column_label: Table 2: Domain I mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 24), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'N181A': column 'KM,app (mM)' = 0.17 ± 0.02; column 'kcat,app (s-1)' = 3.3 ± 0.1; column '(kcat/KM)app (s-1 M-1)' = 1.9 x 10^4; unheaded relative-efficiency column = 0.7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.3 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 3.3 s^(-1); the exported value is 3.3 s^(-1). Km: printed Table 2 cell 0.17 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.17 mM; the exported value is 0.17 mM. kcat/KM: printed Table 2 cell 1.9 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^4 / 1000 = 19.0 s^-1 mM^-1; the paper value is 19.0 s^(-1)*mM^(-1); the exported value is 19.41176470588235 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Protein row 'N181A', pyruvate as the variable substrate: KM,app = 0.17 mM; kcat,app = 3.3 s-1; printed (kcat/KM)app = 1.9 x 10^4 s-1 M-1.

row_label: Table 2, Protein row 'N181A', with pyruvate as the variable substrate


enzyme_display_name: 1-deoxy-D-xylulose-5-phosphate synthase

organism: Deinococcus radiodurans

substrate_name: pyruvate

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature Y395F to reconstruct the assayed variant sequence.

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

mutation_type: substitution

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

column_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395F': column 'KM,app (mM)' = 0.19 ± 0.01; column 'kcat,app (s-1)' = 2.9 ± 0.02; column '(kcat/KM)app (s-1 M-1)' = 1.6 x 10^4; unheaded relative-efficiency column = 0.6.

normalized_value_unit_evidence: kcat: printed Table 4 cell 2.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 2.9 s^(-1); the exported value is 2.9 s^(-1). Km: printed Table 4 cell 0.19 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.19 mM; the exported value is 0.19 mM. kcat/KM: printed Table 4 cell 1.6 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^4 / 1000 = 16.0 s^-1 mM^-1; the paper value is 16.0 s^(-1)*mM^(-1); the exported value is 15.26315789473684 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Protein row 'Y395F', pyruvate as the variable substrate: KM,app = 0.19 mM; kcat,app = 2.9 s-1; printed (kcat/KM)app = 1.6 x 10^4 s-1 M-1.

row_label: Table 4, Protein row 'Y395F', with pyruvate as the variable substrate

data_origin: experimental

enzyme: 1-deoxy-D-xylulose-5-phosphate synthase

substrate: pyruvate

status: corrected

source: oed


substrate_name: D-glyceraldehyde 3-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature Y395A to reconstruct the assayed variant sequence.

column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395A': column 'KM,app (mM)' = 0.67 ± 0.05; column 'kcat,app (s-1)' = 3.9 ± 0.1; column '(kcat/KM)app (s-1 M-1)' = 5.8 x 10^3; unheaded relative-efficiency column = 0.04.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 3.9 s^(-1); the exported value is 3.9 s^(-1). Km: printed Table 3 cell 0.67 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.67 mM; the exported value is 0.59 mM. kcat/KM: printed Table 3 cell 5.8 x 10^3 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 5.8 x 10^3 / 1000 = 5.8 s^-1 mM^-1; the paper value is 5.8 s^(-1)*mM^(-1); the exported value is 6.610169491525424 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Protein row 'Y395A', GAP as the variable substrate: KM,app = 0.67 mM; kcat,app = 3.9 s-1; printed (kcat/KM)app = 5.8 x 10^3 s-1 M-1.

row_label: Table 3, Protein row 'Y395A', with GAP as the variable substrate

substrate: D-glyceraldehyde 3-phosphate


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9RUB5 REST lookup plus selected-row mutation_signature R423K and applied mutation signature R423K to reconstruct the assayed variant sequence.

status: unverified


source_db: brenda

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H434K to reconstruct the assayed variant sequence.

column_label: Table 4: Domain II mutants: Measurement of steady-state kinetic parameters with pyruvate is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 26), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'H434K': column 'KM,app (mM)' = 1.7 ± 0.1; column 'kcat,app (s-1)' = 9.9 ± 0.2; column '(kcat/KM)app (s-1 M-1)' = 5.9 x 10^3; unheaded relative-efficiency column = 0.2+.

normalized_value_unit_evidence: kcat: printed Table 4 cell 9.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 9.9 s^(-1); the exported value is 9.9 s^(-1). Km: printed Table 4 cell 1.7 mM; the printed unit is already mM, no unit conversion applies; the paper value is 1.7 mM; the exported value is 0.05 mM. kcat/KM: printed Table 4 cell 5.9 x 10^3 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 5.9 x 10^3 / 1000 = 5.9 s^-1 mM^-1; the paper value is 5.9 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 4, Protein row 'H434K', pyruvate as the variable substrate: KM,app = 1.7 mM; kcat,app = 9.9 s-1; printed (kcat/KM)app = 5.9 x 10^3 s-1 M-1.

row_label: Table 4, Protein row 'H434K', with pyruvate as the variable substrate

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature R423K to reconstruct the assayed variant sequence.

column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'R423K': column 'KM,app (mM)' = 0.60 ± 0.1; column 'kcat,app (s-1)' = 6.4 ± 0.2; column '(kcat/KM)app (s-1 M-1)' = 1.1 x 10^4; unheaded relative-efficiency column = 0.07.

normalized_value_unit_evidence: kcat: printed Table 3 cell 6.4 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 6.4 s^(-1); the exported value is 6.4 s^(-1). Km: printed Table 3 cell 0.60 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.6 mM; the exported value is 0.6 mM. kcat/KM: printed Table 3 cell 1.1 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^4 / 1000 = 11.0 s^-1 mM^-1; the paper value is 11.0 s^(-1)*mM^(-1); the exported value is 10.666666666666668 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Protein row 'R423K', GAP as the variable substrate: KM,app = 0.60 mM; kcat,app = 6.4 s-1; printed (kcat/KM)app = 1.1 x 10^4 s-1 M-1.

row_label: Table 3, Protein row 'R423K', with GAP as the variable substrate


mutation_signature: Unknown

kcat_over_km_origin: calculated

sequence_source: UniProtKB reviewed accession Q9RUB5 REST lookup on 2026-06-16

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


column_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25), printed column heads Protein | KM,app (mM) | kcat,app (s-1) | (kcat/KM)app (s-1 M-1), followed by one unheaded column printing the efficiency of that protein relative to wildtype. Protein row 'Y395F': column 'KM,app (mM)' = 0.59 ± 0.04; column 'kcat,app (s-1)' = 5.9 ± 0.2; column '(kcat/KM)app (s-1 M-1)' = 1.0 x 10^4; unheaded relative-efficiency column = 0.07.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.9 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 5.9 s^(-1); the exported value is 5.9 s^(-1). Km: printed Table 3 cell 0.59 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.59 mM; the exported value is 7.7 mM. kcat/KM: printed Table 3 cell 1.0 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.0 x 10^4 / 1000 = 10.0 s^-1 mM^-1; the paper value is 10.0 s^(-1)*mM^(-1); the exported value is 0.7662337662337663 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Protein row 'Y395F', GAP as the variable substrate: KM,app = 0.59 mM; kcat,app = 5.9 s-1; printed (kcat/KM)app = 1.0 x 10^4 s-1 M-1.

row_label: Table 3, Protein row 'Y395F', with GAP as the variable substrate


normalized_value_unit_evidence: kcat: printed Table 3 cell 6.4 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 6.4 s^(-1); the exported value is 6.4 s^(-1). Km: printed Table 3 cell 0.60 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.6 mM; the exported value is 0.06 mM. kcat/KM: printed Table 3 cell 1.1 x 10^4 s-1 M-1; 1 s-1 M-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^4 / 1000 = 11.0 s^-1 mM^-1; the paper value is 11.0 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

table_label: Table 3: Domain II mutants: Measurement of steady-state kinetic parameters with GAP is the variable substrate (Biochem Mol Biol J. 2018; 4(1), author manuscript page 25)


organism: Escherichia coli

substrate_name: D-Glyceraldehyde 3-phosphate

sequence_source: UniProtKB reviewed accession P77488 REST lookup on 2026-06-16

substrate: D-Glyceraldehyde 3-phosphate


enzyme_display_name: hydroxyacylglutathione hydrolase

organism: Arabidopsis thaliana

substrate_name: S-D-lactoylglutathione

sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction H54N. and applied mutation signature H54N to reconstruct the assayed variant sequence.

enzyme: hydroxyacylglutathione hydrolase

substrate: S-D-lactoylglutathione


sequence_source: UniProt REST canonical accession O24496; variant sequence not accepted.

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


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction W57N. and applied mutation signature W57N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction L9A. and applied mutation signature L9A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST canonical accession O24496.

proof_lines: recombinant wild-type enzyme, pH 7.2, 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction W57D. and applied mutation signature W57D to reconstruct the assayed variant sequence.


substrate_name: Unknown

kcat_display: Not reported

km_display: Not reported

ki_unit: mM

sequence_source: UniProt REST canonical accession O24496; double-variant sequence not accepted.

proof_lines: recombinant mutants W57N and K65A, pH 7.2, 25°C

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProt REST canonical accession O24496 plus one-based substitution reconstruction K65A. and applied mutation signature K65A to reconstruct the assayed variant sequence.


proof_lines: recombinant enzyme grown in medium not supplemented with metal ions, pH 7.2, 25°C

proof_lines: recombinant enzyme grown in medium supplemented with Mn2+, pH 7.2, 25°C

proof_lines: recombinant enzyme grown in medium supplemented with Fe2+, pH 7.2, 25°C


substrate_name: S-Lactoylglutathione

source_db: brenda,skid

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

sequence_source: UniProt REST canonical accession Q9SID3.

proof_lines:
25°C, pH 7.2
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.2

source_databases_merged: brenda skid

substrate: S-Lactoylglutathione

source: brenda,skid


substrate_name: (R)-S-Mandeloylglutathione

substrate: (R)-S-Mandeloylglutathione


substrate_name: (R)-S-Lactoylglutathione

substrate: (R)-S-Lactoylglutathione


organism: Brassica juncea

sequence_source: UniProt REST canonical accession Q84XQ5.

assay_conditions_summary: pH 7


sequence_source: UniProt REST canonical accession P0AC84.


organism: Homo sapiens

sequence_source: UniProt REST canonical accession Q16775; variant sequence not accepted.


sequence_source: UniProt REST canonical accession Q16775.


organism: Salvia splendens

substrate_name: malonyl-CoA; 4'''-demalonylsalvianin

sequence_source: UniProtKB:Q6TXD2 direct lookup

assay_conditions_summary: pH 8.5; cofactor CoA

proof_lines: pH 8.5, temperature not specified in the publication

substrate: malonyl-CoA; 4'''-demalonylsalvianin


substrate_name: Malonyl-CoA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

substrate: Malonyl-CoA


enzyme_display_name: Kdo2-lipid IVA acyltransferase

sequence_source: UniProtKB:P0ACV0 direct lookup

enzyme: Kdo2-lipid IVA acyltransferase


organism: Mycobacterium tuberculosis

substrate_name: Trehalose 2-sulfate

sequence_source: UniProtKB:P9WIK7 direct lookup

substrate: Trehalose 2-sulfate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


substrate_name: Phenylthioacetohydroximate

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

substrate: Phenylthioacetohydroximate


organism: Lachnoclostridium phytofermentans

substrate_name: L-Rhamnose

sequence_source: UniProtKB:A9KM56 direct lookup

substrate: L-Rhamnose


substrate_name: beta-D-Glucose 1-phosphate

substrate: beta-D-Glucose 1-phosphate


substrate_name: L-rhamnose; beta-D-glucose 1-phosphate

proof_lines: pH 6.5, 30°C, reverse phosphorolysis reaction, cosubstrate beta-D-glucose 1-phosphate

substrate: L-rhamnose; beta-D-glucose 1-phosphate


enzyme_display_name: sym-norspermidine synthase

organism: Pyrococcus furiosus

verification_status: verified

sequence_source: UniProtKB:Q8U4G1 direct lookup

smiles: NCCCN

column_label: Table 5 (Kinetic parameters of ACAPT from P. furiosus), row '1,3-Diaminopropane'; column 'Km (uM)' = 1,877; column 'kcat (s^-1)' = 0.06; column 'kcat/Km (M^-1 s^-1) (x10^2)' = 0.32 (i.e. 0.32 x 10^2 = 32 M^-1 s^-1).

normalized_value_unit_evidence: Km: printed cell 1,877 uM; 1,877 / 1000 = 1.877 mM; the exported value is 1.877 mM. kcat: printed cell 0.06 s^-1; already in s^-1, no unit change applies; the exported value is 0.06 s^(-1). kcat/Km: the exact quotient of this row's own two printed cells is 0.06 / 1.877 = 0.031965903036760786 s^-1 mM^-1, which is the exported value; the printed kcat/Km column cell (0.32 x 10^2 = 32 M^-1 s^-1 = 0.032 s^-1 mM^-1) rounds to the same two-figure precision as this exact quotient, corroborating it.

raw_value_unit_evidence: Table 5, row 1,3-Diaminopropane: Km = 1,877 uM; kcat = 0.06 s^-1; printed kcat/Km column value = 0.32, with the column head noting a shared x10^2 scale, i.e. 0.32 x 10^2 = 32 M^-1 s^-1.

row_label: Table 5, row 1,3-Diaminopropane

table_label: Table 5: Kinetic parameters of ACAPT from P. furiosus (J Bacteriol 2007, 189(16):6057-6067)

enzyme: sym-norspermidine synthase

status: verified


enzyme_display_name: cysteate synthase

organism: Methanosarcina acetivorans

substrate_name: sulfite

sequence_source: UniProtKB:Q8TKU7 direct lookup

enzyme: cysteate synthase

substrate: sulfite


substrate_name: L-phosphoserine

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

substrate: L-phosphoserine


enzyme_display_name: thermospermine synthase

organism: Thermus thermophilus

substrate_name: Spermidine

sequence_source: UniProtKB:Q5SK28 direct lookup

smiles: NCCCCNCCCN

enzyme: thermospermine synthase

substrate: Spermidine


substrate_name: Mitsubishine

substrate: Mitsubishine


organism: Rattus norvegicus

sequence_source: UniProt REST direct lookup 2026-06-16, accession O35952


organism: Saccharomyces cerevisiae

substrate_name: S-D-mandeloylglutathione

sequence_source: UniProt REST direct lookup 2026-06-16, accession Q12320

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

substrate: S-D-mandeloylglutathione


sequence_source: UniProt REST direct lookup 2026-06-16, accession Q05584


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: S-D-lactoylglutathione

sequence_source: UniProt REST direct lookup 2026-06-16, accession Q8ZRM2

proof_lines: enzyme obtained from minimal medium supplemented with Fe2+

proof_lines: enzyme obtained from minimal medium supplemented with Zn2+

substrate: S-D-lactoylglutathione


organism: Salmonella typhimurium


organism: Shouchella lehensis


organism: Trypanosoma brucei

substrate_name: bis-(lactoyl)trypanothione

sequence_source: UniProt REST direct lookup 2026-06-16, accession Q6KF36

proof_lines:
pH 7.2, 25°C
recombinant enzyme, pH 7.2, 25°C
above, recombinant enzyme, pH 7.2, 25°C

substrate: bis-(lactoyl)trypanothione


substrate_name: S-hydroxyglutaryltrypanothione

sequence_source: UniProt REST direct lookup 2026-06-16, accession Q581U6

substrate: S-hydroxyglutaryltrypanothione


enzyme_display_name: dGTPase

substrate_name: dGTP

sequence_source: UniProt REST direct lookup 2026-06-16, accession P15723

enzyme: dGTPase

substrate: dGTP


substrate_name: Unknown

substrate: Unknown


organism: Leeuwenhoekiella blandensis

sequence_source: UniProt REST direct lookup 2026-06-16, accession A3XHN1

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication


enzyme_display_name: chymase

organism: Cavia porcellus

enzyme: chymase


organism: Escherichia coli

sequence_source: UniProtKB:P77488 direct accession lookup

column_label: Table 1: Substrate specificity of nitroso substrates (Chembiochem 2013, volume 14, issue 11, pages 1309-1315); printed column heads Substrate | kcat (min^-1) | KM (uM) | kcat/KM, x 10^4 (M^-1 min^-1). Table 1, nitroso substrate row 4; column kcat (min^-1) = 0.9; column KM (uM) = 54; column kcat/KM, x 10^4 (M^-1 min^-1) = 1.7. captured primary segment: Table 1, nitroso substrate 4 | E. coli DXP synthase | kcat 0.9 min^-1 | KM 54 uM | kcat/KM 1.7 x 10^4 M^-1 min^-1 | 100 mM HEPES, pH 8.0, 37 C

normalized_value_unit_evidence: Km: printed Table 1 cell 54 uM; 54 / 1000 = 0.054 mM; the exported value is 0.054 mM. kcat: printed Table 1 cell 0.9 min^-1; 1 min^-1 is 1/60 s^-1, so 0.9 / 60 = 0.015 s^(-1); the exported value is 0.015 s^(-1). kcat/Km: printed Table 1 cell 1.7 x 10^4 M^-1 min^-1; 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1, so 17000 / 60000 = 0.2833333333333333 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.015 / 0.054 = 0.2777777777777778 s^-1 mM^-1, the exported value, and 0.9 / 0.054 = 16.666667 min^-1 mM^-1, that is 1.6666667 x 10^4 M^-1 min^-1, which at the two printed digits of the efficiency column is the printed cell 1.7 x 10^4 M^-1 min^-1.

raw_value_unit_evidence: Table 1, nitroso substrate row 4: kcat = 0.9 min^-1; KM = 54 uM; printed kcat/KM = 1.7 x 10^4 M^-1 min^-1.

row_label: Table 1, nitroso substrate row 4


column_label: Table 1: Substrate specificity of nitroso substrates (Chembiochem 2013, volume 14, issue 11, pages 1309-1315); printed column heads Substrate | kcat (min^-1) | KM (uM) | kcat/KM, x 10^4 (M^-1 min^-1). Table 1, nitroso substrate row 3; column kcat (min^-1) = 36; column KM (uM) = 99; column kcat/KM, x 10^4 (M^-1 min^-1) = 36. captured primary segment: Table 1, nitroso substrate 3 | E. coli DXP synthase | kcat 36 min^-1 | KM 99 uM | kcat/KM 36 x 10^4 M^-1 min^-1 | 100 mM HEPES, pH 8.0, 37 C

normalized_value_unit_evidence: Km: printed Table 1 cell 99 uM; 99 / 1000 = 0.099 mM; the exported value is 0.099 mM. kcat: printed Table 1 cell 36 min^-1; 1 min^-1 is 1/60 s^-1, so 36 / 60 = 0.6 s^(-1); the exported value is 0.6 s^(-1). kcat/Km: printed Table 1 cell 36 x 10^4 M^-1 min^-1; 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1, so 360000 / 60000 = 6.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.6 / 0.099 = 6.06060606060606 s^-1 mM^-1, the exported value, and 36 / 0.099 = 363.63636 min^-1 mM^-1, that is 36.363636 x 10^4 M^-1 min^-1, which at the two printed digits of the efficiency column is the printed cell 36 x 10^4 M^-1 min^-1.

raw_value_unit_evidence: Table 1, nitroso substrate row 3: kcat = 36 min^-1; KM = 99 uM; printed kcat/KM = 36 x 10^4 M^-1 min^-1.

row_label: Table 1, nitroso substrate row 3


sequence_variant_note: Resolved canonical sequence from UniProtKB:P77488 direct accession lookup; variant sequence reconstructed from canonical sequence by applying R478A and applied mutation signature R478A to reconstruct the assayed variant sequence.


substrate_name: D-glyceraldehyde 3-phosphate; 1-methyl-2-nitrosobenzene; 6-bromo-1-nitrosonaphthalen-2-ol; 6-hydroxy-5-nitrosonaphthalene-2-sulfonamide; 1-nitrosonaphthalen-2-ol; N,N-dimethyl-4-nitrosoaniline; 2-hydroxy-4,6-dinitrobenzaldehyde; 7-methoxy-1-nitrosonaphthalen-2-ol; 3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole; pyruvate; D-glyceraldehyde

sequence_source: UniProtKB:P77488 direct accession lookup; canonical accession sequence recorded as identity context

proof_lines: pH 8, temperature not specified in the publication


substrate_name: pyruvate; D-glyceraldehyde 3-phosphate

sequence_source: UniProtKB:P9WNS3 direct accession lookup

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

substrate: pyruvate; D-glyceraldehyde 3-phosphate


substrate_name: D-glyceraldehyde 3-phosphate; pyruvate

sequence_source: UniProtKB:P9WNS3 canonical accession context only; selected source note does not provide a coordinate-validated variant sequence.

proof_lines: mutant lacking loop 190-234, pH 8.0, temperature not specified in the publication

substrate: D-glyceraldehyde 3-phosphate; pyruvate


organism: Plasmodium vivax

sequence_source: UniProtKB:A5K817 direct accession lookup; canonical accession sequence recorded as identity context

proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9KGU7 direct accession lookup; canonical accession sequence recorded as identity context


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9KGU7 direct accession lookup; variant sequence reconstructed from canonical sequence by applying R106A and applied mutation signature R106A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9KGU7 direct accession lookup


organism: Homo sapiens

substrate_name: S-Glycolylglutathione

substrate: S-Glycolylglutathione


substrate_name: (S)-S-Glyceroylglutathione

substrate: (S)-S-Glyceroylglutathione


substrate_name: S-mandeloylglutathione

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

proof_lines:
enzyme from erythrocytes
recombinant enzyme

substrate: S-mandeloylglutathione


substrate_name: (R)-S-Mandeloylglutathione

substrate: (R)-S-Mandeloylglutathione


organism: Leishmania donovani

substrate_name: mono-(lactoyl)trypanothione

substrate: mono-(lactoyl)trypanothione


organism: Leishmania infantum

substrate_name: S-D-lactoyltrypanothione

proof_lines: wild type protein, no activity observed with S-D-lactoylglutathione, pH not specified in the publication, temperature not specified in the publication

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

substrate: S-D-lactoyltrypanothione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y291R/C294K to reconstruct the assayed variant sequence.

proof_lines: Y291R/C294K mutant protein, pH not specified in the publication, temperature not specified in the publication


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Mus musculus

substrate_name: (R)-S-Lactoylglutathione

substrate: (R)-S-Lactoylglutathione


organism: Nostoc sp. PCC 7120 = FACHB-418

proof_lines:
pH 7.5, 25°C
at pH 7.5 and 25°C


organism: Oryza sativa


organism: Plasmodium falciparum


substrate_name: S-Lactoylglutathione

substrate: S-Lactoylglutathione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y185F to reconstruct the assayed variant sequence.


enzyme_display_name: arginine deiminase

organism: Enterococcus faecalis

substrate_name: L-arginine

enzyme: arginine deiminase

substrate: L-arginine


substrate_name: L-Arginine

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

substrate: L-Arginine


proof_lines: pH 6.0, 45°C, mutant enzyme R15K/F269Y/G292P


organism: Giardia duodenalis

substrate_name: L-arginine ethyl ester

sequence_source: UniProtKB Q27657 direct lookup on 2026-06-16; unreviewed TrEMBL entry Q27657_GIAIN for Giardia intestinalis/Giardia lamblia; EC 3.5.3.6.

substrate: L-arginine ethyl ester


organism: Giardia intestinalis


substrate_name: Nomega-amino-L-arginine

substrate: Nomega-amino-L-arginine


organism: Halothermothrix orenii

sequence_source: UniProtKB B8D2J5 direct lookup on 2026-06-16; reviewed Swiss-Prot entry ARCA_HALOH for Halothermothrix orenii strain H 168/OCM 544/DSM 9562; EC 3.5.3.6.


substrate_name: N-alpha-benzoyl-L-arginine ethyl ester

substrate: N-alpha-benzoyl-L-arginine ethyl ester


enzyme_display_name: cathepsin K

sequence_source: UniProtKB REST direct lookup P43235 (UniProtKB reviewed (Swiss-Prot))

enzyme: cathepsin K


proof_lines:
at pH 5.5 and 28°C
at pH 5.5 and 37°C
pH 7.0, 37°C, recombinant enzyme


organism: Rattus norvegicus

sequence_source: UniProtKB REST direct lookup O35186 (UniProtKB reviewed (Swiss-Prot))

proof_lines: pH 7.0, 37°C, recombinant wild-type enzyme


proof_lines: pH 7.0, 37°C, recombinant mutant S134A/V160L


substrate_name: Abz-HPGGPQ-(3 NO2-Tyr)

proof_lines:
at pH 5.5 and 28°C
pH 5.5, 28°C

substrate: Abz-HPGGPQ-(3 NO2-Tyr)


enzyme_display_name: deaminated glutathione amidase

organism: Arabidopsis thaliana

sequence_source: UniProtKB REST direct lookup Q94JV5 (UniProtKB reviewed (Swiss-Prot))

enzyme: deaminated glutathione amidase


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB REST direct lookup P47016 (UniProtKB reviewed (Swiss-Prot))

proof_lines:
pH 8.5, 30°C
Raw SKiD Env: Temp=30°C, pH=8.5


enzyme_display_name: glutathionylspermidine amidase

organism: Trypanosoma brucei

substrate_name: Glutathionylspermidine

sequence_source: UniProtKB REST direct lookup Q8IEX1 (UniProtKB unreviewed (TrEMBL))

enzyme: glutathionylspermidine amidase

substrate: Glutathionylspermidine


organism: Cavia porcellus


substrate_name: Neurotensin

substrate: Neurotensin


substrate_name: Angiotensin I

substrate: Angiotensin I


enzyme_display_name: tryptase

organism: Equus caballus

substrate_name: N-(p-tosyl)-Gly-Pro-Lys-p-nitroanilide

enzyme: tryptase

substrate: N-(p-tosyl)-Gly-Pro-Lys-p-nitroanilide


organism: Homo sapiens


proof_lines: mutant enzyme I99C/Y75A/Y37bA, at pH 6.8 and 25°C

proof_lines: mutant enzyme I99C*/Y75A/Y37bA, at pH 6.8 and 25°C


organism: Pseudomonas aeruginosa

substrate_name: L-Arg

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature E224A to reconstruct the assayed variant sequence.

substrate: L-Arg


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R401L to reconstruct the assayed variant sequence.


substrate_name: N(omega)-amino-L-Arginine

sequence_source: UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json)

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

substrate: N(omega)-amino-L-Arginine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R243K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R185L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R243L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R185A to reconstruct the assayed variant sequence.


substrate_name: Nomega-amino-Arg

substrate: Nomega-amino-Arg


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R401A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature E224D to reconstruct the assayed variant sequence.


substrate_name: N(omega)-methyl-L-Arginine

smiles: CN=C(N)NCCCC(N)C(=O)O

substrate: N(omega)-methyl-L-Arginine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13981 direct accession lookup (https://rest.uniprot.org/uniprotkb/P13981.json) and applied mutation signature R243A to reconstruct the assayed variant sequence.


proof_lines:
at pH 5.6 and 25°C
pH 5.6, 25°C
Raw SKiD Env: Temp=25°C, pH=5.6


organism: Pseudomonas plecoglossicida

sequence_variant_note: Resolved canonical sequence from UniProtKB:A7LKB0 direct accession lookup (https://rest.uniprot.org/uniprotkb/A7LKB0.json) and applied mutation signature K30R/C37R/L148P/V291L to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme K30R/C37R/L148P/V291L


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7LKB0 direct accession lookup (https://rest.uniprot.org/uniprotkb/A7LKB0.json) and applied mutation signature K30R/C37R/G129S/L148P/V291L to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme K30R/C37R/G129S/L148P/V291L


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7LKB0 direct accession lookup (https://rest.uniprot.org/uniprotkb/A7LKB0.json) and applied mutation signature K5T/D38H/D44E/A128T/E296K/H404R to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme K5T/D38H/D44E/A128T/E296K/H404R


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7LKB0 direct entry plus reconstructed A128T/I410L substitutions and applied mutation signature A128T/I410L to reconstruct the assayed variant sequence.


proof_lines: pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K


organism: Pseudomonas putida

sequence_source: UniProtKB:Q88P52 direct entry

proof_lines: pH and temperature not specified in the publication


organism: Streptococcus pyogenes

sequence_source: UniProtKB:B5XMC3 direct entry


enzyme_display_name: 2,3-epoxybenzoyl-CoA dihydrolase

organism: Aromatoleum evansii

sequence_source: UniProtKB:Q84HH6 direct entry

assay_conditions_summary: cofactor CoA

enzyme: 2,3-epoxybenzoyl-CoA dihydrolase


organism: Azoarcus evansii

assay_conditions_summary: pH 9; 295.15 K; cofactor CoA


enzyme_display_name: L-threo-3-deoxy-hexylosonate aldolase

organism: Trichoderma reesei

substrate_name: pyruvate

sequence_source: UniProtKB:A6Y9S5 direct entry

enzyme: L-threo-3-deoxy-hexylosonate aldolase

substrate: pyruvate


substrate_name: L-Glyceraldehyde

substrate: L-Glyceraldehyde


enzyme_display_name: indole-3-glycerol-phosphate lyase

organism: Oryza sativa

sequence_source: UniProtKB:Q7Y1I9 direct entry

enzyme: indole-3-glycerol-phosphate lyase


organism: Lactococcus lactis subsp. lactis

sequence_source: UniProt REST Q2HYA0


organism: Metapseudomonas furukawaii

sequence_source: UniProt REST A0AAD1C5K5


organism: Mycoplasma arthritidis

sequence_source: UniProt REST Q9RND4


organism: Mycoplasmopsis arginini

sequence_source: UniProt REST P23793


sequence_variant_note: Resolved canonical sequence from UniProt REST P13981 with N160A reconstruction and applied mutation signature N160A to reconstruct the assayed variant sequence.


organism: Rhodobacter capsulatus

proof_lines: pH 7.4, 37°C, cosubstrate: D-glyceraldehyde 3-phosphate


organism: Unknown

substrate_name: Unknown

substrate: Unknown


organism: Arabidopsis thaliana

substrate_name: S-D-mandeloylglutathione

proof_lines: recombinant cytosolic isozyme, minimal medium, pH 7.2, 25°C

proof_lines: pH 7.2, 25°C, growth on minimal medium without added metal ion

proof_lines: recombinant cytosolic isozyme, medium with Zn added, pH 7.2, 25°C

substrate: S-D-mandeloylglutathione


organism: Bos taurus

proof_lines: mitochondrial isozyme, pH 7.2, 25°C, in presence of cardiolipin

proof_lines: mitochondrial isozyme, pH 7.2, 25°C, in presence of dioleoyl phosphatidic acid


organism: Homo sapiens

proof_lines:
enzyme from brain
enzyme from liver
brain


substrate_name: S-D-lactoylglutathione

substrate: S-D-lactoylglutathione


organism: Cavia porcellus

substrate_name: Benzyloxycarbonyl-Gln-Gly

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

substrate: Benzyloxycarbonyl-Gln-Gly


sequence_source: UniProtKB:H0VXN6 direct REST lookup 2026-06-16


substrate_name: Z-Glu(HMC)-Gly-OH

substrate: Z-Glu(HMC)-Gly-OH


substrate_name: Z-Glu(HC)-Gly-OH

substrate: Z-Glu(HC)-Gly-OH


proof_lines: pH 6.5, 30°C, with/versus substrate Z-Glu(HMC)-Gly-OH


substrate_name: pentylamine

sequence_source: UniProtKB:A0A286XL02 direct REST lookup 2026-06-16

smiles: CCCCCN

substrate: pentylamine


substrate_name: N,N'-dimethyl casein glutamine

sequence_source: UniProtKB:P21980 direct REST lookup 2026-06-16

proof_lines: pH 7.5, 37°C, recombinant TG2 without DNAJA1

proof_lines: 0.05 mM EDTA, 3.3 mM CaCl2, in 0.11 M MOPS at pH 7.0 and 25°C

substrate: N,N'-dimethyl casein glutamine


organism: Pacifastacus leniusculus

sequence_source: UniProtKB:Q964D3 direct REST lookup 2026-06-16


organism: Paracentrotus lividus

substrate_name: GTP

sequence_source: UniProtKB:Q8T316 direct REST lookup 2026-06-16

substrate: GTP


organism: Streptomyces cinnamoneus

substrate_name: L-lysine

sequence_source: UniProtKB:Q8GR90 direct REST lookup 2026-06-16

proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme

substrate: L-lysine


organism: Streptomyces hygroscopicus

substrate_name: N-Cbz-Gln-Gly

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

proof_lines: mutant enzyme N160Q/N355Q, at pH 6.0 and 37°C

substrate: N-Cbz-Gln-Gly


sequence_source: UniProtKB Q7Y1I9 REST lookup


organism: Zea mays

substrate_name: indole-3-glycerol phosphate

sequence_source: UniProtKB Q9FQ77 REST lookup

substrate: indole-3-glycerol phosphate


sequence_source: UniProtKB B2Y0K4 REST lookup


substrate_name: (3-Indolyl)-glycerol phosphate

sequence_source: UniProtKB P42390 REST lookup

substrate: (3-Indolyl)-glycerol phosphate


enzyme_display_name: (R)-2-methylmalate dehydratase

organism: Methanocaldococcus jannaschii

substrate_name: D-Citramalate

enzyme: (R)-2-methylmalate dehydratase

substrate: D-Citramalate


sequence_source: UniProt REST P43235 FASTA direct check


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

assay_conditions_summary: pH 5.5; 301.15 K; buffer 100 mM sodium acetate

proof_lines: mutant enzyme K9E/N190M/K191G/L195K , in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C

proof_lines: mutant enzyme K9E/N190M/K191G/L195K, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


proof_lines: wild type enzyme, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


proof_lines: mutant enzyme K9E, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


proof_lines: mutant enzyme N190M/K191G/L195K, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


proof_lines: mutant enzyme K9E/I171E/Q172S/N190M/K191G/L195K, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


organism: Pseudomonas plecoglossicida

substrate_name: L-arginine

sequence_source: UniProt REST A7LKB0 FASTA direct check

substrate: L-arginine


proof_lines: pH 7.4, 37°C, mutant enzyme A128T/H404/I410L


substrate_name: L-Arginine

substrate: L-Arginine


organism: Escherichia coli (strain K12)

substrate_name: lauroyl-ACP

source_db: uniprot

substrate: lauroyl-ACP

source: uniprot


organism: Cavia cutleri

substrate_name: serotonin (for protein-glutamine serotonyltransferase activity)


substrate_name: PATH

substrate: PATH


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

substrate_name: S-adenosylmethioninamine (at 78 degrees Celsius and at pH 7.5)


organism: Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)

substrate_name: O-phospho-L-serine

substrate: O-phospho-L-serine


substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


substrate: S-adenosylmethioninamine (at 78 degrees Celsius and at pH 7.5)


enzyme_display_name: sedoheptulokinase

substrate_name: sedoheptulose

enzyme: sedoheptulokinase

substrate: sedoheptulose


organism: Mus musculus


enzyme_display_name: CTP-dependent riboflavin kinase

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

substrate_name: riboflavin

enzyme: CTP-dependent riboflavin kinase

substrate: riboflavin


enzyme_display_name: alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase

substrate_name: GTP (in the presence of PhnI alone)

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 1.4 sec(-1) for ATP hydrolysis in the presence of PhnI alone, and 20 sec(-1) for RPnTP synthesis from ATP in the presence of PhnI, PhnG, PhnH and PhnL.

substrate: GTP (in the presence of PhnI alone)


enzyme_display_name: (3S)-malyl-CoA thioesterase

substrate_name: (3S)-citramalyl-CoA (for citramalyl-CoA lyase activity)

proof_lines: kcat is 0.12 sec(-1) for malate synthase reaction (PubMed:24334609). kcat is 0.09 sec(-1) for beta-methylmalate synthase reaction (PubMed:24334609). kcat is 0.135 sec(-1) for beta-methylmalate synthase reaction (PubMed:29056341). kcat is 0.

enzyme: (3S)-malyl-CoA thioesterase


enzyme_display_name: hydroxyacylglutathione hydrolase

substrate_name: (R)-S-lactoylglutathione

proof_lines: kcat is 53 sec(-1) for the hydrolysis of (R)-S-lactoylglutathione (PubMed:17196158). kcat is 15.6 sec(-1) for the hydrolysis of (R)-S-lactoylglutathione (PubMed:25670698).

enzyme: hydroxyacylglutathione hydrolase

substrate: (R)-S-lactoylglutathione


proof_lines: kcat is 0.9 sec(-1) for the hydrolysis of (R)-S-lactoylglutathione.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 979 sec(-1) with (R)-S-lactoylglutathione as substrate and 35.1 sec(-1) with (R)-S-mandeloylglutathione as substrate.


proof_lines: kcat is 605 sec(-1) with (R)-S-lactoylglutathione as substrate and 38.1 sec(-1) with (R)-S-mandeloylglutathione as substrate.


substrate_name: ATP (at pH 6.8)

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: kcat is 7 sec(-1) for Gsp synthetase activity at pH 6.8 and 2.1 sec(-1) for Gsp amidase activity at pH 7.5.

substrate: ATP (at pH 6.8)


organism: Aromatoleum evansii

proof_lines: The substrate was earlier believed to be 2,3-dihydro-2,3-dihydroxybenzoyl-CoA but it has later been shown to be the epoxide as the substrate was enzymatically produced by BoxAB.


substrate_name: indole-3-glycerol phosphate

proof_lines: kcat is 0.02 sec(-1) with indole-3-glycerol phosphate as substrate.


enzyme_display_name: L-methionine (S)-S-oxide reductase

organism: Saccharomyces cerevisiae

substrate_name: L-(-)-methionine S-oxide

enzyme: L-methionine (S)-S-oxide reductase

substrate: L-(-)-methionine S-oxide


enzyme_display_name: 1-deoxy-D-xylulose-5-phosphate synthase

organism: Agrobacterium tumefaciens

substrate_name: D-glyceraldehyde 3-phosphate

enzyme: 1-deoxy-D-xylulose-5-phosphate synthase

substrate: D-glyceraldehyde 3-phosphate


organism: Deinococcus radiodurans


substrate_name: pyruvate

substrate: pyruvate


proof_lines: pH and temperature not specified in the publication


organism: Escherichia coli

proof_lines:
pH 8.0, 37°C
Ki above 0.2 mM, at pH 8.0 and 37°C
Ki above 0.1 mM, at pH 8.0 and 37°C


substrate_name: N-Cbz-Gln-Gly

substrate: N-Cbz-Gln-Gly


organism: Streptomyces mobaraensis

substrate_name: Z-Gln-Gly

sequence_source: UniProtKB reviewed entry P81453, direct REST lookup on 2026-06-16

substrate: Z-Gln-Gly


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry P81453, direct REST lookup on 2026-06-16 and applied mutation signature S2P with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant S2P, pH 7.2, 37°C
recombinant mutant S2P, pH 6.0, 37°C


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

proof_lines: recombinant wild-type enzyme, pH 7.2, 37°C

proof_lines: recombinant wild-type enzyme, pH 6.0, 37°C

proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme


substrate_name: CBZ-Gln-Gly-OH

substrate: CBZ-Gln-Gly-OH


proof_lines: pH 8.0, 37°C, recombinant chimeric mutant


substrate_name: N-CBZ-Glu-Gly

substrate: N-CBZ-Glu-Gly


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


organism: Homo sapiens

sequence_source: UniProtKB reviewed entry P43235, direct REST lookup on 2026-06-16

sequence_variant_note: Mutation signature K9E/I171E/Q172S/N190M/K191G/L195K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K9E/N190M/K191G/L195K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K9E/I171E/Q172S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 5.5; buffer 100 mM sodium acetate

proof_lines: mutant enzyme K9E/I171E/Q172S, in 100 mM sodium acetate buffer, pH 5.5, containing 2.5 mM dithiothreitol, and 2.5 mM EDTA, at 28°C


enzyme_display_name: nicotinamidase

substrate_name: nicotinamide

sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature D51A and applied mutation signature D51A to reconstruct the assayed variant sequence.

proof_lines: Km below 0.0024 mM, mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C

proof_lines: kcat/Km above 8.3 (1/sec*mM), mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C

enzyme: nicotinamidase

substrate: nicotinamide


sequence_source: UniProtKB:P53184 reviewed canonical FASTA direct lookup

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

column_label: Table 4 (Steady-state kinetic parameters and 15N and 13C KIE for the reaction catalyzed by Pnc1 with alternate substrates), body row 'nicotinamide': column 'kcat (s-1)' = 0.69; column 'Km (uM)' = 9.6; column 'kcat/Km (M-1 s-1)' = 7.2 x 10^4. The number printed after the plus/minus sign beside the kcat and Km cells of this line is the printed uncertainty and is not an exported metric. The 15N KIE and 13C KIE columns of the same line print 1.0122 and 1.0125, which are isotope effects and not kinetic metric fields the export schema carries.

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.69 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.69 s^(-1). Km: printed Table 4 cell 9.6 in a column headed Km (uM); 1 uM is 0.001 mM, so 9.6 / 1000 = 0.0096 mM. kcat/Km: printed Table 4 cell 7.2 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.2 x 10^4 / 1000 = 72.0 s^(-1)*mM^(-1). The exported values are kcat 2.56 s^(-1) and Km 0.0096 mM.

raw_value_unit_evidence: Table 4, body row 'nicotinamide': kcat = 0.69 s-1; Km = 9.6 uM; printed kcat/Km = 7.2 x 10^4 in a column headed kcat/Km (M-1 s-1).

row_label: Table 4, row nicotinamide

table_label: Table 4: Steady-state kinetic parameters and 15N and 13C KIE for the reaction catalyzed by Pnc1 with alternate substrates (Biochemistry 2012, 51(1):243-256). Printed column heads: Substrate; Structure; kcat (s-1); Km (uM); kcat/Km (M-1 s-1); 15N KIE; 13C KIE.


substrate_name: Benzamide

column_label: Table 4 (Steady-state kinetic parameters and 15N and 13C KIE for the reaction catalyzed by Pnc1 with alternate substrates), body row 'benzamide': column 'kcat (s-1)' = 0.0088; column 'Km (uM)' = 25; column 'kcat/Km (M-1 s-1)' = 3.5 x 10^2. The number printed after the plus/minus sign beside the kcat and Km cells of this line is the printed uncertainty and is not an exported metric. The 15N KIE and 13C KIE columns of the same line print ND, so the paper reports no isotope effect for this line.

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.0088 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.0088 s^(-1). Km: printed Table 4 cell 25 in a column headed Km (uM); 1 uM is 0.001 mM, so 25 / 1000 = 0.025 mM. kcat/Km: printed Table 4 cell 3.5 x 10^2 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.5 x 10^2 / 1000 = 0.35 s^(-1)*mM^(-1). The exported values are kcat 0.0088 s^(-1), Km 0.025 mM and kcat_over_km 0.352 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row 'benzamide': kcat = 0.0088 s-1; Km = 25 uM; printed kcat/Km = 3.5 x 10^2 in a column headed kcat/Km (M-1 s-1).

row_label: Table 4, row benzamide

substrate: Benzamide


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature D51N and applied mutation signature D51N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P53184 canonical FASTA plus selected mutation_signature D51N

proof_lines: Km below 0.0018 mM, mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C

proof_lines: kcat/Km above 35 (1/sec*mM), mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C


substrate_name: Pyrazinamide

column_label: Table 4 (Steady-state kinetic parameters and 15N and 13C KIE for the reaction catalyzed by Pnc1 with alternate substrates), body row 'pyrazinamide': column 'kcat (s-1)' = 2.56; column 'Km (uM)' = 157; column 'kcat/Km (M-1 s-1)' = 1.6 x 10^4. The number printed after the plus/minus sign beside the kcat and Km cells of this line is the printed uncertainty and is not an exported metric. The 15N KIE and 13C KIE columns of the same line print 1.0231 and 1.0196, which are isotope effects and not kinetic metric fields the export schema carries.

normalized_value_unit_evidence: kcat: printed Table 4 cell 2.56 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.56 s^(-1). Km: printed Table 4 cell 157 in a column headed Km (uM); 1 uM is 0.001 mM, so 157 / 1000 = 0.157 mM. kcat/Km: printed Table 4 cell 1.6 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^4 / 1000 = 16.0 s^(-1)*mM^(-1). The exported values are kcat 2.56 s^(-1), Km 0.157 mM and kcat_over_km 16.305732484076433 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row 'pyrazinamide': kcat = 2.56 s-1; Km = 157 uM; printed kcat/Km = 1.6 x 10^4 in a column headed kcat/Km (M-1 s-1).

row_label: Table 4, row pyrazinamide

substrate: Pyrazinamide


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature K122R and applied mutation signature K122R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K122R, in 50 mM sodium phosphate (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature D8E and applied mutation signature D8E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D8E, in 50 mM sodium phosphate (pH 7.5), at 25°C


column_label: Table 4 (Steady-state kinetic parameters and 15N and 13C KIE for the reaction catalyzed by Pnc1 with alternate substrates), body row '5-methylnicotinamide': column 'kcat (s-1)' = 1.75; column 'Km (uM)' = 61; column 'kcat/Km (M-1 s-1)' = 2.9 x 10^4. The number printed after the plus/minus sign beside the kcat and Km cells of this line is the printed uncertainty and is not an exported metric. The 15N KIE and 13C KIE columns of the same line print 1.0151 and 1.0269, which are isotope effects and not kinetic metric fields the export schema carries.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.75 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.75 s^(-1). Km: printed Table 4 cell 61 in a column headed Km (uM); 1 uM is 0.001 mM, so 61 / 1000 = 0.061 mM. kcat/Km: printed Table 4 cell 2.9 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^4 / 1000 = 29.0 s^(-1)*mM^(-1). The exported values are kcat 1.75 s^(-1), Km 0.061 mM and kcat_over_km 28.688524590163937 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, body row '5-methylnicotinamide': kcat = 1.75 s-1; Km = 61 uM; printed kcat/Km = 2.9 x 10^4 in a column headed kcat/Km (M-1 s-1).

row_label: Table 4, row 5-methylnicotinamide


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature H94A and applied mutation signature H94A to reconstruct the assayed variant sequence.

proof_lines: Km below 0.0027 mM, mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C

proof_lines: kcat/Km above 7.4 (1/sec*mM), mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature K122A and applied mutation signature K122A to reconstruct the assayed variant sequence.

proof_lines: Km below 0.0065 mM, mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C

proof_lines: kcat/Km above 6.7 (1/sec*mM), mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature D8A and applied mutation signature D8A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D8A, in 50 mM sodium phosphate (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical FASTA plus selected mutation_signature D8N and applied mutation signature D8N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D8N, in 50 mM sodium phosphate (pH 7.5), at 25°C


normalized_value_unit_evidence: kcat: printed Table 4 cell 0.69 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.69 s^(-1). Km: printed Table 4 cell 9.6 in a column headed Km (uM); 1 uM is 0.001 mM, so 9.6 / 1000 = 0.0096 mM. kcat/Km: printed Table 4 cell 7.2 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.2 x 10^4 / 1000 = 72.0 s^(-1)*mM^(-1). The exported values are kcat 0.69 s^(-1), Km 0.0096 mM and kcat_over_km 71.875 s^(-1)*mM^(-1).


sequence_source: UniProtKB:P53184 canonical FASTA plus selected mutation_signature D51A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P53184 and applied mutation signature H53A to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-state kinetic parameters of Pnc1 mutants), body row 'H53A': column 'kcat (s-1)' = 0.014; column 'Km (uM)' = 6.5; column 'kcat/Km (M-1 s-1)' = 2.2 x 10^3. The number printed after the plus/minus sign beside the kcat and Km cells of this line is the printed uncertainty and is not an exported metric. The 15N KIE and 13C KIE columns of the same line print ND, so the paper reports no isotope effect for this line.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.014 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.014 s^(-1). Km: printed Table 3 cell 6.5 in a column headed Km (uM); 1 uM is 0.001 mM, so 6.5 / 1000 = 0.0065 mM. kcat/Km: printed Table 3 cell 2.2 x 10^3 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.2 x 10^3 / 1000 = 2.2 s^(-1)*mM^(-1). The exported values are kcat 0.014 s^(-1), Km 0.0065 mM and kcat_over_km 2.153846153846154 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, body row 'H53A': kcat = 0.014 s-1; Km = 6.5 uM; printed kcat/Km = 2.2 x 10^3 in a column headed kcat/Km (M-1 s-1).

row_label: Table 3, row H53A

table_label: Table 3: Steady-state kinetic parameters of Pnc1 mutants (Biochemistry 2012, 51(1):243-256). Printed column heads: Pnc1 mutant; kcat (s-1); Km (uM); kcat/Km (M-1 s-1); 15N KIE; 13C KIE.


organism: Oceanobacillus iheyensis

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8ESQ6 canonical FASTA direct lookup on 2026-06-16 with Q96A reconstructed after canonical residue-coordinate validation and applied mutation signature Q96A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8ESQ6 canonical FASTA direct lookup on 2026-06-16 with Q96K reconstructed after canonical residue-coordinate validation and applied mutation signature Q96K to reconstruct the assayed variant sequence.


substrate_name: ethyl nicotinate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8ESQ6 canonical FASTA direct lookup on 2026-06-16 with C133A reconstructed after canonical residue-coordinate validation and applied mutation signature C133A to reconstruct the assayed variant sequence.

substrate: ethyl nicotinate


sequence_source: UniProtKB Q8ESQ6 canonical FASTA direct lookup on 2026-06-16 with Q96K reconstructed after canonical residue-coordinate validation


substrate_name: methyl nicotinate

sequence_source: UniProtKB Q8ESQ6 canonical FASTA direct lookup on 2026-06-16 with Q96A reconstructed after canonical residue-coordinate validation

substrate: methyl nicotinate


sequence_source: UniProtKB Q8ESQ6 canonical sequence checked on 2026-06-16, but row-specific variant sequence was not accepted.

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


sequence_source: UniProtKB Q8ESQ6 canonical FASTA direct lookup on 2026-06-16

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


substrate_name: 5-methyl nicotinamide

substrate: 5-methyl nicotinamide


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8ESQ6 canonical sequence checked on 2026-06-16, but row-specific variant sequence was not accepted. and applied mutation signature Q96K to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8ESQ6 canonical FASTA direct lookup on 2026-06-16 with C133A reconstructed after canonical residue-coordinate validation


organism: uncultured Acidobacteria bacterium

substrate_name: methylnicotinate

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

substrate: methylnicotinate


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


substrate_name: ethylnicotinate

substrate: ethylnicotinate


organism: uncultured Acidobacteriota bacterium


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: catechol O-methyltransferase

substrate_name: dopamine

enzyme: catechol O-methyltransferase

substrate: dopamine


organism: Mycolicibacterium smegmatis

sequence_source: GenBank AF058285.1 CDS protein_id AAC77368.1 from PMID 9811635; UniProt Q9ZHK8 sequence cross-check


sequence_variant_note: Resolved canonical sequence from NCBI Protein BAL58158.1 canonical sequence plus PMID 28750065 H75E site-directed mutagenesis; reconstructed by replacing residue 75 H with E. and applied mutation signature H75E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ESQ6 and applied mutation signature Q96K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 310.15 K; buffer 100 mM phosphate; cofactor NADPH

column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Q96K, substrate row 5-methyl-NAM; column Specific activity (U/mg) = 3.96±0.12; column Km (mM) = 0.62; column k cat (s-1) = 2.16; column k cat/Km (mM-1 s-1) = 3.40. captured primary segment: 5-methyl-NAM | Q96K OiNIC | Km 0.62 mM | kcat 2.16 s^-1 | kcat/Km 3.40 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.62 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.62 mM. kcat: printed Table 1 k cat cell 2.16 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 2.16 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 3.40 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 3.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.16 / 0.62 = 3.483870967741936 s^-1 mM^-1, against the printed efficiency cell 3.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Q96K, substrate row 5-methyl-NAM: Km = 0.62 mM; k cat = 2.16 s^-1; k cat/Km = 3.40 mM^-1 s^-1; Specific activity = 3.96±0.12 U/mg.


column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Wild-type, substrate row NAM; column Specific activity (U/mg) = 23.3a/25.0 b±0.5; column Km (mM) = 0.26; column k cat (s-1) = 11.65; column k cat/Km (mM-1 s-1) = 43.48. captured primary segment: NAM | wild-type OiNIC | Km 0.26 mM | kcat 11.65 s^-1 | kcat/Km 43.48 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.26 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.26 mM. kcat: printed Table 1 k cat cell 11.65 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 11.65 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 43.48 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 43.48 s^(-1)*mM^(-1). Quotient disclosure for this row: 11.65 / 0.26 = 44.80769230769231 s^-1 mM^-1, against the printed efficiency cell 43.48 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Wild-type, substrate row NAM: Km = 0.26 mM; k cat = 11.65 s^-1; k cat/Km = 43.48 mM^-1 s^-1; Specific activity = 23.3a/25.0 b±0.5 U/mg.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ESQ6 and applied mutation signature Q96A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Q96A, substrate row PZA; column Specific activity (U/mg) = 1.80±0.2; column Km (mM) = 1.20; column k cat (s-1) = 1.61; column k cat/Km (mM-1 s-1) = 1.34. captured primary segment: PZA | Q96A OiNIC | Km 1.20 mM | kcat 1.61 s^-1 | kcat/Km 1.34 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 1.20 mM; the printed column is already in millimolar, so no conversion is applied and the value is 1.2 mM. kcat: printed Table 1 k cat cell 1.61 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 1.61 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 1.34 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 1.34 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.61 / 1.2 = 1.3416666666666668 s^-1 mM^-1, against the printed efficiency cell 1.34 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Q96A, substrate row PZA: Km = 1.20 mM; k cat = 1.61 s^-1; k cat/Km = 1.34 mM^-1 s^-1; Specific activity = 1.80±0.2 U/mg.


column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Wild-type, substrate row Ethylnicotinate; column Specific activity (U/mg) = 0.13±0.01; column Km (mM) = 1.02; column k cat (s-1) = 0.10; column k cat/Km (mM-1 s-1) = 0.10. captured primary segment: Ethylnicotinate | wild-type OiNIC | Km 1.02 mM | kcat 0.10 s^-1 | kcat/Km 0.10 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 1.02 mM; the printed column is already in millimolar, so no conversion is applied and the value is 1.02 mM. kcat: printed Table 1 k cat cell 0.10 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 0.1 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 0.10 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 0.1 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.1 / 1.02 = 0.09803921568627451 s^-1 mM^-1, against the printed efficiency cell 0.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Wild-type, substrate row Ethylnicotinate: Km = 1.02 mM; k cat = 0.10 s^-1; k cat/Km = 0.10 mM^-1 s^-1; Specific activity = 0.13±0.01 U/mg.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ESQ6 and applied mutation signature E65H to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block E65H, substrate row PZA; column Specific activity (U/mg) = 0.70±0.03; column Km (mM) = 0.82; column k cat (s-1) = 0.43; column k cat/Km (mM-1 s-1) = 0.52. captured primary segment: PZA | E65H OiNIC | Km 0.82 mM | kcat 0.43 s^-1 | kcat/Km 0.52 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.82 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.82 mM. kcat: printed Table 1 k cat cell 0.43 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 0.43 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 0.52 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 0.52 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.43 / 0.82 = 0.524390243902439 s^-1 mM^-1, against the printed efficiency cell 0.52 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block E65H, substrate row PZA: Km = 0.82 mM; k cat = 0.43 s^-1; k cat/Km = 0.52 mM^-1 s^-1; Specific activity = 0.70±0.03 U/mg.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ESQ6 and applied mutation signature C133A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block C133A, substrate row PZA; column Specific activity (U/mg) = 6.39±0.2; column Km (mM) = 0.36; column k cat (s-1) = 3.31; column k cat/Km (mM-1 s-1) = 9.19. captured primary segment: PZA | C133A OiNIC | Km 0.36 mM | kcat 3.31 s^-1 | kcat/Km 9.19 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.36 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.36 mM. kcat: printed Table 1 k cat cell 3.31 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 3.31 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 9.19 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 9.19 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.31 / 0.36 = 9.194444444444445 s^-1 mM^-1, against the printed efficiency cell 9.19 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block C133A, substrate row PZA: Km = 0.36 mM; k cat = 3.31 s^-1; k cat/Km = 9.19 mM^-1 s^-1; Specific activity = 6.39±0.2 U/mg.


column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block C133A, substrate row Ethylnicotinate; column Specific activity (U/mg) = 0.34±0.02; column Km (mM) = 0.34; column k cat (s-1) = 0.14; column k cat/Km (mM-1 s-1) = 0.41. captured primary segment: Ethylnicotinate | C133A OiNIC | Km 0.34 mM | kcat 0.14 s^-1 | kcat/Km 0.41 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.34 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.34 mM. kcat: printed Table 1 k cat cell 0.14 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 0.14 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 0.41 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 0.41 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.14 / 0.34 = 0.411764705882353 s^-1 mM^-1, against the printed efficiency cell 0.41 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block C133A, substrate row Ethylnicotinate: Km = 0.34 mM; k cat = 0.14 s^-1; k cat/Km = 0.41 mM^-1 s^-1; Specific activity = 0.34±0.02 U/mg.


column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Q96K, substrate row Methylnicotinate; column Specific activity (U/mg) = 0.31±0.02; column Km (mM) = 0.44; column k cat (s-1) = 0.17; column k cat/Km (mM-1 s-1) = 0.38. captured primary segment: Methylnicotinate | Q96K OiNIC | Km 0.44 mM | kcat 0.17 s^-1 | kcat/Km 0.38 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.44 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.44 mM. kcat: printed Table 1 k cat cell 0.17 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 0.17 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 0.38 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 0.38 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.17 / 0.44 = 0.3863636363636364 s^-1 mM^-1, against the printed efficiency cell 0.38 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Q96K, substrate row Methylnicotinate: Km = 0.44 mM; k cat = 0.17 s^-1; k cat/Km = 0.38 mM^-1 s^-1; Specific activity = 0.31±0.02 U/mg.


column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Q96A, substrate row 5-methyl-NAM; column Specific activity (U/mg) = 28.0±0.1; column Km (mM) = 0.55; column k cat (s-1) = 15.90; column k cat/Km (mM-1 s-1) = 29.04. captured primary segment: 5-methyl-NAM | Q96A OiNIC | Km 0.55 mM | kcat 15.90 s^-1 | kcat/Km 29.04 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.55 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.55 mM. kcat: printed Table 1 k cat cell 15.90 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 15.9 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 29.04 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 29.04 s^(-1)*mM^(-1). Quotient disclosure for this row: 15.9 / 0.55 = 28.909090909090907 s^-1 mM^-1, against the printed efficiency cell 29.04 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Q96A, substrate row 5-methyl-NAM: Km = 0.55 mM; k cat = 15.90 s^-1; k cat/Km = 29.04 mM^-1 s^-1; Specific activity = 28.0±0.1 U/mg.


column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Wild-type, substrate row 5-methyl-NAM; column Specific activity (U/mg) = 9.01±0.1; column Km (mM) = 0.68; column k cat (s-1) = 5.10; column k cat/Km (mM-1 s-1) = 7.50. captured primary segment: 5-methyl-NAM | wild-type OiNIC | Km 0.68 mM | kcat 5.10 s^-1 | kcat/Km 7.50 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.68 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.68 mM. kcat: printed Table 1 k cat cell 5.10 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 5.1 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 7.50 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 7.5 s^(-1)*mM^(-1). Quotient disclosure for this row: 5.1 / 0.68 = 7.499999999999999 s^-1 mM^-1, against the printed efficiency cell 7.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Wild-type, substrate row 5-methyl-NAM: Km = 0.68 mM; k cat = 5.10 s^-1; k cat/Km = 7.50 mM^-1 s^-1; Specific activity = 9.01±0.1 U/mg.


column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block C133A, substrate row 5-methyl-NAM; column Specific activity (U/mg) = 11.74±0.2; column Km (mM) = 0.64; column k cat (s-1) = 7.09; column k cat/Km (mM-1 s-1) = 11.07. captured primary segment: 5-methyl-NAM | C133A OiNIC | Km 0.64 mM | kcat 7.09 s^-1 | kcat/Km 11.07 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.64 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.64 mM. kcat: printed Table 1 k cat cell 7.09 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 7.09 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 11.07 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 11.07 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.09 / 0.64 = 11.078125 s^-1 mM^-1, against the printed efficiency cell 11.07 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block C133A, substrate row 5-methyl-NAM: Km = 0.64 mM; k cat = 7.09 s^-1; k cat/Km = 11.07 mM^-1 s^-1; Specific activity = 11.74±0.2 U/mg.


proof_lines: about 3fold higher than with pyrazinamide as substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical sequence with selected mutation H53A reconstructed by direct residue check and applied mutation signature H53A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical sequence with selected mutation H94A reconstructed by direct residue check and applied mutation signature H94A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53184 canonical sequence with selected mutation K122A reconstructed by direct residue check and applied mutation signature K122A to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


enzyme_display_name: anhydro-N-acetylmuramic acid kinase

organism: Escherichia coli (strain K12)

substrate_name: anhMurNAc

enzyme: anhydro-N-acetylmuramic acid kinase

substrate: anhMurNAc


enzyme_display_name: glycoprotein-mannosyl O(6)-kinase

substrate_name: ATP

enzyme: glycoprotein-mannosyl O(6)-kinase

substrate: ATP


enzyme_display_name: tRNA uracil 4-sulfurtransferase

enzyme: tRNA uracil 4-sulfurtransferase


enzyme_display_name: keratan sulfotransferase

enzyme: keratan sulfotransferase


organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)

substrate_name: (3S)-malyl-CoA (in the presence of Mg(2+) or Mn(2+))


organism: Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

substrate_name: (S)-malyl-CoA (cleavage reaction)

substrate: (S)-malyl-CoA (cleavage reaction)


organism: Arabidopsis thaliana

substrate_name: S-D-lactoylglutathion

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

substrate: S-D-lactoylglutathion


substrate_name: S-D-lactoylglutathione

substrate: S-D-lactoylglutathione


enzyme_display_name: glutamyl aminopeptidase

organism: Bitis rhinoceros

substrate_name: Glu-AMC (in presence of 1.2 mM Ca(2+))

enzyme: glutamyl aminopeptidase

substrate: Glu-AMC (in presence of 1.2 mM Ca(2+))


substrate_name: nicotinamide

substrate: nicotinamide


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from Direct UniProt REST FASTA lookup for P53184; C167A reconstructed from residue 167 of the canonical sequence. and applied mutation signature C167A to reconstruct the assayed variant sequence.

proof_lines: kcat below 0.0005 s-1, mutant enzyme C167A, in 50 mM sodium phosphate (pH 7.5), at 25°C


organism: Thermus thermophilus

proof_lines: pH and temperature not specified in the publication


substrate_name: Pyrazinamide


sequence_variant_note: Resolved canonical sequence from UniProt P21964-2 soluble isoform FASTA; mutation positions match selected COMT mutation signature directly and applied mutation signature Y68A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme Y68A, at pH 7.5 and 10°C
mutant enzyme Y68A, at pH 7.4 and 37°C
mutant enzyme Y68A, at pH 7.5 and 20°C


sequence_source: UniProt P21964 canonical FASTA direct accession lookup

proof_lines:
wild type enzyme, at pH 7.5 and 5°C
wild type enzyme, at pH 7.5 and 29°C
wild type enzyme, at pH 7.5 and 33°C


sequence_variant_note: Resolved canonical sequence from UniProt P21964-2 soluble isoform FASTA; mutation positions match selected COMT mutation signature directly and applied mutation signature W143F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P21964-2 soluble isoform FASTA; mutation positions match selected COMT mutation signature directly and applied mutation signature W143F/Y68A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W143F/Y68A, at pH 7.4 and 37°C


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

proof_lines: enzyme from liver microsomal fraction, at pH 7.4 and 37°C


substrate_name: epinephrine

sequence_source: UniProt P22734 canonical FASTA direct accession lookup

proof_lines: enzyme from pooled liver S9, at pH 7.4 and 37°C

substrate: epinephrine


organism: Schizosaccharomyces pombe

substrate_name: esculetin

sequence_source: UniProt O42898 canonical FASTA direct accession lookup

proof_lines: pH 7.5, temperature not specified in the publication

substrate: esculetin


organism: Sus scrofa

substrate_name: (-)-norepinephrine

sequence_source: UniProt Q99028 canonical FASTA direct accession lookup

substrate: (-)-norepinephrine


organism: Aspergillus oryzae


organism: Lactobacillus delbrueckii subsp. lactis


organism: Mus musculus

substrate_name: alpha-L-Glu-beta-naphthylamide

sequence_source: UniProt P16406 canonical FASTA direct accession lookup

substrate: alpha-L-Glu-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from UniProt P16406 canonical FASTA; mutation positions match selected mutation signature directly and applied mutation signature H450F to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, mutant enzyme H450F enzyme, in presence of 4 mM Ca2+

proof_lines: pH 7.4, 37°C, mutant enzyme H450F, in presence of 0.025 mM Ca2+

proof_lines: pH 7.4, 37°C, mutant enzyme H450F, 0.025 mM Ca2+


substrate_name: angiotensin II

assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM Tris/HCl

proof_lines: pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q

proof_lines: pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A

substrate: angiotensin II


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProt P16406 canonical FASTA; mutation positions match selected mutation signature directly and applied mutation signature N363A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P16406 canonical FASTA; mutation positions match selected mutation signature directly and applied mutation signature N363Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P16406 canonical FASTA; mutation positions match selected mutation signature directly and applied mutation signature E215D to reconstruct the assayed variant sequence.


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


organism: Candida tropicalis

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

proof_lines:
cosubstrate esculetin
cosubstrate S-adenosyl-L-methionine


organism: Clarias gariepinus

substrate_name: dopamine


organism: Cricetinae

substrate_name: quercetin

substrate: quercetin


organism: Homo sapiens

assay_conditions_summary: pH 7.8; 310.15 K; buffer phosphate

proof_lines:
S-COMT, 0.1 mM S-adenosyl-L-methionine
pH 7.8
S-COMT, 0.25 mM S-adenosyl-L-methionine


proof_lines:
membrane-bound enzyme form
soluble enzyme form


organism: Neotoma albigula

substrate_name: catechol

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

substrate: catechol


organism: Neotoma stephensi


organism: Oryctolagus cuniculus

proof_lines:
soluble enzyme form
membrane-bound enzyme form


organism: Rattus norvegicus

substrate_name: adrenaline

proof_lines:
brain MB-COMT, native
brain MB-COMT, solubilized
S-COMT, recombinant fusion protein

substrate: adrenaline


organism: Solanum lycopersicum


organism: Streptomyces griseus

substrate_name: S-adenosyl-L-methionine


substrate_name: epigallocatechin gallate

substrate: epigallocatechin gallate


sequence_variant_note: Resolved canonical sequence from UniProt REST P16406 (2026-06-16) and applied mutation signature E215Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P16406 (2026-06-16) and applied mutation signature E215A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P16406 (2026-06-16) and applied mutation signature T348Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; buffer 50 mM Tris-HCl

proof_lines: recombinant mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+

proof_lines: recombinant mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+


sequence_variant_note: Resolved canonical sequence from UniProt REST P16406 (2026-06-16) and applied mutation signature T348S to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+

proof_lines: recombinant mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+


sequence_variant_note: Resolved canonical sequence from UniProt REST P16406 (2026-06-16) and applied mutation signature T348D to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+

proof_lines: recombinant mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+


substrate_name: alpha-L-glutamyl-beta-naphthylamide

sequence_variant_note: Resolved canonical sequence from UniProt REST P16406 (2026-06-16) and applied mutation signature R878K to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K, with 4 mM Ca2+

substrate: alpha-L-glutamyl-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from UniProt REST P16406 (2026-06-16) and applied mutation signature R878A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A, with 4 mM Ca2+


organism: Plasmodium falciparum

proof_lines:
in the absence of cobalt
in the presence of 1 mM cobalt


proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Acidilobus saccharovorans

substrate: Pyrazinamide


organism: Oceanobacillus iheyensis

substrate_name: methyl nicotinate

sequence_source: UniProt REST Q8ESQ6 (2026-06-16)

column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Wild-type, substrate row Methylnicotinate; column Specific activity (U/mg) = 0.45±0.02; column Km (mM) = 1.03; column k cat (s-1) = 0.32; column k cat/Km (mM-1 s-1) = 0.31. captured primary segment: Methylnicotinate | wild-type OiNIC | Km 1.03 mM | kcat 0.32 s^-1 | kcat/Km 0.31 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 1.03 mM; the printed column is already in millimolar, so no conversion is applied and the value is 1.03 mM. kcat: printed Table 1 k cat cell 0.32 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 0.32 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 0.31 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 0.31 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.32 / 1.03 = 0.3106796116504854 s^-1 mM^-1, against the printed efficiency cell 0.31 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Wild-type, substrate row Methylnicotinate: Km = 1.03 mM; k cat = 0.32 s^-1; k cat/Km = 0.31 mM^-1 s^-1; Specific activity = 0.45±0.02 U/mg.

substrate: methyl nicotinate


sequence_source: UniProt REST Q8ESQ6 (2026-06-16); 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: recombinant mutant F68W/C133A, pH 7.3, 37°C


substrate_name: ethyl nicotinate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ESQ6 and applied mutation signature Q96A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block Q96A, substrate row Ethylnicotinate; column Specific activity (U/mg) = 0.22±0.02; column Km (mM) = 1.43; column k cat (s-1) = 0.19; column k cat/Km (mM-1 s-1) = 0.13. captured primary segment: Ethylnicotinate | Q96A OiNIC | Km 1.43 mM | kcat 0.19 s^-1 | kcat/Km 0.13 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 1.43 mM; the printed column is already in millimolar, so no conversion is applied and the value is 1.43 mM. kcat: printed Table 1 k cat cell 0.19 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 0.19 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 0.13 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 0.13 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.19 / 1.43 = 0.13286713286713286 s^-1 mM^-1, against the printed efficiency cell 0.13 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Q96A, substrate row Ethylnicotinate: Km = 1.43 mM; k cat = 0.19 s^-1; k cat/Km = 0.13 mM^-1 s^-1; Specific activity = 0.22±0.02 U/mg.

substrate: ethyl nicotinate


substrate_name: nicotinamide

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8ESQ6 and applied mutation signature E65H to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type OiNIC and its mutants. (PLoS ONE 2013, 8(2): e56727); printed column heads Specific activity (U/mg) | Km (mM) | k cat (s-1) | k cat/Km (mM-1 s-1). Table 1, enzyme block E65H, substrate row NAM; column Specific activity (U/mg) = 13.50±0.1; column Km (mM) = 0.13; column k cat (s-1) = 5.63; column k cat/Km (mM-1 s-1) = 42.65. captured primary segment: NAM | E65H OiNIC | Km 0.13 mM | kcat 5.63 s^-1 | kcat/Km 42.65 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.13 mM; the printed column is already in millimolar, so no conversion is applied and the value is 0.13 mM. kcat: printed Table 1 k cat cell 5.63 s^-1; the printed turnover column is per second, so no conversion is applied and the value is 5.63 s^(-1). kcat/Km: printed Table 1 k cat/Km cell 42.65 mM^-1 s^-1; the printed efficiency column is already per millimolar per second, so no conversion is applied and the value is 42.65 s^(-1)*mM^(-1). Quotient disclosure for this row: 5.63 / 0.13 = 43.30769230769231 s^-1 mM^-1, against the printed efficiency cell 42.65 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block E65H, substrate row NAM: Km = 0.13 mM; k cat = 5.63 s^-1; k cat/Km = 42.65 mM^-1 s^-1; Specific activity = 13.50±0.1 U/mg.


organism: Escherichia coli

substrate_name: D-glyceraldehyde 3-phosphate

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

proof_lines: apparent value, mutant enzyme H299A, at pH 8.0 and 25-28°C

substrate: D-glyceraldehyde 3-phosphate


proof_lines: apparent value, mutant enzyme H49N, at pH 8.0 and 25-28°C


proof_lines: apparent value, wild type enzyme, at pH 8.0 and 25-28°C


proof_lines: apparent value, mutant enzyme H49A, at pH 8.0 and 25-28°C


proof_lines: apparent value, mutant enzyme H299N, at pH 8.0 and 25-28°C


organism: Mycobacterium tuberculosis

substrate_name: D-erythrose 4-phosphate

substrate: D-erythrose 4-phosphate


substrate_name: pyruvate

substrate: pyruvate


organism: Plasmodium vivax


organism: Populus tremula x Populus alba


organism: Populus trichocarpa


organism: Streptomyces sp.


organism: Zea mays

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

proof_lines: kcat is 2.1 sec(-1) for DIBOA-glucoside.


enzyme_display_name: geraniol 8-hydroxylase

organism: Catharanthus roseus

substrate_name: geraniol

proof_lines: kcat is 3.15 min(-1) for naringenin. kcat is 7.86 min(-1) for geraniol.

enzyme: geraniol 8-hydroxylase

substrate: geraniol


enzyme_display_name: 4-aminobenzoate N-oxygenase

organism: Streptomyces thioluteus

substrate_name: p-aminobenzoate

proof_lines: kcat is 6.21 min(-1) with p-aminobenzoate as substrate.

enzyme: 4-aminobenzoate N-oxygenase

substrate: p-aminobenzoate


organism: Escherichia coli (strain K12)

substrate_name: L-methionine (S)-S-oxide

proof_lines: kcat is 3.2 min(-1) for the reduction of Met-S-SO using benzyl viologen as an artificial electron donor.

substrate: L-methionine (S)-S-oxide


enzyme_display_name: mitomycin 6-O-methyltransferase

organism: Streptomyces lavendulae

proof_lines: kcat is 0.110 min(-1) for methyltransferase activity with S-adenosyl-L-methionine as substrate. kcat is 0.103 min(-1) for methyltransferase activity with 6-demethylmitomycin A as substrate.

enzyme: mitomycin 6-O-methyltransferase

substrate: S-adenosyl-L-methionine


organism: Homo sapiens

substrate_name: 2-hydroxy-17beta-estradiol (at 37 degrees Celsius)

proof_lines: kcats are 6.8 min(-1), 3.4 min(-1), 3.3 min(-1) and 6.7 min(-1) with 2-hydroxy-17beta-estradiol, 4-hydroxy-17beta-estradiol, 2-hydroxyestrone and 4-hydroxyestrone as substrates, respectively.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.080 min(-1) with 5OMeBA as substrate. kcat is 0.22 min(-1) with PCA as substrate. kcat is 0.43 min(-1) with CA as substrate.


organism: Salvia splendens

substrate_name: malonyl-CoA (with native enzyme)

proof_lines: kcat is 0.55 sec(-1) (with native enzyme). kcat is 0.76 sec(-1) (with recombinant enzyme).

substrate: malonyl-CoA (with native enzyme)


proof_lines: kcat is 0.4 min(-1) with trehalose-2-sulfate as substrate. kcat is 0.19 min(-1) with palmitoyl-CoA as substrate.


substrate_name: benzyloxycarbonyl-Gln-Gly (for protein-glutamine deamidase activity)

proof_lines: kcat is 11.2 min(-1) with benzyloxycarbonyl-Gln-Gly substrate for protein-glutamine deamidase activity.


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

substrate_name: L-rhamnose

proof_lines: kcat is 16 sec(-1) with L-rhamnose. kcat is 2.5 sec(-1) with beta-D-glucose 1-phosphate.

substrate: L-rhamnose


enzyme_display_name: sym-norspermidine synthase

organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: agmatine

proof_lines: kcat is 2.09 sec(-1) for aminopropyl transferase activity with cadaverine as amine acceptor. kcat is 0.18 sec(-1) for aminopropyl transferase activity with putrescine as amine acceptor. kcat is 0.1 sec(-1) for aminopropyl transferase activi

enzyme: sym-norspermidine synthase

substrate: agmatine


enzyme_display_name: fumigaclavine B O-acetyltransferase

organism: Aspergillus fumigatus

substrate_name: Fumigaclavine B

sequence_source: UniProtKB:Q4WZ64 direct lookup 2026-06-16

enzyme: fumigaclavine B O-acetyltransferase

substrate: Fumigaclavine B


substrate_name: Acetyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

substrate: Acetyl-CoA


enzyme_display_name: protein-serine/threonine phosphatase

organism: Escherichia coli

substrate_name: 4-Nitrophenyl phosphate; H2O

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

sequence_source: UniProtKB:P76395 direct lookup 2026-06-16

enzyme: protein-serine/threonine phosphatase

substrate: 4-Nitrophenyl phosphate; H2O


substrate_name: O-Phospho-tau-protein; H2O

sequence_source: UniProtKB:P53041 direct lookup 2026-06-16

substrate: O-Phospho-tau-protein; H2O


substrate_name: Casein kinase I epsilon phosphorylated; H2O


substrate: Casein kinase I epsilon phosphorylated; H2O


substrate_name: 4-Nitrophenyl phosphate

sequence_source: UniProtKB:O95476 direct lookup 2026-06-16

substrate: 4-Nitrophenyl phosphate


substrate_name: 4-nitrophenyl phosphate

sequence_source: UniProtKB:P62136 direct lookup 2026-06-16

substrate: 4-nitrophenyl phosphate


substrate_name: S6K1p; H2O

substrate: S6K1p; H2O


sequence_source: UniProtKB:O60346 direct lookup 2026-06-16


sequence_source: UniProtKB:Q6ZVD8 direct lookup 2026-06-16


substrate_name: RRApTVA

substrate: RRApTVA


substrate_name: SQLHIpTPGTAY

sequence_source: UniProtKB:Q96HS1 direct REST lookup 2026-06-16

proof_lines: at pH 7.5 and, temperature not specified in the publication

substrate: SQLHIpTPGTAY


proof_lines: recombinant mutant S39E, pH and temperature not specified in the publication


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


proof_lines: recombinant mutant S19A, pH and temperature not specified in the publication


proof_lines: recombinant mutant S19E, pH and temperature not specified in the publication


organism: Listeria monocytogenes

substrate_name: [Myelin basic protein]-serine/threonine phosphate; H2O

sequence_source: UniProtKB:Q8Y678 direct REST lookup 2026-06-16


organism: Mycoplasmopsis synoviae

sequence_source: UniProtKB:Q4A6S8 direct REST lookup 2026-06-16

proof_lines: pH 9.0, 30°C, recombinant wild-type enzyme


substrate_name: RRA(pT)VA

substrate: RRA(pT)VA


organism: Opisthokonta

substrate_name: cdc2k-P; H2O

substrate: cdc2k-P; H2O


organism: Rattus norvegicus

substrate_name: H2O; 4-Nitrophenyl phosphate

sequence_source: UniProtKB:P53042 direct REST lookup 2026-06-16

substrate: H2O; 4-Nitrophenyl phosphate


sequence_source: UniProtKB:P53042 direct REST lookup 2026-06-16; selected from source accession bundle after P10636 checked as tau substrate


organism: Saccharomyces cerevisiae

substrate_name: IERPKpSerFSTEK; H2O

sequence_source: UniProtKB:P38797 direct REST lookup 2026-06-16 plus selected SABIO-RK Nd38 N-terminal deletion note

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: phosphoprotein phosphatase(Enzyme) wildtype Nd38 (N-terminal truncated 1-38)

substrate: IERPKpSerFSTEK; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38797 direct REST lookup 2026-06-16 plus selected SABIO-RK D109A Nd38 note and applied mutation signature D109A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoprotein phosphatase(Enzyme) mutant D109A Nd38 (N-terminal truncated 1-38)


organism: Streptococcus pyogenes

sequence_source: UniProtKB:Q99YM9 direct REST lookup 2026-06-16


organism: Sulfolobus acidocaldarius

substrate_name: ETTYERW(pT)TITQRER

substrate: ETTYERW(pT)TITQRER


substrate_name: 4-nitrophenyl phosphate; RRA(pT)VA

sequence_source: UniProtKB Q4JAD1 REST FASTA checked 2026-06-16

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

substrate: 4-nitrophenyl phosphate; RRA(pT)VA


organism: Thermococcus kodakarensis

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed E132A and applied mutation signature E132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed E132Q and applied mutation signature E132Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed R124A and applied mutation signature R124A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed E132Q

proof_lines:
pH 5.0, 60°C, mutant E132Q
pH 5.0, 20°C, mutant E132Q


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed D63N and applied mutation signature D63N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed R124E and applied mutation signature R124E to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 60°C, mutant R124E
pH 5.0, 20°C, mutant R124E


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed G95A and applied mutation signature G95A to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 60°C, mutant G95A
pH 5.0, 20°C, mutant G95A


sequence_source: UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed R124E


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8X270 REST FASTA checked 2026-06-16; reconstructed E132L and applied mutation signature E132L to reconstruct the assayed variant sequence.