7.0, 5°C, recombinant enzyme


organism: Sus scrofa

substrate_name: Dephospho-CoA; Diphosphate

sequence_source: UniProtKB reviewed accession Q8MIR4 (COASY_PIG), direct REST lookup 2026-06-14

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

substrate: Dephospho-CoA; Diphosphate


enzyme_display_name: phosphinothricin acetyltransferase

organism: Pseudomonas syringae pv. tomato

substrate_name: L-methionine sulfoximine

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q87ZV1 REST FASTA release 2026_02 plus selected record mutation signature R78F. and applied mutation signature R78F to reconstruct the assayed variant sequence.

proof_lines: mutant R78F, pH not specified in the publication, temperature not specified in the publication

enzyme: phosphinothricin acetyltransferase

substrate: L-methionine sulfoximine


substrate_name: DL-phosphinothricin

sequence_source: UniProtKB Q87ZV1 REST FASTA release 2026_02.

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

substrate: DL-phosphinothricin


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q87ZV1 REST FASTA release 2026_02 plus selected record mutation signature S32I. and applied mutation signature S32I to reconstruct the assayed variant sequence.

proof_lines: mutant S32I, pH not specified in the publication, temperature not specified in the publication


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)


organism: Streptomyces coelicolor

substrate_name: Phosphinothricin; Acetyl-CoA

sequence_source: UniProtKB reviewed entry P21861 REST FASTA release 2026_02.

assay_conditions_summary: cofactor CoA

substrate: Phosphinothricin; Acetyl-CoA


organism: Streptomyces hygroscopicus

substrate_name: Acetyl-CoA; Phosphinothricin

sequence_source: UniProtKB reviewed entry P16426 REST FASTA release 2026_02.

substrate: Acetyl-CoA; Phosphinothricin


enzyme_display_name: LL-diaminopimelate aminotransferase

organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed entry Q93ZN9 REST FASTA release 2026_02.

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

enzyme: LL-diaminopimelate aminotransferase


substrate_name: L-Glutamate

substrate: L-Glutamate


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:Q93ZN9; direct REST accession lookup on 2026-06-14; reviewed entry; length 461 aa

source_databases_merged: sabio_rk brenda skid


organism: Candidatus protochlamydia amoebophila

sequence_source: UniProtKB:Q6MDE0; direct REST accession lookup on 2026-06-14; reviewed entry; length 411 aa


organism: Chlamydia trachomatis

sequence_source: UniProtKB:O84395; direct REST accession lookup on 2026-06-14; reviewed entry; length 394 aa


organism: Chlamydomonas reinhardtii

substrate_name: tetrahydrodipicolinate

sequence_source: UniProtKB:A8IW39; direct REST accession lookup on 2026-06-14; unreviewed entry; length 441 aa

proof_lines: pH 7.6, temperature not specified in the publication

substrate: tetrahydrodipicolinate


organism: Desulfitobacterium hafniense

sequence_source: UniProtKB:Q18T09; direct REST accession lookup on 2026-06-14; reviewed entry; length 411 aa


organism: Leptospira interrogans

sequence_source: UniProtKB:Q72NJ3; direct REST accession lookup on 2026-06-14; reviewed entry; length 408 aa


organism: Methanothermobacter thermautotrophicus

sequence_source: UniProtKB:O26158; direct REST accession lookup on 2026-06-14; reviewed entry; length 410 aa


organism: Moorella thermoacetica

sequence_source: UniProtKB:Q2RK33; direct REST accession lookup on 2026-06-14; reviewed entry; length 390 aa


organism: Deinococcus radiodurans

substrate_name: Phosphinothricin

sequence_source: UniProt Q9RV48 FASTA checked directly on 2026-06-14

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

substrate: Phosphinothricin


organism: Geobacillus kaustophilus


substrate_name: L-methionine sulfone

substrate: L-methionine sulfone


sequence_source: UniProt Q5L2F2 FASTA checked directly on 2026-06-14


sequence_variant_note: Resolved canonical sequence from UniProt Q5KVT1 FASTA checked directly on 2026-06-14; M55ter reconstructed from selected source mutation note and applied mutation signature M55ter to reconstruct the assayed variant sequence.

mutation_type: truncation


organism: Nocardia sp. AB2253

substrate_name: L-phosphinothricin

substrate: L-phosphinothricin


organism: Pseudomonas aeruginosa

sequence_source: UniProt Q9HUU7 FASTA checked directly on 2026-06-14

proof_lines:
apparent Kcat
apparent KM


enzyme_display_name: heme oxygenase (biliverdin-producing)

organism: Homo sapiens

substrate_name: [reduced cytochrome P450 reductase]

sequence_variant_note: Resolved canonical sequence from UniProtKB:P09601 and applied mutation signature K149A to reconstruct the assayed variant sequence.

enzyme: heme oxygenase (biliverdin-producing)

substrate: [reduced cytochrome P450 reductase]


organism: Medicago sativa

substrate_name: heme

substrate: heme


organism: Rattus norvegicus

substrate_name: Heme; NADPH; O2

assay_conditions_summary: cofactor NADPH

substrate: Heme; NADPH; O2


organism: Thermus thermophilus

substrate_name: GTP

sequence_source: UniProtKB Q5SH52 direct accession lookup; RCSB 1WUQ entity 1 SIFTS alignment to UniProt Q5SH52

proof_lines:
pH 8.5, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=8.5

substrate: GTP


organism: Helicobacter pylori

substrate_name: GTP; H2O

sequence_source: UniProtKB O25613 direct REST/FASTA lookup on 2026-06-14

substrate: GTP; H2O


sequence_source: UniProtKB P30793 direct REST/FASTA lookup on 2026-06-14


organism: Listeria monocytogenes serotype 1/2a

sequence_source: UniProtKB Q8Y5X1 direct REST/FASTA lookup on 2026-06-14

proof_lines: pH and temperature not specified in the publication


organism: Neisseria gonorrhoeae

sequence_source: UniProtKB Q5F9K6 direct REST/FASTA lookup on 2026-06-14


organism: Nocardia iowensis

sequence_source: UniProtKB Q8GLS8 direct REST/FASTA lookup on 2026-06-14

proof_lines: recombinant enzyme expressed in Escherichia coli


organism: Plasmodium falciparum

sequence_source: UniProtKB O97071 direct REST/FASTA lookup on 2026-06-14


substrate_name: H2O; GTP

sequence_source: UniProtKB P22288 direct REST/FASTA lookup on 2026-06-14

substrate: H2O; GTP


organism: Solanum lycopersicum

ki_unit: mM

sequence_source: UniProtKB Q8VYU3 direct REST/FASTA lookup on 2026-06-14


organism: Gallus gallus

sequence_source: UniProtKB reviewed accession P14791, checked via https://rest.uniprot.org/uniprotkb/P14791.json


substrate_name: O2; Heme; NADPH

substrate: O2; Heme; NADPH


substrate_name: Unknown

sequence_source: UniProtKB reviewed accession P09601, checked via https://rest.uniprot.org/uniprotkb/P09601.json

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession P30519, checked via https://rest.uniprot.org/uniprotkb/P30519.json and applied mutation signature R87A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession P30519, checked via https://rest.uniprot.org/uniprotkb/P30519.json and applied mutation signature L201A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession P30519, checked via https://rest.uniprot.org/uniprotkb/P30519.json and applied mutation signature K169A to reconstruct the assayed variant sequence.


organism: Moorella thermoacetica (strain ATCC 39073 / JCM 9320)


organism: Protochlamydia amoebophila (strain UWE25)

substrate_name: LL-2,6-diaminopimelate (at 30 degrees Celsius and pH 7.6)


organism: Arabidopsis thaliana


organism: Sus scrofa

substrate_name: dephospho-CoA (in the PPAT reaction)

substrate: dephospho-CoA (in the PPAT reaction)


organism: Verrucomicrobium spinosum


organism: Verrucomicrobium spinosum WP_009961032 GenBank

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


substrate_name: dephospho-CoA

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

substrate: dephospho-CoA


substrate_name: Dephospho-CoA; Diphosphate

substrate: Dephospho-CoA; Diphosphate


organism: Escherichia coli


substrate_name: 3'-Dephospho-CoA; Diphosphate

substrate: 3'-Dephospho-CoA; Diphosphate


organism: Escherichia coli (strain K12)

sequence_source: source_record; direct UniProt FASTA equality check for P0A6I6 on 2026-06-14

proof_lines: kcat is 1.37 sec(-1) for the forward reaction, with ATP and pantetheine 4'-phosphate as substrates (PubMed:17873050). kcat is 3.3 sec(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates (PubMed:10480925). kcat


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

sequence_source: source_record; direct UniProt FASTA equality check for P9WPA5 on 2026-06-14

proof_lines: kcat is 288.5 min(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates, which is nearly identical to that of the forward reaction fitted to the Hill equation. The enzyme seems to utilize a nonrapid-equilibrium r


organism: Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)

substrate: LL-2,6-diaminopimelate (at 30 degrees Celsius and pH 7.6)


organism: Desulfitobacterium hafniense (strain DSM 10664 / DCB-2)


organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: alpha-ketoglutarate (alpha-KG)(at pH 8.8 and at 70 degrees Celsius)


organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)


organism: Bacillus subtilis

sequence_source: UniProtKB:P94398 reviewed FolE2/yciA entry, anchored by PMID 19767425 GCYH-IB paper context

assay_conditions_summary: pH 8


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

proof_lines:
HO4, without ascorbate
HO3, without ascorbate


organism: Bos taurus

sequence_source: UniProt Q5E9F2 FASTA; catalytic activity cites PubMed 6806282

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


organism: Gallus gallus

sequence_source: UniProt P14791 FASTA; catalytic activity cites PubMed 2158889

proof_lines:
in the absence of bovine serum albumin
in the presence of bovine serum albumin


organism: Homo sapiens

proof_lines: recombinant heme oxygenase-1/cytochrome P450 reductase fusion protein


mutation_signature: recombinant C-terminal truncated heme oxygenase-1 recombinant C-terminal truncated heme oxygenase-1

sequence_source: UniProt P09601 FASTA plus PubMed 7703255 abstract construct description

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


sequence_variant_note: Resolved canonical sequence from UniProt P09601 FASTA plus PubMed 8547275 H132S mutant description and applied mutation signature H132S to reconstruct the assayed variant sequence.


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

proof_lines: heme oxygenase-1, H132G and H132A mutants


organism: Leptospira interrogans serovar Icterohaemorrhagiae

substrate_name: [reduced NADPH-hemoprotein reductase]

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: [reduced NADPH-hemoprotein reductase]


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:Q8EXM2 and applied mutation signature F157I to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: NADPH; Heme; O2

proof_lines:
heme oxygenase-1
enzyme from spleen and liver
intestinal enzyme

substrate: NADPH; Heme; O2


organism: Enterobacteriaceae bacterium

substrate_name: Phosphinothricin

substrate: Phosphinothricin


organism: Mus musculus

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


organism: Streptomyces tubercidicus


organism: Arabidopsis thaliana

substrate_name: hemin

substrate: hemin


substrate_name: heme b

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

substrate: heme b


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

substrate_name: phosphinothricin

substrate: phosphinothricin


organism: Streptomyces hygroscopicus


organism: Methanococcus maripaludis

substrate_name: LL-diaminopimelate

sequence_source: UniProtKB:Q6LX26; reviewed; UniProt release 2026_02; direct query EC 2.6.1.83 plus organism Methanococcus maripaludis returned X-Total-Results=1

proof_lines: after correction for a purity of 70%, pH 8.5, 70°C

substrate: LL-diaminopimelate


organism: Verrucomicrobium spinosum

sequence_source: UniProtKB:A0A6P3CW87; unreviewed; UniProt release 2026_02; direct query EC 2.6.1.83 plus organism Verrucomicrobium spinosum returned X-Total-Results=1


organism: Corynebacterium ammoniagenes

substrate_name: pantetheine 4'-phosphate

sequence_source: UniProtKB:A0ABN0ADC1; unreviewed; UniProt release 2026_02; direct query EC 2.7.7.3 plus organism Corynebacterium ammoniagenes returned X-Total-Results=1

substrate: pantetheine 4'-phosphate


organism: Escherichia coli

substrate_name: ATP; 4'-Phosphopantetheine

proof_lines:
25°C, pH 8
forward reaction
reverse reaction

substrate: ATP; 4'-Phosphopantetheine


substrate_name: 4'-Phosphopantetheine; ATP

sequence_source: UniProtKB:Q5XIA5; unreviewed; UniProt release 2026_02; direct query EC 2.7.7.3 plus organism Rattus norvegicus returned X-Total-Results=1

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 8.5, cytosol
30°C, pH 8.5
37°C, pH 8

substrate: 4'-Phosphopantetheine; ATP


organism: Geobacillus stearothermophilus

substrate_name: GTP

sequence_source: UniProtKB:A0ACH1E519; unreviewed; UniProt release 2026_02; direct query EC 3.5.4.16 plus organism Geobacillus stearothermophilus returned X-Total-Results=1

substrate: GTP


enzyme_display_name: beta-lactamase

organism: Aeromonas hydrophila

substrate_name: Imipenem

assay_conditions_summary: pH 10; 303.15 K; buffer 20 mM sodium cacodylate

proof_lines:
wild type enzyme, at pH 8.0
wild type enzyme, at pH 9.0
wild-type, 30°C, pH 6.5

enzyme: beta-lactamase

substrate: Imipenem


organism: Brachyspira pilosicoli

substrate_name: carbenicillin

sequence_source: UniProtKB:Q50H31 direct sequence

assay_conditions_summary: pH 7; 298.15 K; buffer phosphate

proof_lines: at 25°C in 100 mM sodium phosphate (pH 7.0)

substrate: carbenicillin


organism: Chryseobacterium indologenes

substrate_name: Sulbactam

sequence_source: UniProtKB:Q6JE29 direct sequence

assay_conditions_summary: pH 6.5; buffer plus ZnSO4

proof_lines: in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4

substrate: Sulbactam


enzyme_display_name: pyruvate kinase

organism: Bos taurus

substrate_name: Phosphoenolpyruvate; ADP

sequence_source: UniProtKB Q1JPG7 direct lookup

assay_conditions_summary: cofactor ADP

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Chlamydia trachomatis

sequence_source: UniProtKB B0B7Q0 direct lookup


organism: Corynebacterium glutamicum

substrate_name: ADP; Phosphoenolpyruvate

sequence_source: UniProtKB Q46078 direct lookup

assay_conditions_summary: pH 7; 308.15 K; cofactor ADP

substrate: ADP; Phosphoenolpyruvate


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AD61 direct lookup plus K382Q reconstruction and applied mutation signature K382Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K382Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AD61 direct lookup plus R431E reconstruction and applied mutation signature R431E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R431E


sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA P0AD61; reconstructed single substitution R271L and applied mutation signature R271L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R271L


sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA P0AD61; reconstructed single substitution K413Q and applied mutation signature K413Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K413Q


sequence_source: UniProt REST FASTA P0AD61


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA P30613; reconstructed single substitution R510Q and applied mutation signature R510Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R510Q


substrate_name: Pyruvate; ATP

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

sequence_source: UniProtKB REST lookup for P30613

assay_conditions_summary: 303.15 K; cofactor ATP

substrate: Pyruvate; ATP


sequence_source: UniProtKB REST lookup for P14618

assay_conditions_summary: pH 8; 305.15 K; cofactor ADP

proof_lines: pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate

proof_lines: Zn2+ bound to the ADP-binding site of the free enzyme, pH 7.4, 37°C


organism: Lactococcus lactis subsp. cremoris

sequence_source: UniProtKB REST lookup for A2RKA3


organism: Lactococcus lactis subsp. lactis

sequence_source: UniProtKB REST lookup for Q07637


organism: Amycolatopsis methanolica

sequence_source: UniProtKB direct lookup accession A0A076MW80; organism Amycolatopsis methanolica 239; protein Pyruvate kinase; EC 2.7.1.40.


organism: Arabidopsis thaliana


organism: Leishmania mexicana

substrate_name: ADP

sequence_source: UniProtKB:Q27686 direct accession lookup

assay_conditions_summary: pH 7.5; cofactor ADP

substrate: ADP


organism: Mus musculus

substrate_name: ATP; Pyruvate

sequence_source: UniProtKB:P52480 direct accession lookup

assay_conditions_summary: cofactor ATP

substrate: ATP; Pyruvate


sequence_source: UniProtKB:P53657 direct accession lookup


organism: Oncorhynchus mykiss

substrate_name: AMP; Phosphate; Phosphoenolpyruvate

sequence_source: UniProtKB:Q98TA0 direct accession lookup

substrate: AMP; Phosphate; Phosphoenolpyruvate


organism: Oryctolagus cuniculus

sequence_source: UniProtKB:P11974 direct accession lookup


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11980 (KPYM_RAT), retrieved 2026-06-15 and applied mutation signature A398R/E432D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432D


sequence_source: UniProtKB reviewed accession B1WBN9 (B1WBN9_RAT), retrieved 2026-06-15


organism: Ricinus communis

sequence_source: UniProtKB reviewed accession Q43117 (KPYA_RICCO), retrieved 2026-06-15


organism: Saccharolobus solfataricus

substrate_name: phosphoenolpyruvate

sequence_source: UniProtKB reviewed accession Q97ZD7 (Q97ZD7_SACS2), retrieved 2026-06-15

proof_lines: 70°C, pH not specified in the publication

proof_lines: 50°C, pH not specified in the publication

proof_lines: 65°C, pH not specified in the publication

substrate: phosphoenolpyruvate


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P00549 (KPYK1_YEAST), retrieved 2026-06-15 and applied mutation signature T403E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T403E


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R336K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 and applied mutation signature A398R/E432A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 and applied mutation signature A398R/E432K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 and applied mutation signature E432A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 and applied mutation signature E432D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 and applied mutation signature E432K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11980 and applied mutation signature A398R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R336Q


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


sequence_variant_note: Resolved canonical sequence from UniProt P00549 canonical sequence reconstructed with SABIO-RK mutation Y436F and applied mutation signature Y436F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Y436F


sequence_variant_note: Resolved canonical sequence from UniProt P00549 canonical sequence reconstructed with SABIO-RK mutation Q299N and applied mutation signature Q299N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Q299N


sequence_variant_note: Resolved canonical sequence from UniProt P00549 canonical sequence reconstructed with SABIO-RK mutation A458K and applied mutation signature A458K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant A458K


sequence_variant_note: Resolved canonical sequence from UniProt P00549 canonical sequence reconstructed with SABIO-RK mutation K236Q and applied mutation signature K236Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K236Q


sequence_variant_note: Resolved canonical sequence from UniProt P00549 canonical sequence reconstructed with SABIO-RK mutation Y436S and applied mutation signature Y436S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Y436S


sequence_variant_note: Resolved canonical sequence from UniProt P00549 canonical sequence reconstructed with SABIO-RK mutation T406R and applied mutation signature T406R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T406R


organism: Ustilago maydis

substrate_name: ADP; Phosphoenolpyruvate; ADP; Phosphoenolpyruvate; ATP; Pyruvate; Phosphoenolpyruvate; ADP

sequence_source: UniProtKB:A0A0D1E735 direct lookup

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


organism: Vibrio cholerae serotype O1

substrate_name: ADP; phosphoenolpyruvate

sequence_source: UniProtKB:Q9KUN0 direct lookup

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines: pH 7.0, 25°C, recombinant non-His-tagged enzyme

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of fructose 1,6-bisphosphate

substrate: ADP; phosphoenolpyruvate


organism: Zymomonas mobilis

substrate_name: ADP; Phosphoenolpyruvate; ADP; Phosphoenolpyruvate; Pyruvate; ATP; Phosphoenolpyruvate; ADP

sequence_source: UniProtKB:Q5NR78 direct lookup


enzyme_display_name: trypsin

organism: Bos taurus

substrate_name: Benzyloxycarbonyl-Arg-Arg-7-amino-4-methylcoumarin; H2O; Benzyloxycarbonyl-Arg-Arg-7-amino-4-methylcoumarin; H2O; 7-Amino-4-methylcoumarin; Benzyloxycarbonyl-Arg-Arg

enzyme: trypsin


substrate_name: H2O; N-Ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester; H2O; N-Ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine p-nitrophenyl ester; p-Nitrophenol; N-Ethoxycarbonyl-D-phenylalanyl-L-prolyl-alpha-azalysine

sequence_source: UniProtKB:P00760 direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 canonical sequence with reviewer-reconstructed substitution and applied mutation signature R409Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R409Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 canonical sequence with reviewer-reconstructed substitution and applied mutation signature R369A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R369A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 canonical sequence with reviewer-reconstructed substitution and applied mutation signature T403K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T403K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 canonical sequence with reviewer-reconstructed substitution and applied mutation signature R459Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R459Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 canonical sequence with reviewer-reconstructed substitution and applied mutation signature K292Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K292Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 canonical sequence with reviewer-reconstructed substitution and applied mutation signature T311M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T311M


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 canonical sequence with reviewer-reconstructed substitution and applied mutation signature E392A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant E392A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 canonical sequence with reviewer-reconstructed substitution and applied mutation signature R77Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R77Q


organism: Trichomonas vaginalis


organism: Trypanosoma brucei


organism: Channa argus


organism: Gallus gallus


organism: Homo sapiens

substrate_name: H2O; Glu-Gly-Arg-p-nitroanilide

substrate: H2O; Glu-Gly-Arg-p-nitroanilide


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 REST lookup 2026-06-15; PMID 12562754 abstract mutation context and applied mutation signature T298S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme Pyk1 T298S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 REST lookup 2026-06-15; PMID 12562754 abstract mutation context and applied mutation signature T298A to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00549 REST lookup 2026-06-15; PMID 7646433 abstract mutation context and applied mutation signature S384P with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

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


sequence_source: UniProtKB:P00549 REST lookup 2026-06-15


sequence_source: UniProtKB:P52489 REST lookup 2026-06-15; PMID 9139918 abstract identity context


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


substrate_name: D-Val-Leu-Lys-thiobenzyl ester

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

substrate: D-Val-Leu-Lys-thiobenzyl ester


proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant DeltaI16V17/ D194N trypsinogen

proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant D194N trypsin


organism: Saccharopolyspora erythraea

sequence_source: UniProtKB Q54137 canonical sequence from direct REST lookup

proof_lines: recombinant enzyme, in 100 mM Tris-HCl, pH 8.0 at 25°C


organism: Salmo salar

sequence_source: UniProtKB P35031 canonical sequence from direct REST lookup


sequence_source: UniProtKB P35033 canonical sequence from direct REST lookup


organism: Streptomyces griseus


sequence_source: UniProtKB P00775 canonical sequence from direct REST lookup

proof_lines:
pH 7.6, wild-type enzyme
wild-type, pH 8.0, 25°C


sequence_source: UniProtKB:P00775 canonical sequence context only


substrate_name: factor Xa

substrate: factor Xa


organism: Sus scrofa

substrate_name: H-D-Ile-Pro-Arg-p-nitroanilide; H2O

substrate: H-D-Ile-Pro-Arg-p-nitroanilide; H2O


substrate_name: H2O; H-D-Ile-Pro-Arg-p-nitroanilide

substrate: H2O; H-D-Ile-Pro-Arg-p-nitroanilide


substrate_name: Unknown

sequence_source: UniProt P07477 direct REST check

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

substrate: Unknown


organism: Rattus norvegicus

substrate_name: Benzyloxycarbonyl-Lys-thiobenzyl ester

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

substrate: Benzyloxycarbonyl-Lys-thiobenzyl ester


proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant I16G trypsinogen


mutation_type: deletion

proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant DeltaI16 trypsinogen

proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant DeltaI16V17 trypsinogen


proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant I16G/ D194N trypsinogen


proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant DeltaI16V17/ H40F trypsinogen

proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant H40F trypsin


substrate_name: Benzyloxycarbonyl-Arg-thiobenzyl ester

substrate: Benzyloxycarbonyl-Arg-thiobenzyl ester


proof_lines: SABIO-RK modifier species: trypsin(Enzyme) mutant K15A trypsinogen


enzyme_display_name: ferredoxin--NADP(+) reductase

organism: Anabaena sp.

substrate_name: NADPH

sequence_source: UniProtKB:P21890 direct accession lookup; BRENDA mutation note requires separate variant reconstruction

assay_conditions_summary: pH 8; cofactor NADPH

enzyme: ferredoxin--NADP(+) reductase

substrate: NADPH


substrate_name: NADH

substrate: NADH


proof_lines: mutant T155G/A160T/L263P/Y303S, called PP3CT


proof_lines: mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5


proof_lines: mutant T155G/A160T/L263P/R264P/G265P, called PP5


proof_lines: mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q9XI55 direct REST lookup

assay_conditions_summary: pH 7; 298.15 K; cofactor FAD

proof_lines: with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C


organism: Bacillus subtilis

substrate_name: NADPH; Oxidized ferredoxin

sequence_source: UniProtKB:O05268 direct REST lookup

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines:
cosubstrate NADPH, pH 7, 25°C
Raw SKiD Env: Temp=25°C, pH=7

substrate: NADPH; Oxidized ferredoxin


assay_conditions_summary: pH 7; 297.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature S223D/R233L/Y235F with inferred residue-numbering offset +137 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NADH


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature T155G/A160T/S223D/R224Q/R233L/Y235F/L263P with inferred residue-numbering offset +137 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature T155G/A160T/L263P with inferred residue-numbering offset +137 to reconstruct the assayed variant sequence.

proof_lines:
mutant T155G/A160T/L263P, pH 8.0
mutant T155G/A160T/L263P, called PP3


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature T155G/A160T with inferred residue-numbering offset +137 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature S223D/R224Q/R233L/Y235F with inferred residue-numbering offset +137 to reconstruct the assayed variant sequence.


substrate_name: reduced ferredoxin

sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature Y303W with inferred residue-numbering offset +137 to reconstruct the assayed variant sequence.

substrate: reduced ferredoxin


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature Y303F with inferred residue-numbering offset +137 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O05268 direct REST FASTA lookup; Y50S reconstructed from the checked canonical sequence. and applied mutation signature Y50S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


sequence_source: UniProtKB O05268 direct REST FASTA lookup; Y50S reconstructed from the checked canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O05268 direct REST FASTA lookup; Y50W reconstructed from the checked canonical sequence. and applied mutation signature Y50W to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O05268 direct REST FASTA lookup.

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

proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme


sequence_source: UniProtKB O05268 direct REST FASTA lookup; Y50W reconstructed from the checked canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O05268 direct REST FASTA lookup; Y50G reconstructed from the checked canonical sequence. and applied mutation signature Y50G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O05268 direct REST FASTA lookup; Y50G reconstructed from the checked canonical sequence.


assay_conditions_summary: cofactor NADPH


organism: Chlamydomonas reinhardtii

substrate_name: oxidized Fdx2

substrate: oxidized Fdx2


organism: Chlorobaculum tepidum

substrate_name: oxidized [2Fe-2S]-[rubredoxin]

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines:
cosubstrate NADH, pH 7, 25°C
pH 7, 25°C
cosubstrate NADPH, pH 7, 25°C

substrate: oxidized [2Fe-2S]-[rubredoxin]


organism: Cyanidium caldarium

proof_lines: in a 2,6-dichlorophenolindophenol reduction assay


organism: Escherichia coli

substrate_name: Fe(III)-EDTA

substrate: Fe(III)-EDTA


proof_lines: in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C


substrate_name: oxidized ferredoxin

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines: mutant with an insertion of the iloop of Pisum sativum enzyme plus deletion of residue W248, pH 8.0, 30°C

substrate: oxidized ferredoxin


sequence_source: UniProtKB REST FASTA direct check for P28861


mutation_type: insertion

proof_lines: mutant with an insertion of the iloop of Pisum sativum enzyme, pH 8.0, 30°C


organism: Lathyrus oleraceus

proof_lines: mutant lacking the beta-hairpin, pH 8.0, 30°C

proof_lines: mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C


sequence_source: UniProtKB REST FASTA direct check for P10933


organism: Leptospira interrogans

sequence_source: UniProtKB REST FASTA direct check for Q8EY89

proof_lines:
in 50 mM Tris-HCl, pH 8, at 30°C
Raw SKiD Env: Temp=30°C, pH=8


organism: Mycobacterium tuberculosis

substrate_name: NADH; 2,6-Dichloroindophenol; H+

sequence_source: UniProtKB REST FASTA direct check for P9WIQ3

substrate: NADH; 2,6-Dichloroindophenol; H+


organism: Pisum sativum

substrate_name: NADPH; Cytochrome c; H+

assay_conditions_summary: cofactor NADP+

proof_lines: SABIO-RK modifier species: ferredoxin---NADP+ reductase(Enzyme) mutant FNR-tail

substrate: NADPH; Cytochrome c; H+


organism: Plasmodium falciparum

substrate_name: NADPH; Hexacyanoferrate(III)

sequence_variant_note: Resolved canonical sequence from UniProtKB C6KT68 FASTA; UniProt PMID 19736991 feature/reference mapping for H286 to full-sequence H341 and applied mutation signature H286A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ferredoxin---NADP+ reductase(Enzyme) mutant H286A

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A

substrate: NADPH; Hexacyanoferrate(III)


substrate_name: Hexacyanoferrate(III); NADPH

sequence_source: UniProtKB C6KT68 FASTA; UniProt PMID 19736991 feature/reference mapping for H286 to full-sequence H341

sequence_variant_note: Mutation signature H286K matches the mutant residue at offset +3 and the reference residue at offset +12; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: ferredoxin---NADP+ reductase(Enzyme) mutant H286K

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286K

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K

substrate: Hexacyanoferrate(III); NADPH


assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KT68 FASTA; UniProt PMID 19736991 feature/reference mapping for H286 to full-sequence H341 and applied mutation signature H286L with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ferredoxin---NADP+ reductase(Enzyme) mutant H286L

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L


sequence_variant_note: Mutation signature H286Q matches the mutant residue at offset +2 and the reference residue at offset +12; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: Rhodobacter capsulatus

sequence_source: UniProtKB Q9L6V3 FASTA

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines:
diaphorase activity, pH 8.0
pH 8.0
Raw SKiD Env: Temp=-----, pH=8


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

proof_lines: wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: wild-type, substrate ferricyanide, pH 7.2, 25°C


organism: Spinacia oleracea

substrate_name: Reduced ferredoxin; H+; NADP+

sequence_source: UniProtKB:P00455 direct lookup; reviewed Swiss-Prot FENR_SPIOL; Ferredoxin--NADP reductase, chloroplastic; EC 1.18.1.2; organism Spinacia oleracea.

substrate: Reduced ferredoxin; H+; NADP+


assay_conditions_summary: pH 8.7; 292.15 K; cofactor NADPH


substrate_name: H+; NADPH; Dibromothymoquinone

substrate: H+; NADPH; Dibromothymoquinone


substrate_name: H+; Hexacyanoferrate(III); NADPH

substrate: H+; Hexacyanoferrate(III); NADPH


organism: Xanthomonas axonopodis

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

proof_lines: pH 8.0, temperature not specified in the publication


organism: Zea mays

sequence_source: UniProtKB:Q41736 direct lookup; TrEMBL Q41736_MAIZE; ferredoxin--NADP(+) reductase; EC 1.18.1.2; organism Zea mays.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


substrate_name: 2,6-Dichloroindophenol; NADPH; H+

substrate: 2,6-Dichloroindophenol; NADPH; H+


substrate_name: Oxidized ferredoxin I; NADPH; H+

substrate: Oxidized ferredoxin I; NADPH; H+


substrate_name: Oxidized ferredoxin I; H+; NADPH

sequence_source: UniProtKB direct lookup: Q9SLP6

substrate: Oxidized ferredoxin I; H+; NADPH


substrate_name: Oxidized ferredoxin III; NADPH; H+

sequence_source: UniProtKB direct lookup: Q41736

substrate: Oxidized ferredoxin III; NADPH; H+


substrate_name: NADPH

substrate: NADPH


substrate_name: H+; NADPH; 2,6-Dichloroindophenol

substrate: H+; NADPH; 2,6-Dichloroindophenol


substrate_name: Oxidized ferredoxin III; H+; NADPH

substrate: Oxidized ferredoxin III; H+; NADPH


substrate_name: iodonitrotetrazolium

substrate: iodonitrotetrazolium


substrate_name: Oxidized ferredoxin; NADPH

sequence_source: Canonical context only from UniProtKB direct lookup: Q41736; row-specific E92A variant sequence unresolved

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: ferredoxin---NADP+ reductase(Enzyme) mutant E92A

substrate: Oxidized ferredoxin; NADPH


sequence_source: Canonical context only from UniProtKB direct lookup: Q41736; row-specific E92K variant sequence unresolved

proof_lines: SABIO-RK modifier species: ferredoxin---NADP+ reductase(Enzyme) mutant E92K


sequence_source: UniProtKB Q41736 direct accession lookup


substrate_name: reduced ferredoxin

proof_lines: pH 7.5, 25°C, mutant Y314S, in presence of 0.05 mM NADPH

proof_lines: pH 7.5, 25°C, mutant Y314S, in presence of 0.50 mM NADPH

proof_lines: pH 7.5, 25°C, mutant Y314S, in presence of 0.25 mM NADPH

substrate: reduced ferredoxin


sequence_source: UniProtKB Q9SLP6 direct accession lookup

proof_lines: pH 7.5, 25°C, wild-type enzyme, NADPH-dependent diaphorase activity using DCPIP

proof_lines: pH 7.5, 25°C, wild-type enzyme, in presence of 1 mM NADPH

proof_lines: pH 7.5, 25°C, wild-type enzyme, in presence of 0.05 mM NADPH


proof_lines: pH 7.5, 25°C, mutant R235Q, in presence of 0.05 mM NADPH

proof_lines: pH 7.5, 25°C, mutant R235Q, in presence of 0.50 mM NADPH

proof_lines: pH 7.5, 25°C, mutant R235Q, in presence of 1.0 mM NADPH


proof_lines: pH 7.5, 25°C, mutant R244Q, in presence of 1.0 mM NADPH

proof_lines: pH 7.5, 25°C, mutant R244Q, in presence of 0.05 mM NADPH

proof_lines: pH 7.5, 25°C, mutant R244Q, in presence of 0.50 mM NADPH


substrate_name: NADH

sequence_source: UniProtKB:P10933 canonical sequence from direct accession lookup

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

substrate: NADH


sequence_source: UniProtKB:C6KT68 canonical sequence from direct accession lookup

assay_conditions_summary: pH 9; 298.15 K; cofactor NADPH

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor

proof_lines: using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor


assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADH


sequence_source: Reconstructed from UniProtKB:C6KT68 canonical sequence using PMID 19736991/UniProt mutagenesis mapping

proof_lines: SABIO-RK modifier species: ferredoxin---NADP+ reductase(Enzyme) mutant H286Q

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:C6KT68 canonical sequence using PMID 19736991/UniProt mutagenesis mapping and applied mutation signature H286L with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


substrate_name: NADPH; 2,6-Dichloroindophenol; H+

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

proof_lines: SABIO-RK modifier species: ferredoxin---NADP+ reductase(Enzyme) mutant K249A

substrate: NADPH; 2,6-Dichloroindophenol; H+


proof_lines: mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C


proof_lines: mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: mutant A266Y, substrate ferricyanide, pH 7.2, 25°C

proof_lines: mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C


organism: Rhodopseudomonas palustris

proof_lines: wild-type enzyme with ferricyanide, pH 7.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6N2U4 and applied mutation signature Y328S to reconstruct the assayed variant sequence.

proof_lines: mutant Y328S with ferricyanide, pH 7.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6N2U4 and applied mutation signature Y328H to reconstruct the assayed variant sequence.

proof_lines: mutant Y328H with ferricyanide, pH 7.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6N2U4 and applied mutation signature Y328F to reconstruct the assayed variant sequence.

proof_lines: mutant Y328F with ferricyanide, pH 7.0, 25°C


enzyme_display_name: amidase

organism: Achromobacter xylosoxidans

sequence_source: UniProt REST accessions endpoint direct check

enzyme: amidase


organism: Alcaligenes sp.

substrate_name: acetate-prelabeled chicken histones

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

substrate: acetate-prelabeled chicken histones


organism: Gallus gallus

substrate_name: Propionamide; H2O

substrate: Propionamide; H2O


organism: Paracoccus sp. (in: a-proteobacteria)

substrate_name: Acrylamide

substrate: Acrylamide


organism: Pseudomonas aeruginosa

substrate_name: acetamide

smiles: CC(=N)O

substrate: acetamide


substrate_name: H2O; Acrylamide

proof_lines:
strain AI3
strain 10A
strain 3B

substrate: H2O; Acrylamide


smiles: C=CC(=N)O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11436 canonical sequence reconstructed with selected mutation_signature C91A and applied mutation signature C91A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11436 canonical sequence reconstructed with selected mutation_signature T103I and applied mutation signature T103I to reconstruct the assayed variant sequence.


substrate_name: H2O; Acetamide; H2O; Acetamide; NH3; Acetate; Acetamide; H2O; Acrylamide; H2O; Acrylamide; Acrylate; H2O; Acrylamide; 4-Nitroacetanilide; H2O; 4-Nitroacetanilide

sequence_source: UniProtKB:P11436 canonical sequence reconstructed with selected mutation_signature T103I

proof_lines: SABIO-RK modifier species: amidase(Enzyme) mutant T103I


sequence_source: UniProtKB:P11436 canonical sequence


substrate_name: Acetamide; H2O; Acetamide; H2O; NH3; Acetate; H2O; Acetamide

sequence_source: UniProtKB:P11436 canonical sequence reconstructed with selected mutation_signature C91A

proof_lines: SABIO-RK modifier species: amidase(Enzyme) mutant C91A


organism: Pyrococcus yayanosii

sequence_source: UniProtKB:F8AEP0 canonical sequence


organism: Saccharolobus solfataricus

substrate_name: picolinamide

sequence_source: UniProtKB reviewed P95896 FASTA direct accession check

substrate: picolinamide


substrate_name: lactamide

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

substrate: lactamide


substrate_name: Propionamide

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P95896 FASTA direct accession check and applied mutation signature K96R to reconstruct the assayed variant sequence.

proof_lines: 85°C, pH not specified in the publication, mutant enzyme K96R

substrate: Propionamide


substrate_name: Benzamide

substrate: Benzamide


substrate_name: Pentanamide

smiles: CCCCC(=N)O

substrate: Pentanamide


assay_conditions_summary: pH 5; 343.15 K; buffer 50 mM citrate buffer

column_label: Table 1. Kinetic properties of Sulfolobus solfataricus amidase. The turnover number (kcat) was obtained dividing by the molecular mass of the active monomer (55,784 Da); temperature was 70 C; in 50 mM citrate buffer at pH 5.0. Wild-type non-bold line of the substrate block 'p-OH benzamide'; column 'Km (mM)' = 0.1; column 'kcat (sec-1)' = 1.9; column 'kcat/Km (M^-1 sec^-1) x 10^2' = 190.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.1 mM; already in mM, no conversion; the exported value is 0.1 mM. kcat: printed Table 1 cell 1.9 sec-1; 1 sec-1 is 1 s^(-1), so the printed cell is 1.9 s^(-1); the exported value is 1.9. kcat/Km: printed Table 1 cell 190.0 in the column headed kcat/Km (M^-1 sec^-1) x 10^2, that is 19000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 mM^-1 s^-1, so the printed cell is 19.0 s^(-1)*mM^(-1); the exported value is 19.0.

raw_value_unit_evidence: Table 1, wild-type non-bold line of the substrate block 'p-OH benzamide': Km = 0.1 mM; kcat = 1.9 sec-1; printed kcat/Km = 190.0 in the column unit 10^2 M^-1 sec^-1, that is 19000 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription (section 2), wild-type non-bold line of the substrate block 'p-OH benzamide'


column_label: Table 1. Kinetic properties of Sulfolobus solfataricus amidase. The turnover number (kcat) was obtained dividing by the molecular mass of the active monomer (55,784 Da); temperature was 70 C; in 50 mM citrate buffer at pH 5.0. Wild-type non-bold line of the substrate block '3-phenylpropionamide'; column 'Km (mM)' = 3.0; column 'kcat (sec-1)' = 15.3; column 'kcat/Km (M^-1 sec^-1) x 10^2' = 51.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 3.0 mM; already in mM, no conversion; the exported value is 3.0 mM. kcat: printed Table 1 cell 15.3 sec-1; 1 sec-1 is 1 s^(-1), so the printed cell is 15.3 s^(-1); the exported value is 15.3. kcat/Km: printed Table 1 cell 51.0 in the column headed kcat/Km (M^-1 sec^-1) x 10^2, that is 5100 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 mM^-1 s^-1, so the printed cell is 5.1 s^(-1)*mM^(-1); the exported value is 5.1.

raw_value_unit_evidence: Table 1, wild-type non-bold line of the substrate block '3-phenylpropionamide': Km = 3.0 mM; kcat = 15.3 sec-1; printed kcat/Km = 51.0 in the column unit 10^2 M^-1 sec^-1, that is 5100 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription (section 2), wild-type non-bold line of the substrate block '3-phenylpropionamide'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y41C to reconstruct the assayed variant sequence.