enzyme_display_name: Multicopper oxidase CueO

organism: Escherichia coli (strain K12)

substrate_name: enterobactin (at pH 5.0, in the presence of 1 mM Cu(2+))

assay_conditions_summary: pH 5

proof_lines: kcat is 914 min(-1) with Cu(+) as substrate (at pH 5.0, in the absence of added Cu(2+)) (PubMed:15516598). kcat is 651 min(-1) with Cu(+) as substrate (at pH 5.0, in the presence of 1 mM Cu(2+)) (PubMed:15516598). kcat is 57 min(-1) with Cu

enzyme: Multicopper oxidase CueO


substrate_name: ABTS (at pH 5.0, in the presence of 1 mM Cu(2+))

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

status: unverified

source: uniprot


substrate_name: 2,6-DMP (at pH 5.0, in the presence of 1 mM Cu(2+))


enzyme_display_name: ferroxidase

organism: Saccharomyces cerevisiae

substrate_name: Fe(II)

source_db: brenda

verification_status: corrected

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38993 and applied mutation signature E185A/D409A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6

column_label: Table 2 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII), Fet3p species row 'E185A/D409A'; column 'KM (µM)' = 3994±387; column 'kcat (min-1)' = 13.9±0.4; column 'single-turnover reduction by FeII (s-1), fast phase' = 0.41 ± 0.01; column 'single-turnover reduction by FeII (s-1), slow phase' = 0.02 ± 0.07; Table 2 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 13.9 min-1; min^-1 to s^-1 is a division by 60, so 13.9 / 60 = 0.23166666666666666 s^(-1); the export carries 0.232 s^(-1). Km: printed Table 2 cell 3994 µM in the 'KM (µM)' column; µM to mM is a division by 1000, so 3994 / 1000 = 3.994 mM; the export carries 3.994 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.058003672174929057 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.23166666666666666 / 3.994 of this row's own two printed cells, typed derived_same_measurement; the export carries 0.05808713069604406 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Fet3p species row 'E185A/D409A': KM = 3994 µM; kcat = 13.9 min-1; Table 2 prints no kcat/KM cell for this row.

table_label: Table 2: Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII (Biochemistry 2006, 45(42):12741-12749)

enzyme: ferroxidase

substrate: Fe(II)

status: corrected

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38993 and applied mutation signature E185A to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 2 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII), Fet3p species row 'E185A'; column 'KM (µM)' = 35.6±2.8; column 'kcat (min-1)' = 24.3±0.6; column 'single-turnover reduction by FeII (s-1), fast phase' = 2.47 ± 0.04; column 'single-turnover reduction by FeII (s-1), slow phase' = 0.36 ± 0.01; Table 2 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 24.3 min-1; min^-1 to s^-1 is a division by 60, so 24.3 / 60 = 0.405 s^(-1); the export carries 0.48 s^(-1). Km: printed Table 2 cell 35.6 µM in the 'KM (µM)' column; µM to mM is a division by 1000, so 35.6 / 1000 = 0.0356 mM; the export carries 0.0356 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 11.376404494382024 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.405 / 0.0356 of this row's own two printed cells, typed derived_same_measurement; the export carries 13.48314606741573 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Fet3p species row 'E185A': KM = 35.6 µM; kcat = 24.3 min-1; Table 2 prints no kcat/KM cell for this row.

row_label: Table 2, Fet3p species row 'E185A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38993 and applied mutation signature D409A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII), Fet3p species row 'D409A'; column 'KM (µM)' = 18.8±1.6; column 'kcat (min-1)' = 48.2±1.2; column 'single-turnover reduction by FeII (s-1), fast phase' = 62.03 ± 0.60; column 'single-turnover reduction by FeII (s-1), slow phase' = 1.31 ± 0.07; Table 2 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 48.2 min-1; min^-1 to s^-1 is a division by 60, so 48.2 / 60 = 0.8033333333333333 s^(-1); the export carries 6.08 s^(-1). Km: printed Table 2 cell 18.8 µM in the 'KM (µM)' column; µM to mM is a division by 1000, so 18.8 / 1000 = 0.0188 mM; the export carries 0.0188 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 42.730496453900706 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.8033333333333333 / 0.0188 of this row's own two printed cells, typed derived_same_measurement; the export carries 323.40425531914894 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Fet3p species row 'D409A': KM = 18.8 µM; kcat = 48.2 min-1; Table 2 prints no kcat/KM cell for this row.

row_label: Table 2, Fet3p species row 'D409A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P38993 and applied mutation signature D283A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with FeII), Fet3p species row 'D283A'; column 'KM (µM)' = 19.3±1.5; column 'kcat (min-1)' = 75.7±1.9; column 'single-turnover reduction by FeII (s-1), fast phase' = 681.9 ± 23.7; column 'single-turnover reduction by FeII (s-1), slow phase' = 2.46 ± 0.28; Table 2 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 75.7 min-1; min^-1 to s^-1 is a division by 60, so 75.7 / 60 = 1.2616666666666667 s^(-1); the export carries 1.26 s^(-1). Km: printed Table 2 cell 19.3 µM in the 'KM (µM)' column; µM to mM is a division by 1000, so 19.3 / 1000 = 0.0193 mM; the export carries 0.0193 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 65.37132987910189 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.2616666666666667 / 0.0193 of this row's own two printed cells, typed derived_same_measurement; the export carries 65.28497409326424 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Fet3p species row 'D283A': KM = 19.3 µM; kcat = 75.7 min-1; Table 2 prints no kcat/KM cell for this row.

row_label: Table 2, Fet3p species row 'D283A'


substrate_name: hydroquinone

column_label: Table 3 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with HQ), Fet3p species row 'E185A/D409A'; column 'KM (mM)' = 30.5±2.1; column 'kcat (min-1)' = 132.8±3.9; column 'single-turnover reduction by HQ (s-1), fast phase' = 2.127 ± 0.085; column 'single-turnover reduction by HQ (s-1), slow phase' = 0.256 ± 0.020; Table 3 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 132.8 min-1; min^-1 to s^-1 is a division by 60, so 132.8 / 60 = 2.2133333333333334 s^(-1); the export carries 2.3 s^(-1). Km: printed Table 3 cell 30.5 mM in the 'KM (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 30.5 mM; the export carries 0.03 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.07256830601092897 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.2133333333333334 / 30.5 of this row's own two printed cells, typed derived_same_measurement; the export carries 76.66666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Fet3p species row 'E185A/D409A': KM = 30.5 mM; kcat = 132.8 min-1; Table 3 prints no kcat/KM cell for this row.

table_label: Table 3: Steady-State Kinetic Constants and Single-Turnover Reduction Rates with HQ (Biochemistry 2006, 45(42):12741-12749)

substrate: hydroquinone


column_label: Table 3 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with HQ), Fet3p species row 'D409A'; column 'KM (mM)' = 30.3±2.4; column 'kcat (min-1)' = 139.7±4.7; column 'single-turnover reduction by HQ (s-1), fast phase' = 1.124 ± 0.103; column 'single-turnover reduction by HQ (s-1), slow phase' = 0.105 ± 0.003; Table 3 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 139.7 min-1; min^-1 to s^-1 is a division by 60, so 139.7 / 60 = 2.328333333333333 s^(-1); the export carries 2.33 s^(-1). Km: printed Table 3 cell 30.3 mM in the 'KM (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 30.3 mM; the export carries 0.03 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.07684268426842683 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.328333333333333 / 30.3 of this row's own two printed cells, typed derived_same_measurement; the export carries 77.66666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Fet3p species row 'D409A': KM = 30.3 mM; kcat = 139.7 min-1; Table 3 prints no kcat/KM cell for this row.

row_label: Table 3, Fet3p species row 'D409A'


column_label: Table 3 (Steady-State Kinetic Constants and Single-Turnover Reduction Rates with HQ), Fet3p species row 'D283A'; column 'KM (mM)' = 19.3±1.1; column 'kcat (min-1)' = 169.5±3.5; column 'single-turnover reduction by HQ (s-1), fast phase' = 0.072 ± 0.018; column 'single-turnover reduction by HQ (s-1), slow phase' = 0.001 ± 0.101; Table 3 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 169.5 min-1; min^-1 to s^-1 is a division by 60, so 169.5 / 60 = 2.825 s^(-1); the export carries 2.81 s^(-1). Km: printed Table 3 cell 19.3 mM in the 'KM (mM)' column; the cell is already in mM, so no unit conversion applies and the paper value is 19.3 mM; the export carries 0.019 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.14637305699481865 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.825 / 19.3 of this row's own two printed cells, typed derived_same_measurement; the export carries 147.89473684210526 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Fet3p species row 'D283A': KM = 19.3 mM; kcat = 169.5 min-1; Table 3 prints no kcat/KM cell for this row.

row_label: Table 3, Fet3p species row 'D283A'


substrate_name: Cu(+) (at pH 5.0, in the absence of added Cu(2+))


substrate_name: Fe(2+) (at pH 5.0, in the presence of 1 mM Cu(2+))


enzyme_display_name: Ceruloplasmin

organism: Homo sapiens

verification_status: verified

column_label: Table 1; hCp row; Cu1+ KM (uM) column = 36.8 +/- 5.1.

raw_value_unit_evidence: Table 1 hCp row reports Cu1+ KM = 36.8 +/- 5.1 uM.

row_label: hCp row; Cu1+ KM column

table_label: PMID 14623105, Table 1: Kinetic constants for the cuprous oxidase and ferroxidase reactions of Fet3p and hCp

enzyme: Ceruloplasmin

status: verified


column_label: Table 1; hCp row; Fe2+ KM (uM) column = 8.3 +/- 1.5.

raw_value_unit_evidence: Table 1 hCp row reports Fe2+ KM = 8.3 +/- 1.5 uM.

row_label: hCp row; Fe2+ KM column


proof_lines: kcat is 22.5 min(-1) and 30.3 min(-1) with Cu(+) and Fe(2+) as substrates, respectively.


substrate_name: p-phenylenediamine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E185A/Y354A to reconstruct the assayed variant sequence.

substrate: p-phenylenediamine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E185A with inferred residue-numbering offset -31 to reconstruct the assayed variant sequence.

proof_lines:
mutant E185A, pH 6.0
mutant E185A
mutant E185A, pH 6.5, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D278A with inferred residue-numbering offset -31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E185D with inferred residue-numbering offset -31 to reconstruct the assayed variant sequence.

proof_lines:
mutant E185D, pH 6.0
mutant E185D, pH 6.5, 4°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y354A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines:
mutant Y354A, pH 6.0
mutant Y354A, pH 6.5, 4°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y354F with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines:
mutant Y354F, pH 6.0
mutant Y354F, pH 6.5, 4°C


proof_lines:
mutant E185D, pH 6.0
mutant E185D, pH 6.5, 25°C


proof_lines:
mutant Y354F, pH 6.0
mutant Y354F, pH 6.5, 25°C


proof_lines:
mutant Y354A, pH 6.0
mutant Y354A, pH 6.5, 25°C


enzyme_display_name: Hephaestin

proof_lines: kcat is 18 min(-1) for the oxidation of Fe(2+) (at pH 5.0).

enzyme: Hephaestin


enzyme_display_name: manganese oxidase

organism: Bacillus pumilus

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

assay_conditions_summary: pH 8

enzyme: manganese oxidase


enzyme_display_name: Iron transport multicopper oxidase FET3

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

column_label: Table 1; Fet3p row; Cu1+ KM (uM) column = 37.9 +/- 3.6.

raw_value_unit_evidence: Table 1 Fet3p row reports Cu1+ KM = 37.9 +/- 3.6 uM.

row_label: Fet3p row; Cu1+ KM column

enzyme: Iron transport multicopper oxidase FET3


column_label: Table 1; Fet3p row; Fe2+ KM (uM) column = 5.4 +/- 0.8.

raw_value_unit_evidence: Table 1 Fet3p row reports Fe2+ KM = 5.4 +/- 0.8 uM.

row_label: Fet3p row; Fe2+ KM column


organism: Aquifex aeolicus

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


organism: Campylobacter jejuni


organism: Escherichia coli


organism: Rana catesbeiana

km_display: Not reported


enzyme_display_name: cuproxidase

organism: Desulfovibrio sp. A2

enzyme: cuproxidase


proof_lines: kcat is 79.2 min(-1) and 63.9 min(-1) with Cu(+) and Fe(2+) as substrates, respectively.


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

sequence_source: multiple


substrate_name: 2,3-DHB (at pH 5.0, in the presence of 1 mM Cu(2+))


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: mercury(II) reductase

organism: Lysinibacillus sphaericus

source_db: oed

enzyme: mercury(II) reductase

source: oed


enzyme_display_name: Mercuric reductase

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: Mercuric reductase

substrate: NADPH


organism: Rhodobacter capsulatus


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


organism: Salmonella typhimurium


substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

substrate: glutathione


substrate_name: tert-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: tert-butyl hydroperoxide


substrate_name: ferric enterobactin (at pH 6.5, in the presence of 0.5 mM Cu(2+))


assay_conditions_summary: pH 6; 298.15 K; buffer pH 6

column_label: PDF page 5, Results kinetic-analysis prose immediately before Figure 6: Fe(II) oxidation fit gives Km [Fe(II)] 4.8 +/- 0.3 uM and kcat [Fe(II) turnover] 9.5 min^-1; Figure 6 caption states Fe(II) oxidation was followed by Fe(III) appearance at 315 nm.

raw_value_unit_evidence: PDF page 5 Results text reports Km [Fe(II)] = 4.8 +/- 0.3 uM and kcat [Fe(II) turnover] = 9.5 min^-1.

row_label: Fet3p Fe(II) oxidation limiting-substrate fit

table_label: Results kinetic-analysis prose and Figure 6 caption


smiles: O=O

column_label: PDF page 5, Results kinetic-analysis prose immediately before Figure 6: O2 fit gives Km (O2) 1.3 +/- 0.2 uM and kcat [O2 turnover] 2.3 min^-1; Figure 6 caption states O2 consumption was determined by O2 electrode.

raw_value_unit_evidence: PDF page 5 Results text reports Km (O2) = 1.3 +/- 0.2 uM and kcat [O2 turnover] = 2.3 min^-1.

row_label: Fet3p O2 consumption limiting-substrate fit


substrate_name: Cu+

column_label: Table 1; Fet3p row; Cu1+ KM (uM) column = 37.9 +/- 3.6; Cu1+ kcat (min^-1) column = 79.2 +/- 2.7; no separate kcat/KM column is printed.

raw_value_unit_evidence: Table 1 Fet3p row reports Cu1+ KM = 37.9 +/- 3.6 uM and Cu1+ kcat = 79.2 +/- 2.7 min^-1.

row_label: Fet3p row; Cu1+ KM and Cu1+ kcat columns

source_databases_merged: brenda uniprot

substrate: Cu+


enzyme_display_name: DNA-binding protein HupB

organism: Mycobacterium leprae (strain TN)

column_label: Primary article prose/abstract segment; M. leprae ML-LBP/MDP1 ferroxidase activity; Km metric value.

raw_value_unit_evidence: Abstract paragraph reports MDP1 Km values: M. leprae 0.129 mM.

table_label: Abstract/results prose: MDP1 ferroxidase Km values

enzyme: DNA-binding protein HupB


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

column_label: Primary article prose/abstract segment; M. tuberculosis MDP1 ferroxidase activity; Km metric value.

raw_value_unit_evidence: Abstract paragraph reports MDP1 Km values: M. tuberculosis 0.252 mM.


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

column_label: Primary article prose/abstract segment; M. smegmatis MDP1 ferroxidase activity; Km metric value.

raw_value_unit_evidence: Results text for M. smegmatis MDP1-deficient strain section reports Km value 0.136 mM.

row_label: M. smegmatis MDP1 ferroxidase activity


organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)

column_label: Primary article prose/abstract segment; M. bovis BCG MDP1 ferroxidase activity; Km metric value.

raw_value_unit_evidence: Abstract paragraph reports MDP1 Km values: M. bovis BCG 0.292 mM.

row_label: M. bovis BCG MDP1 ferroxidase activity


assay_conditions_summary: pH 5; 313.15 K; buffer 100 mM Mes

column_label: Public ITQB PDF text, Table 1, wild-type Fe(II) row, + Cu(II) columns: Km 7 uM, kcat 38 min^-1, kcat/Km 5.4 min^-1 uM^-1. Local text refs: itqb_public_pdf_pmid_17451433_text.txt lines 467-486.

normalized_value_unit_evidence: Km 7 uM normalizes to 0.007 mM and kcat 38 min^-1 normalizes to 0.633 s^-1, matching the export values. The paper's explicit kcat/Km cell 5.4 min^-1 uM^-1 normalizes to 90.0 s^-1*mM^-1, while the export carries 90.42857142857143 s^-1*mM^-1.

raw_value_unit_evidence: Table 1 wild-type Fe(II) row reports + Cu(II) Km 7 +/- 2 uM, kcat 38 +/- 0.6 min^-1, and kcat/Km 5.4 min^-1 uM^-1.

row_label: Wild type / Fe(II)

table_label: Table 1. Kinetic parameters for oxidation of the metal ions Cu(I), Fe(II) and laccase substrates


substrate_name: prochlorperazine

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

substrate: prochlorperazine


substrate_name: perphenazine

substrate: perphenazine


substrate_name: promazine

substrate: promazine


substrate_name: alimemazine

substrate: alimemazine


substrate_name: thioridazine

substrate: thioridazine


substrate_name: p-Aminophenol

substrate: p-Aminophenol


substrate_name: periciazine

substrate: periciazine


substrate_name: diethazine

substrate: diethazine


substrate_name: Promethazine

substrate: Promethazine


substrate_name: L-epinephrine

substrate: L-epinephrine


substrate_name: 2-sulfonic acid-p-phenylenediamine

substrate: 2-sulfonic acid-p-phenylenediamine


substrate_name: Trifluoperazine

substrate: Trifluoperazine


substrate_name: L-norepinephrine

substrate: L-norepinephrine


substrate_name: o-aminophenol

substrate: o-aminophenol


substrate_name: o-phenylenediamine

substrate: o-phenylenediamine


substrate_name: N,N-dimethyl-m-phenylenediamine

substrate: N,N-dimethyl-m-phenylenediamine


substrate_name: chlorpromazine

substrate: chlorpromazine


substrate_name: fluphenazine

substrate: fluphenazine


substrate_name: ascorbate

substrate: ascorbate


substrate_name: p-anisidine

substrate: p-anisidine


substrate_name: 5-hydroxyindol-3-ylacetic acid

substrate: 5-hydroxyindol-3-ylacetic acid


substrate_name: triflupromazine

substrate: triflupromazine


substrate_name: N-acetyl-p-phenylenediamine

substrate: N-acetyl-p-phenylenediamine


substrate_name: m-phenylenediamine

substrate: m-phenylenediamine


substrate_name: N-phenyl-p-phenylenediamine

substrate: N-phenyl-p-phenylenediamine


substrate_name: pyrogallol

substrate: pyrogallol


substrate_name: quinone

substrate: quinone


substrate_name: durenediamine

substrate: durenediamine


substrate_name: N,N-Dimethyl-p-phenylenediamine

substrate: N,N-Dimethyl-p-phenylenediamine


substrate_name: catechol

substrate: catechol


substrate_name: N,N-diethyl-p-phenylenediamine

substrate: N,N-diethyl-p-phenylenediamine


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


enzyme_display_name: UniProt P22985

organism: Rattus norvegicus

substrate_name: NAD+

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P22985

substrate: NAD+

source: skid


proof_lines: mutant enzyme C558A, anaerobic conditions


proof_lines: mutant enzyme C559A, anaerobic conditions


proof_lines:
wild-type enzyme, aerobic conditions
wild-type enzyme, anaerobic conditions


organism: Candida albicans

proof_lines: recombinant E184A/D408A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication


proof_lines: recombinant E184A mutant CaFet34, pH not specified in the publication, temperature not specified in the publication


proof_lines: recombinant wild-type CaFet34, pH not specified in the publication, temperature not specified in the publication


organism: Rhodococcus erythropolis

substrate_name: Cu+

proof_lines: pH 5.5, 30°C, mutant containing a deleted methionine-rich C-terminal tail

substrate: Cu+


organism: Saccharomyces cerevisiae

substrate_name: p-phenylenediamine

substrate: p-phenylenediamine


substrate_name: o-phenylenediamine

substrate: o-phenylenediamine


substrate_name: L-epinephrine

substrate: L-epinephrine


organism: uncultured Pseudomonadota bacterium

proof_lines: isoform ATII-LCL-NH mutant D415A/D416A, at 25°C, pH not specified in the publication


proof_lines: isoform ATII-LCL-NH, at 25°C, pH not specified in the publication


proof_lines: isoform ATII-LCL-NH mutant D414A/D415A/D416A/D417A, at 25°C, pH not specified in the publication


organism: Acidithiobacillus ferrooxidans

smiles: Cl[Hg]Cl


substrate_name: Hg

smiles: [Hg]

substrate: Hg


enzyme_display_name: UniProt P04036

enzyme: UniProt P04036


enzyme_display_name: UniProt Q3M723

organism: Trichormus variabilis

substrate_name: NADH

enzyme: UniProt Q3M723

substrate: NADH


enzyme_display_name: UniProt Q9K1F1

organism: Neisseria meningitidis

enzyme: UniProt Q9K1F1


enzyme_display_name: UniProt Q5HG24

organism: Staphylococcus aureus

substrate_name: NADPH

enzyme: UniProt Q5HG24

substrate: NADPH


enzyme_display_name: UniProt A0A0A1EQY0

organism: [Candida] boidinii

substrate_name: formate

enzyme: UniProt A0A0A1EQY0

substrate: formate


enzyme_display_name: UniProt P33160

organism: Pseudomonas sp. 101

enzyme: UniProt P33160


substrate_name: NADP+

substrate: NADP+


enzyme_display_name: formate dehydrogenase

organism: Thermothelomyces thermophilus

smiles: O=C=O

enzyme: formate dehydrogenase


organism: Thermochaetoides thermophila

smiles: O=CO


enzyme_display_name: UniProt G8NVB5

organism: Granulicella mallensis

enzyme: UniProt G8NVB5


enzyme_display_name: formate dehydrogenase (NADP(+))

organism: Burkholderia stabilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q223E with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

enzyme: formate dehydrogenase (NADP(+))


enzyme_display_name: ferroxidase

organism: Anser sp.

enzyme: ferroxidase


substrate_name: o-Dianisidine

substrate: o-Dianisidine


enzyme_display_name: superoxide dismutase

organism: Bos taurus

enzyme: superoxide dismutase


organism: Escherichia coli

proof_lines: pH 7, presence of Cu(II), temperature not specified in the publication

proof_lines: pH 5, presence of Cu(II), temperature not specified in the publication

proof_lines: pH 5, temperature not specified in the publication


organism: Arabidopsis thaliana

substrate_name: Fe(II)

proof_lines: wild type enzyme, at pH 5.8, temperature not specified in the publication

substrate: Fe(II)


proof_lines: mutant enzyme D370A, at pH 5.8, temperature not specified in the publication


proof_lines: pH 5.0, 23°C, mutant enzyme M358S/M361S/M362S/M364S/M366S


proof_lines: xanthine oxidoreductase with ferroxidase activity


organism: Gallus sp.


organism: Homo sapiens

proof_lines: pH 5.0, temperature not specified in the publication


substrate_name: hypoxia-inducible factor-L-proline

proof_lines: N-terminal oxygen degradation domain DALTLLAP402AAGDTIISLDYG mutant F413Y in absence of NaCl, pH 7.0, 37°C

proof_lines: N-terminal oxygen degradation domain DALTLLAP402AAGDTIISLDYG mutant F413Y in presence of 100 mM NaCl, pH 7.0, 37°C

substrate: hypoxia-inducible factor-L-proline


proof_lines: C-terminal oxygen degradation domain DLDLEALAP564YIPADDDFQL mutant M561A/M568A in absence of NaCl, pH 7.0, 37°C

proof_lines: C-terminal oxygen degradation domain DLDLEALAP564YIPADDDFQL mutant M561A/M568A in presence of 100 mM NaCl, pH 7.0, 37°C


enzyme_display_name: UniProt O54050

organism: Rhodobacter capsulatus

substrate_name: xanthine

enzyme: UniProt O54050

substrate: xanthine


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonate

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonate


enzyme_display_name: arachidonate 15-lipoxygenase

enzyme: arachidonate 15-lipoxygenase


enzyme_display_name: DNA oxidative demethylase

substrate_name: 3-methylcytosine in 3'-tailed DNA

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

enzyme: DNA oxidative demethylase

substrate: 3-methylcytosine in 3'-tailed DNA


proof_lines: in the presence of RAD51C, at pH 8.0 and 37°C


organism: Klebsiella pneumoniae


proof_lines:
wild-type, pH 8,23°C
wild-type enzyme


proof_lines: pH 7.5, 25°C, mutant Y34F with fluorinated Tyr-residues


proof_lines: pH 7.5, 25°C, wild-type with fluorinated Tyr-residues


enzyme_display_name: cuproxidase

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

enzyme: cuproxidase


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


organism: Kitasatospora aureofaciens

substrate_name: CTP

proof_lines:
immobilized enzyme
presence of effector dATP

substrate: CTP


substrate_name: UTP

substrate: UTP


substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines:
immobilized enzyme
in presence of effector dGTP

substrate: ATP


substrate_name: ADP

assay_conditions_summary: cofactor ADP

substrate: ADP


substrate_name: GTP

substrate: GTP


substrate_name: CDP

substrate: CDP


enzyme_display_name: xanthine oxidase

organism: Arthrobacter sp.

enzyme: xanthine oxidase


enzyme_display_name: ribonucleoside-diphosphate reductase

organism: Tequatrovirus T4

substrate_name: GDP

proof_lines: in the presence of 0.4 mM dTTP as effector

enzyme: ribonucleoside-diphosphate reductase

substrate: GDP


proof_lines: in the presence of 0.002 mM dATP as effector

proof_lines: in the presence of 0.5 mM ATP as effector

proof_lines: in the presence of 0.02 mM dTTP as effector


proof_lines: in the presence of 0.007 mM dGTP as effector


substrate_name: UDP

proof_lines: in the presence of 0.3 mM ATP as effector

substrate: UDP


substrate_name: Unknown

ki_unit: mM

proof_lines:
in the presence of 0.15 mM dGTP
with 0.001 mM dATP as positive effector
in the presence of 0.55 mM dTTP

substrate: Unknown


organism: Blastobotrys adeninivorans

substrate_name: hypoxanthine

substrate: hypoxanthine


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 316.15 K; cofactor NAD+

substrate: NAD+


substrate_name: purine

substrate: purine


organism: Locusta sp.


organism: Thermus sp.

proof_lines:
at 37°C
at 70°C


assay_conditions_summary: 343.15 K; cofactor ATP


proof_lines: pH 8.5, 25°C, recombinant wild-type enzyme


enzyme_display_name: pteridine oxidase

organism: Ricinus communis

enzyme: pteridine oxidase


organism: Acinetobacter calcoaceticus


organism: Oshimavirus P7426

proof_lines: pH and temperature not specified in the publication, mutant G68S/R69P


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


substrate_name: Reduced glutaredoxin; CDP

substrate: Reduced glutaredoxin; CDP


substrate_name: CDP; Reduced glutaredoxin

substrate: CDP; Reduced glutaredoxin


enzyme_display_name: ribonucleoside-triphosphate reductase

organism: Lactococcus lactis subsp. cremoris

substrate_name: CTP; Reduced thioredoxin

enzyme: ribonucleoside-triphosphate reductase

substrate: CTP; Reduced thioredoxin


organism: Cellulosimicrobium cellulans

substrate_name: xanthine

substrate: xanthine


enzyme_display_name: 6-hydroxynicotinate dehydrogenase

organism: Neobacillus niacini

enzyme: 6-hydroxynicotinate dehydrogenase


organism: Drosophila melanogaster


organism: Anabaena sp.

substrate_name: CTP; 1,4-Dithiothreitol

substrate: CTP; 1,4-Dithiothreitol


organism: Sinomonas cyclohexanicum

proof_lines: at pH 7.2, temperature not specified in the publication


organism: Lens culinaris

substrate_name: H2O; Xanthine; O2

substrate: H2O; Xanthine; O2


enzyme_display_name: juglone 3-hydroxylase

organism: Pseudomonas putida

proof_lines:
enzyme 1
enzyme 2

enzyme: juglone 3-hydroxylase


organism: Euglena gracilis

substrate_name: Reduced thioredoxin; CTP

substrate: Reduced thioredoxin; CTP


organism: Lactobacillus leichmannii

substrate_name: ATP; Reduced thioredoxin

substrate: ATP; Reduced thioredoxin


substrate_name: CTP

proof_lines:
in presence of dATP
in presence of dTTP

substrate: CTP


substrate_name: ATP

substrate: ATP


organism: Rhodobacter capsulatus

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


enzyme_display_name: Vitamin B12-dependent ribonucleoside-diphosphate reductase

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

substrate_name: CDP (at 80 degrees Celsius)

substrate: CDP (at 80 degrees Celsius)


organism: Cellulosimicrobium funkei


enzyme_display_name: UniProt P80457

organism: Bos taurus

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

source_databases_merged: skid uniprot

enzyme: UniProt P80457


enzyme_display_name: Xanthine dehydrogenase/oxidase

substrate_name: NAD

assay_conditions_summary: cofactor NAD+

enzyme: Xanthine dehydrogenase/oxidase

substrate: NAD


enzyme_display_name: Ribonucleoside-diphosphate reductase small chain 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: Ribonucleoside-diphosphate reductase small chain 2


enzyme_display_name: Ribonucleoside-diphosphate reductase large chain 1


substrate_name: Oxidized thioredoxin

substrate: Oxidized thioredoxin


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: ADP (at 55 degrees Celsius)

assay_conditions_summary: 328.15 K; cofactor ADP

enzyme: Vitamin B12-dependent ribonucleoside-diphosphate reductase

substrate: ADP (at 55 degrees Celsius)


enzyme_display_name: phenylacetyl-CoA dehydrogenase

organism: Thauera aromatica

substrate_name: phenylacetyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: pH 7.5, 30°C, duroquinone as electron acceptor

proof_lines: pH 7.5, 30°C, 2,6-dichlorophenolindophenol as electron acceptor

enzyme: phenylacetyl-CoA dehydrogenase

substrate: phenylacetyl-CoA


substrate_name: pyridine 3-aldehyde

substrate: pyridine 3-aldehyde


substrate_name: succinate semialdehyde

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

substrate: succinate semialdehyde


substrate_name: glyceraldehyde 3-phosphate

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

substrate: glyceraldehyde 3-phosphate


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


enzyme_display_name: Caffeine dehydrogenase subunit alpha

organism: Pseudomonas sp. (strain CBB1)

substrate_name: caffeine (at 35 degrees Celsius and pH 7)

proof_lines: kcat is 10 min(-1) with caffeine as substrate.

enzyme: Caffeine dehydrogenase subunit alpha


enzyme_display_name: Caffeine dehydrogenase subunit gamma

enzyme: Caffeine dehydrogenase subunit gamma

substrate: caffeine (at 35 degrees Celsius and pH 7)


enzyme_display_name: Caffeine dehydrogenase subunit beta

enzyme: Caffeine dehydrogenase subunit beta


substrate_name: NADPH

proof_lines:
cosubstrate cytochrome c
cosubstrate indophenol
cofactor 2,6-dichlorophenolindophenol

substrate: NADPH


substrate_name: hypoxanthine

substrate: hypoxanthine


substrate_name: xanthine

assay_conditions_summary: pH 8.2; 296.65 K; cofactor NADH

proof_lines:
(+ O2)
cofactor 2,6-dichlorophenolindophenol
pH 8.2, 23.5°C

substrate: xanthine


substrate_name: aldehyde

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

substrate: aldehyde


enzyme_display_name: ethylbenzene hydroxylase

organism: Azoarcus sp.

enzyme: ethylbenzene hydroxylase


substrate_name: ferricenium

substrate: ferricenium


organism: Struthio camelus

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: xanthine oxidase

assay_conditions_summary: pH 7


substrate_name: nitrite

substrate: nitrite


organism: Homo sapiens


organism: Mus musculus

substrate_name: all-trans-Retinal

substrate: all-trans-Retinal


organism: Pyrococcus furiosus

substrate_name: CDP

substrate: CDP


enzyme_display_name: ribonucleoside-diphosphate reductase

organism: Escherichia coli


substrate_name: dCDP

substrate: dCDP


organism: Rattus norvegicus

proof_lines: recombinant wild-type enzyme in recombinant Pichia pastoris membranes, pH 7.4, 37°C


proof_lines: native enzyme in membranes, pH 7.4, 37°C


proof_lines: pH 7.4, 37°C, recombinant mutant Y139F enzyme

proof_lines: pH 7.4, 37°C, liver microsomes from rats homozygous for Y139F


proof_lines: pH 7.4, 37°C, recombinant enzyme mutants Y139F, and L128Q


proof_lines: pH 7.4, 37°C, recombinant mutant Y139S enzyme


proof_lines: pH 7.4, 37°C, recombinant mutant L128Q enzyme


proof_lines: pH 7.4, 37°C, recombinant mutant Y139C enzyme


proof_lines: pH 7.4, 37°C, recombinant mutant L120Q enzyme


proof_lines: above, pH 7.4, 37°C, recombinant enzyme mutants Y139F, L120Q, Y139C, Y139F, and Y139S


substrate_name: dTTP

substrate: dTTP


substrate_name: ATP

substrate: ATP


substrate_name: UDP

substrate: UDP


substrate_name: GDP

substrate: GDP


proof_lines:
wild-typpe enzyme, pH 7.4, 37°C
wild-type, pH 8.6, 30°C


proof_lines:
substrate and inhibitor compound
25°C, pH 7.4, oxidized form of enzyme
25°C, pH 7.4, reduced form of enzyme


enzyme_display_name: UniProt P28861

substrate_name: Fe(III)-EDTA

enzyme: UniProt P28861

substrate: Fe(III)-EDTA


enzyme_display_name: UniProt Q8EY89

organism: Leptospira interrogans

enzyme: UniProt Q8EY89


enzyme_display_name: UniProt C6KT68

organism: Plasmodium falciparum

enzyme: UniProt C6KT68


organism: Mesocricetus auratus

proof_lines:
vs. GDP
vs. ADP
vs. UDP


proof_lines:
vs. ADP
vs. CDP
vs. UDP


substrate_name: ADP

proof_lines:
vs. GDP
vs. CDP
vs. UDP

substrate: ADP


proof_lines:
vs. GDP
vs. CDP
vs. ADP


enzyme: xanthine oxidase


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


assay_conditions_summary: pH 8.5; cofactor NADH

proof_lines:
with xanthine as cosubstrate
cosubstrate xanthine, pH 8.5
cosubstrate xanthine, pH 10.0


proof_lines:
pterin as cosubstrate
hypoxanthine as cosubstrate
with xanthine as cosubstrate


substrate_name: methylene blue

substrate: methylene blue


substrate_name: thionine

substrate: thionine


organism: Cricetulus griseus

proof_lines:
in the presence of 1.5 mM ATP
in the presence of 3.6 mM dCTP

enzyme: ribonucleoside-diphosphate reductase


proof_lines:
optimum dGTP concentration
in the presence of 0.2 mM GTP


substrate_name: glyceryl trinitrate

substrate: glyceryl trinitrate


substrate_name: isosorbide dinitrate

substrate: isosorbide dinitrate


substrate_name: xanthine

proof_lines: pH not specified in the publication, temperature not specified in the publication, mutant E802Q

substrate: xanthine


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


enzyme_display_name: UniProt O69054

organism: Pseudomonas stutzeri

substrate_name: phosphonate

enzyme: UniProt O69054

substrate: phosphonate


enzyme_display_name: UniProt G4XDR8

organism: Ralstonia sp.

substrate_name: NAD+

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.2
Raw SKiD Env: Temp=40°C, pH=7.2

enzyme: UniProt G4XDR8

substrate: NAD+


proof_lines:
Raw SKiD Env: Temp=40°C, pH=7.2
Raw SKiD Env: Temp=30°C, pH=7.2


substrate_name: phosphite

substrate: phosphite


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.3


enzyme_display_name: phosphite dehydrogenase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E175A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

smiles: O=[PH](O)O

enzyme: phosphite dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M53A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M53N to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt Q6VAL8

organism: Pseudorhizobium banfieldiae

substrate_name: arsenite

enzyme: UniProt Q6VAL8

substrate: arsenite


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: dATP

substrate: dATP


substrate_name: glutaredoxin 1

substrate: glutaredoxin 1


substrate_name: CDP

substrate: CDP


enzyme_display_name: gibberellin 2beta-dioxygenase

organism: Lathyrus oleraceus

substrate_name: gibberellin 1

enzyme: gibberellin 2beta-dioxygenase

substrate: gibberellin 1


substrate_name: gibberellin 9

substrate: gibberellin 9


organism: Klebsiella pneumoniae

substrate_name: 3,4-dihydroxybenzoic acid

substrate: 3,4-dihydroxybenzoic acid


enzyme_display_name: mercury(II) reductase

enzyme: mercury(II) reductase


organism: Herpes simplex virus


substrate_name: ADP

substrate: ADP


enzyme_display_name: coenzyme F420 hydrogenase

organism: Methanococcus voltae

substrate_name: coenzyme F420

enzyme: coenzyme F420 hydrogenase

substrate: coenzyme F420


substrate_name: methyl viologen

substrate: methyl viologen


organism: Methanothermobacter wolfeii

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: nitric-oxide synthase (NADPH)

organism: Mus musculus

substrate_name: NADPH

enzyme: nitric-oxide synthase (NADPH)

substrate: NADPH


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


enzyme_display_name: 3-ketosteroid 9alpha-monooxygenase

organism: Mycobacterium tuberculosis

proof_lines: in 0.1 M potassium phosphate, pH 7.0, at 25°C

proof_lines: in 0.1 M potassium phosphate, pH 7.0, at 22°C

enzyme: 3-ketosteroid 9alpha-monooxygenase


enzyme_display_name: chlorite O2-lyase

organism: Nitrospira defluvii

substrate_name: Chlorite

smiles: [O-]Cl=O

enzyme: chlorite O2-lyase

substrate: Chlorite


organism: Oryctolagus cuniculus

proof_lines: in the presence of 5'-adenylimidodiphosphate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: nitric-oxide synthase (flavodoxin)

organism: Nocardia sp.

enzyme: nitric-oxide synthase (flavodoxin)


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Populus trichocarpa

substrate_name: trans-cinnamate

proof_lines: isoforms C4H1/C4H2/p-coumaroyl ester 3-hydroxylase C3H3 complex, pH 7.0, 20°C

proof_lines: isoform C4H1/p-coumaroyl ester 3-hydroxylase C3H3 complex, pH 7.0, 20°C

proof_lines: isoform C4H2/p-coumaroyl ester 3-hydroxylase C3H3 complex, pH 7.0, 20°C

enzyme: trans-cinnamate 4-monooxygenase

substrate: trans-cinnamate


proof_lines: isoforms C4H1/C4H2 complex, pH 7.0, 20°C


enzyme_display_name: catechol 1,2-dioxygenase

organism: Pseudomonas putida

enzyme: catechol 1,2-dioxygenase


enzyme_display_name: 6-hydroxynicotinate 3-monooxygenase

enzyme: 6-hydroxynicotinate 3-monooxygenase


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: homogentisate 1,2-dioxygenase

substrate_name: homogentisate

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

enzyme: homogentisate 1,2-dioxygenase

substrate: homogentisate


proof_lines: pH not specified in the publication, 25°C, mutant Y346F


organism: Rattus norvegicus

substrate_name: dithiothreitol

smiles: C(C(C(CS)O)O)S

proof_lines: in the presence of 0.0017 mM R,S-warfarin

substrate: dithiothreitol


substrate_name: vitamin K 2,3-epoxide

substrate: vitamin K 2,3-epoxide


organism: Pseudomonas sp. ZZ-5

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADH


mutation_type: deletion


substrate_name: styrene 1',2'-oxide

substrate: styrene 1',2'-oxide


substrate_name: allylbenzene 2',3'-oxide

substrate: allylbenzene 2',3'-oxide


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonic acid

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)O

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonic acid


substrate_name: 5,8,11,14,17-eicosapentaenoic acid

smiles: CCC=CCC=CCC=CCC=CCC=CCCCC(=O)O

substrate: 5,8,11,14,17-eicosapentaenoic acid


enzyme_display_name: sterol 14alpha-demethylase

organism: Saccharomyces cerevisiae

substrate_name: lanosterol

proof_lines: fusion protein CYP51 (F1) consisting of the ORF of modified CYP51, a linker region containing the amino acid sequence S-T, and DELTA41 P450 reductase

enzyme: sterol 14alpha-demethylase

substrate: lanosterol


proof_lines: fusion protein CYP51 (F2) consisting of the ORF of modified CYP51, a linker region containing the amino acid sequence S-T-E-Q-S-A-K-K-V-R-K-K-A, and DELTA55 P450 reductase


enzyme_display_name: ferroxidase

substrate_name: hydroquinone

proof_lines:
wild-type, pH 6.0
wild-type
wild-type, pH 6.5, 25°C

enzyme: ferroxidase

substrate: hydroquinone


substrate_name: p-phenylenediamine

assay_conditions_summary: pH 6

substrate: p-phenylenediamine


enzyme_display_name: UniProt P10868

substrate_name: S-adenosyl-L-methionine

enzyme: UniProt P10868

substrate: S-adenosyl-L-methionine


substrate_name: Guanidinoacetate

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

substrate: Guanidinoacetate


enzyme_display_name: UniProt Q93088

organism: Homo sapiens

substrate_name: S-methyl-L-methionine

smiles: C[S+](C)CCC(C(=O)O)N

enzyme: UniProt Q93088

substrate: S-methyl-L-methionine


organism: Sorghum sp.


smiles: O=O


enzyme_display_name: superoxide dismutase

organism: Solanum lycopersicum

substrate_name: riboflavin

enzyme: superoxide dismutase

substrate: riboflavin


substrate_name: Nitro blue tetrazolium

substrate: Nitro blue tetrazolium


organism: Sus scrofa

substrate_name: o-Dianisidine

substrate: o-Dianisidine


enzyme_display_name: gibberellin 3beta-dioxygenase

organism: Triticum aestivum

substrate_name: gibberellin a9

enzyme: gibberellin 3beta-dioxygenase

substrate: gibberellin a9


substrate_name: gibberellin a20

substrate: gibberellin a20


enzyme_display_name: biflaviolin synthase

organism: Streptomyces coelicolor

substrate_name: flaviolin

proof_lines: mutant K90I of isoform CYP158A1, at pH 8.2 and 37°C

enzyme: biflaviolin synthase

substrate: flaviolin


proof_lines: mutant I87K of isoform CYP158A2, at pH 8.2 and 37°C


enzyme_display_name: ectoine hydroxylase

organism: Stutzerimonas stutzeri

substrate_name: ectoine

enzyme: ectoine hydroxylase

substrate: ectoine


enzyme_display_name: mercury(II) reductase

organism: Acidithiobacillus ferrooxidans

enzyme: mercury(II) reductase


smiles: CCCCCC=CCC=CCC=CC=CC(CCCC(=O)O)O


organism: Tupaia chinensis

proof_lines: pH 7.4, temperature not specified in the publication


substrate_name: arachidonate

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]

substrate: arachidonate


enzyme_display_name: carnitine monooxygenase

organism: Acinetobacter baumannii

substrate_name: Unknown

proof_lines: pH 7.6, temperature not specified in the publication

enzyme: carnitine monooxygenase

substrate: Unknown


enzyme_display_name: UniProt P50135

enzyme: UniProt P50135


organism: Arabidopsis thaliana

proof_lines: in 100 mM Tris-HCl pH 7.9 containing 4 mM ascorbate, 4 mM DTT, 4 mM 2-oxoglutarate, 0.5 mM FeSO4, 2 mg/ml bovine serum albumin and 1 mg/ml catalase


organism: Acinetobacter sp. Y64

substrate_name: catechol

substrate: catechol


enzyme_display_name: sterol 22-desaturase

substrate_name: beta-sitosterol

proof_lines: isoform CYP710A1, pH and temperature not specified in the publication

proof_lines: isoform CYP710A2, pH and temperature not specified in the publication

enzyme: sterol 22-desaturase

substrate: beta-sitosterol


organism: Zea mays


substrate_name: obtusifoliol

substrate: obtusifoliol


enzyme_display_name: UniProt B2HHT4

organism: Mycobacterium marinum

substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

enzyme: UniProt B2HHT4

substrate: octanoic acid


substrate_name: Decanoic acid

smiles: CCCCCCCCCC(=O)O

substrate: Decanoic acid


substrate_name: 3-hydroxyoctanoic acid

smiles: CCCCCC(CC(=O)O)O

substrate: 3-hydroxyoctanoic acid


substrate_name: 3-hydroxydecanoic acid

smiles: CCCCCCCC(CC(=O)O)O

substrate: 3-hydroxydecanoic acid


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: homogentisate

substrate: homogentisate


enzyme_display_name: indole-3-pyruvate monooxygenase

proof_lines: pH 8.5, 35°C, recombinant His-tagged enzyme

enzyme: indole-3-pyruvate monooxygenase


enzyme_display_name: fatty-acid O-methyltransferase

enzyme: fatty-acid O-methyltransferase


organism: Zymomonas mobilis

substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


substrate_name: phosphatidyl-N-methylethanolamine

substrate: phosphatidyl-N-methylethanolamine


substrate_name: phosphatidylethanolamine

smiles: CC(=O)OCC(COP(=O)(O)OCCN)OC(=O)C

substrate: phosphatidylethanolamine


substrate_name: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


enzyme_display_name: catechol O-methyltransferase

organism: Unknown

source_db: unknown

source_license: see source

enzyme: catechol O-methyltransferase

source: unknown


organism: Mycolicibacterium phlei


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleic acid


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase

enzyme: 9-cis-epoxycarotenoid dioxygenase


substrate_name: dodecanoic acid

smiles: CCCCCCCCCCCC(=O)O

substrate: dodecanoic acid


substrate_name: 3-hydroxydodecanoic acid

smiles: CCCCCCCCCC(CC(=O)O)O

substrate: 3-hydroxydodecanoic acid


organism: Pseudomonas sp.

substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


substrate_name: Trimethylsulfonium

substrate: Trimethylsulfonium


organism: Ricinus communis


enzyme_display_name: UniProt P82610

organism: Candida albicans

substrate_name: L-homocysteine

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

proof_lines: kcat is 25 min(-1) for homocysteine. kcat is 29 min(-1) for 5-methyl-tetrahydrofolate-triglutamate.

enzyme: UniProt P82610

substrate: L-homocysteine


enzyme_display_name: phenylethanolamine N-methyltransferase

organism: Oryctolagus cuniculus

substrate_name: m-octopamine

enzyme: phenylethanolamine N-methyltransferase

substrate: m-octopamine


enzyme_display_name: UniProt P11086

organism: Homo sapiens

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P11086


enzyme_display_name: glycine N-methyltransferase

organism: Rattus norvegicus

enzyme: glycine N-methyltransferase


substrate_name: Gly

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

substrate: Gly


organism: Catharanthus roseus


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

substrate_name: 5-methyltetrahydrofolate-triglutamate (at 37 degrees Celsius)


substrate_name: glycine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R175K with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

substrate: glycine


enzyme_display_name: polysaccharide O-methyltransferase

enzyme: polysaccharide O-methyltransferase


substrate_name: Glycine; S-Adenosyl-L-methionine

substrate: Glycine; S-Adenosyl-L-methionine


organism: Sus scrofa

substrate_name: S-Adenosyl-L-methionine; Glycine

substrate: S-Adenosyl-L-methionine; Glycine


organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: thiol S-methyltransferase

enzyme: thiol S-methyltransferase


organism: Arabidopsis thaliana


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: S-adenosyl-L-methionine (in presence of phosphatidylethanolamine (PE) as substrate)


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


column_label: Table 1 WT row, columns kcat min^-1, AdoMet Km uM, and AdoMet kcat/Km M^-1 s^-1: 174.5 +/- 23.2; 108 +/- 18; 26935 +/- 5738.

normalized_value_unit_evidence: kcat 2.908333333333333 s^(-1); AdoMet Km 0.108 mM; independently printed AdoMet kcat/Km 26.935 s^(-1)*mM^(-1).

raw_value_unit_evidence: WT row: kcat 174.5 +/- 23.2 min^-1; AdoMet Km 108 +/- 18 uM; independently printed AdoMet kcat/Km 26935 +/- 5738 M^-1 s^-1.

row_label: WT

table_label: Table 1. Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21A in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.59; column 'Km (uM)' under the AdoMet spanner = 539; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 18.3; the same data line prints the glycine spanner pair as 'Km (mM)' = 26.6 and 'kcat/Km (M-1 s-1)' = 0.37.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21A in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.59; printed Km (uM) cell 539; printed kcat/Km (M-1 s-1) cell 18.3.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21F in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 25.2; column 'Km (uM)' under the AdoMet spanner = 174; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 2409; the same data line prints the glycine spanner pair as 'Km (mM)' = 1.7 and 'kcat/Km (M-1 s-1)' = 248.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21F in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 25.2; printed Km (uM) cell 174; printed kcat/Km (M-1 s-1) cell 2409.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21G in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.93; column 'Km (uM)' under the AdoMet spanner = 696; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 22.3; the same data line prints the glycine spanner pair as 'Km (mM)' = 33.6 and 'kcat/Km (M-1 s-1)' = 0.46.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21G in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.93; printed Km (uM) cell 696; printed kcat/Km (M-1 s-1) cell 22.3.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21S in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.65; column 'Km (uM)' under the AdoMet spanner = 803; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 13.6; the same data line prints the glycine spanner pair as 'Km (mM)' = 23.4 and 'kcat/Km (M-1 s-1)' = 0.46.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21S in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.65; printed Km (uM) cell 803; printed kcat/Km (M-1 s-1) cell 13.6.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21T in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.81; column 'Km (uM)' under the AdoMet spanner = 1136; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 11.9; the same data line prints the glycine spanner pair as 'Km (mM)' = 22.9 and 'kcat/Km (M-1 s-1)' = 0.59.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21T in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.81; printed Km (uM) cell 1136; printed kcat/Km (M-1 s-1) cell 11.9.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21V in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.58; column 'Km (uM)' under the AdoMet spanner = 582; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 16.7; the same data line prints the glycine spanner pair as 'Km (mM)' = 38.8 and 'kcat/Km (M-1 s-1)' = 0.25.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21V in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.58; printed Km (uM) cell 582; printed kcat/Km (M-1 s-1) cell 16.7.


smiles: CN(C)CCO


substrate_name: 3-hydroxydecanoic acid

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q31A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

smiles: CCCCCCCC(O)CC(=O)O

proof_lines:
MmFAMT
Q31A
3-hydroxydecanoic acid

substrate: 3-hydroxydecanoic acid


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q26A/Q31A to reconstruct the assayed variant sequence.

column_label: Table 1; Wild-Type 3-OH-C10 row; KM, kcat, kcat/KM columns.

row_label: Wild-Type 3-OH-C10 row

table_label: Petronikolou and Nair 2015, Chemistry & Biology, Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase; kinetic table evidence


substrate_name: 3-hydroxyoctanoic acid

smiles: CCCCCC(O)CC(=O)O

column_label: Table 1; Wild-Type 3-OH-C8 row; KM, kcat, kcat/KM columns.

row_label: Wild-Type 3-OH-C8 row

substrate: 3-hydroxyoctanoic acid


substrate_name: Decanoic acid

column_label: Table 1; Wild-Type C10 row; KM, kcat, kcat/KM columns.

row_label: Wild-Type C10 row

substrate: Decanoic acid


substrate_name: octanoic acid

proof_lines:
MmFAMT
Q31A
octanoic acid

substrate: octanoic acid


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q26A/Q31A/V211L/L212V to reconstruct the assayed variant sequence.

column_label: Table 1; Wild-Type C8 row; KM, kcat, kcat/KM columns.

row_label: Wild-Type C8 row


column_label: Table 1; Wild-Type SAM row; KM, kcat, kcat/KM columns.

row_label: Wild-Type SAM row


organism: Mus musculus

assay_conditions_summary: pH 9

column_label: PubMed abstract states the apparent Km values for S-adenosyl-L-methionine were 20 and 400-500 microM for conversion of PE to PME, and 5 microM and 40 microM for conversion of PME to PC.

raw_value_unit_evidence: Km raw_value=20 raw_unit=microM

row_label: murine thymocyte phospholipid N-methyltransferase conversion of PE to PME with S-adenosyl-L-methionine

table_label: PubMed abstract PMID 3872629


enzyme_display_name: UniProt P13255

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.2
Raw SKiD Env: Temp=37°C, pH=7.4

enzyme: UniProt P13255


enzyme_display_name: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic

column_label: Table II row AtMS3, column Km for 5-CH3-H4PteGlu5.

normalized_value_unit_evidence: 17 uM normalizes to 0.017 mM.

raw_value_unit_evidence: Table II reports AtMS3 Km for 5-CH3-H4PteGlu5 as 17 +/- 3 uM.

row_label: AtMS3; Km for 5-CH3-H4PteGlu5

table_label: Table II, Kinetic properties of B12-independent MS isoforms from Arabidopsis


column_label: Table II row AtMS1, column Km for 5-CH3-H4PteGlu5.

normalized_value_unit_evidence: 60 uM normalizes to 0.060 mM.

raw_value_unit_evidence: Table II reports AtMS1 Km for 5-CH3-H4PteGlu5 as 60 +/- 7 uM.

row_label: AtMS1; Km for 5-CH3-H4PteGlu5


substrate_name: phosphatidylethanolamine (PE)

column_label: Abstract reports for the PEMT reactions, the apparent Km values for PE and S-adenosylmethionine were 57 microM and 110 microM, respectively.

raw_value_unit_evidence: Km raw_value=57 microM raw_unit=microM

row_label: Saccharomyces cerevisiae PEMT / phosphatidylethanolamine

table_label: PubMed XML abstract PMID 2198947

substrate: phosphatidylethanolamine (PE)


enzyme_display_name: Glycine N-methyltransferase

enzyme: Glycine N-methyltransferase


proof_lines:
human glycine N-methyltransferase
neutral pH kinetics
S-adenosylmethionine


substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


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


substrate_name: phosphatidylethanolamine

substrate: phosphatidylethanolamine


organism: Phaseolus sp.

substrate_name: homocysteine

substrate: homocysteine


substrate_name: S-methylmethionine

substrate: S-methylmethionine


enzyme_display_name: benzoate 4-monooxygenase

organism: Aspergillus niger

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: benzoate 4-monooxygenase

substrate: NADPH


substrate_name: benzoate

proof_lines: reconstituted enzyme system consisting of benzoate 4-hydroxylase, cytochrome P450 reductase, NADPH and dilauroylphosphatidylcholine

substrate: benzoate


organism: Saccharomyces cerevisiae


proof_lines: inhibition with respect to S-adenosylmethionine

proof_lines: inhibition with respect to phosphatidylethanolamine


enzyme_display_name: cysteine dioxygenase

organism: Bacillus subtilis

substrate_name: L-cysteine

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

proof_lines: YubC, measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography

enzyme: cysteine dioxygenase

substrate: L-cysteine


substrate_name: phosphatidyl-N-methylethanolamine

substrate: phosphatidyl-N-methylethanolamine


substrate_name: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


enzyme_display_name: UniProt P04818

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

enzyme: UniProt P04818


substrate_name: dUMP

proof_lines:
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=22°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

substrate: dUMP


enzyme_display_name: UniProt P0A884

organism: Escherichia coli

enzyme: UniProt P0A884


enzyme_display_name: UniProt Q834R3

organism: Enterococcus faecalis

enzyme: UniProt Q834R3


organism: Bos taurus

substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: Calmodulin

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

enzyme: nitric-oxide synthase (NADPH)

substrate: Calmodulin


enzyme_display_name: xanthine oxidase

enzyme: xanthine oxidase


enzyme_display_name: Indolethylamine N-methyltransferase

substrate_name: dimethyl selenide

smiles: C[Se]C

enzyme: Indolethylamine N-methyltransferase

substrate: dimethyl selenide


substrate_name: dimethyl sulfide

smiles: CSC

substrate: dimethyl sulfide


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: ferroxidase

substrate_name: NADH

assay_conditions_summary: pH 6; 303.15 K; cofactor NADH

proof_lines: pH 6.0, 30°C, presence of triflupromazine

proof_lines: pH 6.0, 30°C, presence of levomepromazine

proof_lines: pH 6.0, 30°C, presence of chlorpromazine

enzyme: ferroxidase

substrate: NADH


enzyme_display_name: peptide-aspartate beta-dioxygenase

substrate_name: first growth factor-like domain-L-aspartate

proof_lines: substrate is of human protein S, 56 kDa protein

proof_lines: substrate is of human protein S with an asparagine replacing the aspartic acid at position 18, 56 kDa protein

proof_lines: substrate is of human protein S, 52 kDa protein

enzyme: peptide-aspartate beta-dioxygenase


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: Unknown

proof_lines: N-alpha-acetyl heptapeptide, identical to the last seven amino acids of R2 subunit C-terminus from mouse enzyme

enzyme: ribonucleoside-diphosphate reductase

substrate: Unknown


substrate_name: allopurinol

substrate: allopurinol


enzyme_display_name: UniProt Q8SR66

organism: Encephalitozoon cuniculi

substrate_name: GDP

enzyme: UniProt Q8SR66

substrate: GDP


enzyme_display_name: mercury(II) reductase

organism: Bacillus sp. (in: firmicutes)

proof_lines: recombinant catalytic core, 25°C, pH 7.3

proof_lines: recombinant catalytic core, presence of N-terminal sequence NmerA, 25°C, pH 7.3

enzyme: mercury(II) reductase


substrate_name: Ngamma-hydroxy-L-arginine

substrate: Ngamma-hydroxy-L-arginine


substrate_name: dibromoacetonitrile

smiles: C(#N)C(Br)Br

substrate: dibromoacetonitrile


proof_lines: in 50 mM potassium phosphate (pH 7.2), 50 mM Tris-Cl (pH 7.2) containing 0.1 mM MgSO4, 10 mM dithiothreitol and 2 mM L-homocysteine at 37°C


substrate_name: L-homocysteine

substrate: L-homocysteine


substrate_name: S-adenosylmethionine

proof_lines:
at pH 8.5
at pH 10

substrate: S-adenosylmethionine


enzyme_display_name: caffeate O-methyltransferase

organism: Leucaena leucocephala

enzyme: caffeate O-methyltransferase


enzyme_display_name: Caffeic acid 3-O-methyltransferase

organism: Zea mays

substrate_name: tricetin

enzyme: Caffeic acid 3-O-methyltransferase

substrate: tricetin


substrate_name: luteolin

substrate: luteolin


substrate_name: pterin

proof_lines: cell-associated enzyme, determined in intact cell monolayers

substrate: pterin


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Buttiauxella sp. S19-1

enzyme: protocatechuate 3,4-dioxygenase


organism: Canis lupus familiaris

substrate_name: vitamin K1 2,3-epoxide


enzyme_display_name: sterol 14alpha-demethylase

organism: Candida albicans

substrate_name: lanosterol

proof_lines: pH and temperature not specified in the publication

enzyme: sterol 14alpha-demethylase

substrate: lanosterol


organism: Nicotiana tabacum


substrate_name: esculetin

substrate: esculetin


substrate_name: homocatechol

substrate: homocatechol


substrate_name: 5-hydroxyferulic acid

substrate: 5-hydroxyferulic acid


substrate_name: caffeic acid

substrate: caffeic acid


substrate_name: Hydrocaffeic acid

substrate: Hydrocaffeic acid


substrate_name: Protocatechuic aldehyde

substrate: Protocatechuic aldehyde


substrate_name: catechol

substrate: catechol


substrate_name: chlorogenic acid

substrate: chlorogenic acid


substrate_name: protocatechuic acid

substrate: protocatechuic acid


organism: Vanilla planifolia

substrate_name: 5-hydroxyferulic acid ethyl ester

substrate: 5-hydroxyferulic acid ethyl ester


substrate_name: caffeic acid ethyl ester

substrate: caffeic acid ethyl ester


substrate_name: caffeoyl aldehyde

substrate: caffeoyl aldehyde


organism: Beta vulgaris

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: Unknown

substrate: Unknown


organism: Triticum aestivum


substrate_name: caffeoyl alcohol

substrate: caffeoyl alcohol


substrate_name: 5-hydroxyconiferyl alcohol

substrate: 5-hydroxyconiferyl alcohol


enzyme_display_name: licodione 2'-O-methyltransferase

organism: Glycyrrhiza echinata

enzyme: licodione 2'-O-methyltransferase


substrate_name: licodione

substrate: licodione


organism: Petroselinum crispum


proof_lines: reaction with bergaptol or 5-hydroxyxanthotoxin


substrate_name: bergaptol

substrate: bergaptol


organism: Conioselinum anthriscoides


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


substrate_name: caffeic acid methyl ester

substrate: caffeic acid methyl ester


organism: Bambusa sp.

substrate_name: 5-hydroxyferulic acid

substrate: 5-hydroxyferulic acid


substrate_name: caffeic acid

substrate: caffeic acid


organism: Trigonella foenum-graecum


enzyme_display_name: thiopurine S-methyltransferase

organism: Homo sapiens

proof_lines:
recombinant enzyme, expressed in yeast
isoenzyme II
cell lysate

enzyme: thiopurine S-methyltransferase


proof_lines:
recombinant enzyme, expressed in yeast
isoenzyme II
isoenzyme I


organism: Cyberlindnera jadinii


enzyme_display_name: trimethylamine monooxygenase

substrate_name: Benzydamine

assay_conditions_summary: pH 7.4; 310.15 K; buffer in 0.1 M tricine

proof_lines: in in 0.1 M tricine buffer, pH 7.4, at 37°C

enzyme: trimethylamine monooxygenase

substrate: Benzydamine


substrate_name: myricetin

substrate: myricetin


substrate_name: methyl gallate

substrate: methyl gallate


proof_lines:
cell lysate
isoenzyme II
Molt-F4 cell


organism: Rehmannia glutinosa


organism: Medicago sativa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N324H/M130L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A162T with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L136Y to reconstruct the assayed variant sequence.


substrate_name: Protocatechuic aldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N131K to reconstruct the assayed variant sequence.

substrate: Protocatechuic aldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N131D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N324Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H183K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F172Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N131E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N131L to reconstruct the assayed variant sequence.


substrate_name: protocatechuic acid

substrate: protocatechuic acid


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M130L with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: quercetin

proof_lines: pH 7.5, temperature not specified in the publication

substrate: quercetin


organism: Lolium arundinaceum

column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row 5-Hydroxyferulic acid; column Km (microM): 10.89 +/- 1.52 microM; normalized Km=0.01089 mM.

normalized_value_unit_evidence: Km paper=0.01089 mM after exact conversion of 10.89 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row 5-Hydroxyferulic acid: Km 10.89 +/- 1.52 microM.

row_label: 5-Hydroxyferulic acid


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row Caffeoyl aldehyde; column Km (microM): 14.78 +/- 1.44 microM; normalized Km=0.01478 mM.

normalized_value_unit_evidence: Km paper=0.01478 mM after exact conversion of 14.78 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row Caffeoyl aldehyde: Km 14.78 +/- 1.44 microM.

row_label: Caffeoyl aldehyde


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row 5-Hydroxyconiferaldehyde; column Km (microM): 18.52 +/- 2.48 microM; normalized Km=0.01852 mM.

normalized_value_unit_evidence: Km paper=0.01852 mM after exact conversion of 18.52 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row 5-Hydroxyconiferaldehyde: Km 18.52 +/- 2.48 microM.


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row Caffeoyl alcohol; column Km (microM): 27.30 +/- 3.40 microM; normalized Km=0.02730 mM.

normalized_value_unit_evidence: Km paper=0.02730 mM after exact conversion of 27.30 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row Caffeoyl alcohol: Km 27.30 +/- 3.40 microM.

row_label: Caffeoyl alcohol


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row Caffeic acid; column Km (microM): 49.74 +/- 4.88 microM; normalized Km=0.04974 mM.

normalized_value_unit_evidence: Km paper=0.04974 mM after exact conversion of 49.74 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row Caffeic acid: Km 49.74 +/- 4.88 microM.

row_label: Caffeic acid


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row 5-Hydroxyconiferyl alcohol; column Km (microM): 67.77 +/- 4.62 microM; normalized Km=0.06777 mM.

normalized_value_unit_evidence: Km paper=0.06777 mM after exact conversion of 67.77 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row 5-Hydroxyconiferyl alcohol: Km 67.77 +/- 4.62 microM.

row_label: 5-Hydroxyconiferyl alcohol


proof_lines:
wild type
wild-type enzyme


enzyme_display_name: Flavone 3'-O-methyltransferase 1

organism: Oryza sativa subsp. japonica

substrate_name: 5-hydroxyferulate (at pH 7.5 and 30 degrees Celsius)

proof_lines: Measured at pH 7.5 and 37 degrees Celsius for all experiments.

enzyme: Flavone 3'-O-methyltransferase 1


substrate_name: caffealdehyde (at pH 7.5 and 30 degrees Celsius)


substrate_name: 5-hydroxyconiferaldehyde (at pH 7.5 and 30 degrees Celsius)


substrate_name: caffeyl alcohol (at pH 7.5 and 30 degrees Celsius)


substrate_name: 5-hydroxyconiferyl alcohol (at pH 7.5 and 30 degrees Celsius)


organism: Rattus norvegicus


substrate_name: S-adenosyl-L-methionine


organism: Oryza sativa

proof_lines: when caffeic acid is supplied at a constant concentration of 1 mM


proof_lines: when S-adenosyl-L-methionine is supplied at a constant concentration of 1 mM


column_label: Table 2 columns Substrate and Km (uM); row Quercetin 1; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Quercetin 1 reports Km = 61.8 uM.

row_label: Quercetin 1

table_label: Table 2: Substrate specificity of purified recombinant protein ROMT-9


substrate_name: luteolin

column_label: Table 2 columns Substrate and Km (uM); row Luteolin 5; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Luteolin 5 reports Km = 61.9 uM.

row_label: Luteolin 5

substrate: luteolin


substrate_name: eriodictyol

column_label: Table 2 columns Substrate and Km (uM); row Eriodictyol 4; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Eriodictyol 4 reports Km = 62.0 uM.

row_label: Eriodictyol 4

substrate: eriodictyol


proof_lines:
isozyme I
isozyme II
recombinant enzyme

source_databases_merged: brenda skid


enzyme_display_name: tocopherol C-methyltransferase

organism: Vinca minor

enzyme: tocopherol C-methyltransferase

substrate: S-adenosyl-L-methionine


substrate_name: picrinine

substrate: picrinine


substrate_name: N-acetylserotonin

column_label: Table 2. Kinetic analysis of AtCOMT WT and mutants towards NAS; row Table 2 row WT; columns Km (mM), kcat (s^-1), kcat/Km (10^3 s^-1 M^-1).

raw_value_unit_evidence: Table 2 Table 2 row WT reports Km 0.74 mM; kcat 2.94 s^-1; kcat/Km 3.99 x 10^3 s^-1 M^-1.

row_label: Table 2 row WT

substrate: N-acetylserotonin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q310L to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic analysis of AtCOMT WT and mutants towards NAS; row Table 2 row Q310L; columns Km (mM), kcat (s^-1), kcat/Km (10^3 s^-1 M^-1).

raw_value_unit_evidence: Table 2 Table 2 row Q310L reports Km 0.36 mM; kcat 4.76 s^-1; kcat/Km 13.11 x 10^3 s^-1 M^-1.

row_label: Table 2 row Q310L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C296F to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic analysis of AtCOMT WT and mutants towards NAS; row Table 2 row C296F; columns Km (mM), kcat (s^-1), kcat/Km (10^3 s^-1 M^-1).

raw_value_unit_evidence: Table 2 Table 2 row C296F reports Km 0.58 mM; kcat 5.41 s^-1; kcat/Km 9.37 x 10^3 s^-1 M^-1.

row_label: Table 2 row C296F


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V314T to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic analysis of AtCOMT WT and mutants towards NAS; row Table 2 row V314T; columns Km (mM), kcat (s^-1), kcat/Km (10^3 s^-1 M^-1).

raw_value_unit_evidence: Table 2 Table 2 row V314T reports Km 0.58 mM; kcat 11.32 s^-1; kcat/Km 19.53 x 10^3 s^-1 M^-1.

row_label: Table 2 row V314T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C296F/Q310L/V314T to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic analysis of AtCOMT WT and mutants towards NAS; row Table 2 row C296F-Q310L-V314T; columns Km (mM), kcat (s^-1), kcat/Km (10^3 s^-1 M^-1).

row_label: Table 2 row C296F-Q310L-V314T


enzyme_display_name: UniProt Q944H0

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

assay_conditions_summary: pH 8

enzyme: UniProt Q944H0


substrate_name: N-methylethanolamine phosphate

smiles: CNCCOP(=O)(O)O

substrate: N-methylethanolamine phosphate


substrate_name: Ethanolamine phosphate

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

substrate: Ethanolamine phosphate


substrate_name: N,N-dimethylethanolamine phosphate

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

substrate: N,N-dimethylethanolamine phosphate


enzyme_display_name: UniProt Q9FR44

enzyme: UniProt Q9FR44


enzyme_display_name: caffeoyl-CoA O-methyltransferase

substrate_name: caffeoyl-CoA

enzyme: caffeoyl-CoA O-methyltransferase

substrate: caffeoyl-CoA


organism: Euglena gracilis

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


organism: Streptomyces antibioticus


organism: Capsicum annuum


substrate_name: gamma-tocopherol

substrate: gamma-tocopherol


substrate_name: delta-tocopherol

substrate: delta-tocopherol


enzyme_display_name: (S)-scoulerine 9-O-methyltransferase

organism: Coptis japonica

substrate_name: (S)-scoulerine

enzyme: (S)-scoulerine 9-O-methyltransferase

substrate: (S)-scoulerine


organism: Spinacia oleracea


substrate_name: S-adenosyl-L-methionine (at pH 9.4)

proof_lines: kcat is 0.036 min(-1) for m7GpppAm capped mRNA (PubMed:31279659). kcat is 0.34 min(-1) for m7GpppAm dinucleotide (PubMed:31279659). kcat is 1.76 min(-1) for capped mRNA analog (at pH 5.4) (PubMed:33428944). kcat is 1.44 min(-1) for S-adenos

substrate: S-adenosyl-L-methionine (at pH 9.4)


organism: Eschscholzia californica

substrate_name: (S)-canadine

substrate: (S)-canadine


organism: Anopheles gambiae


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


organism: Angelica dahurica

substrate_name: bergaptol

substrate: bergaptol


organism: Chlamydomonas reinhardtii

proof_lines: in 50 mM HEPES (pH 7.5), 5 mM dithiothreitol, temperature not specified in the publication


enzyme_display_name: macrocin O-methyltransferase

organism: Streptomyces fradiae

proof_lines:
lactenocin as substrate
macrocin as substrate

enzyme: macrocin O-methyltransferase


organism: Medicago sativa

column_label: Table 3; 5-Hydroxyconiferaldehyde row; K_m (uM) column; raw K_m value 1.8 uM.

raw_value_unit_evidence: Table 3 reports 5-Hydroxyconiferaldehyde K_m = 1.8 uM.

row_label: 5-Hydroxyconiferaldehyde row; K_m column

table_label: PMID 11169195, Table 3: Kinetic properties of purified recombinant alfalfa COMT


substrate_name: 5-hydroxyconiferyl alcohol

column_label: Table 3; 5-Hydroxyconiferyl alcohol row; K_m (uM) column; raw K_m value 3.8 uM.

raw_value_unit_evidence: Table 3 reports 5-Hydroxyconiferyl alcohol K_m = 3.8 uM.

row_label: 5-Hydroxyconiferyl alcohol row; K_m column

substrate: 5-hydroxyconiferyl alcohol


substrate_name: 5-hydroxyferulic acid

column_label: Table 3; 5-Hydroxyferulic acid row; K_m (uM) column; raw K_m value 6.8 uM.

raw_value_unit_evidence: Table 3 reports 5-Hydroxyferulic acid K_m = 6.8 uM.

row_label: 5-Hydroxyferulic acid row; K_m column

substrate: 5-hydroxyferulic acid


substrate_name: caffeoyl aldehyde

column_label: Table 3; Caffeoyl aldehyde row; K_m (uM) column; raw K_m value 6.9 uM.

raw_value_unit_evidence: Table 3 reports Caffeoyl aldehyde K_m = 6.9 uM.

row_label: Caffeoyl aldehyde row; K_m column

substrate: caffeoyl aldehyde


substrate_name: caffeoyl alcohol

column_label: Table 3; Caffeoyl alcohol row; K_m (uM) column; raw K_m value 11.5 uM.

normalized_value_unit_evidence: 11.5 uM = 0.0115 mM; expected rounded value is 0.012 mM.

raw_value_unit_evidence: Table 3 reports Caffeoyl alcohol K_m = 11.5 uM.

row_label: Caffeoyl alcohol row; K_m column

substrate: caffeoyl alcohol


organism: Catharanthus roseus

proof_lines: kcat is 2.47 sec(-1) for 2,3-dihydrotabersonine. kcat is 5.4 sec(-1) for S-adenosyl-L-methionine.


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Rauvolfia serpentina

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


substrate_name: picrinine

substrate: picrinine


enzyme_display_name: UniProt Q948P7

substrate_name: (RS)-coclaurine

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=8

enzyme: UniProt Q948P7

substrate: (RS)-coclaurine


substrate_name: heliamine

substrate: heliamine


substrate_name: (S)-N-methylcoclaurine

substrate: (S)-N-methylcoclaurine


enzyme_display_name: jasmonate O-methyltransferase

organism: Brassica rapa subsp. oleifera

enzyme: jasmonate O-methyltransferase


substrate_name: jasmonate

substrate: jasmonate


organism: Argemone platyceras


substrate_name: S-adenosylmethionine

proof_lines: with (S)-norlaudanosoline as cosubstrate

substrate: S-adenosylmethionine


substrate_name: (R,S)-norlaudanosoline

substrate: (R,S)-norlaudanosoline


substrate_name: (R,S)-laudanosoline

substrate: (R,S)-laudanosoline


proof_lines:
isozyme II
isozyme I


enzyme_display_name: inositol 4-methyltransferase

organism: Vigna umbellata

enzyme: inositol 4-methyltransferase


substrate_name: myo-inositol

substrate: myo-inositol


organism: Arabidopsis thaliana

substrate_name: [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine


organism: Nicotiana rustica


organism: Mus musculus


organism: Stephania tetrandra

substrate_name: (S)-norcoclaurine

substrate: (S)-norcoclaurine


organism: Pseudomonas denitrificans (nom. rej.)


enzyme_display_name: UniProt Q5UVJ4

organism: Helicobacter pylori

enzyme: UniProt Q5UVJ4


substrate_name: dUMP

substrate: dUMP


organism: Tribolium castaneum

proof_lines: kcat is 3.3 min(-1) for S-adenosyl-L-methionine. kcat is 1.4 min(-1) for biotin-S-farnesyl-L-cysteine (BFC).


organism: Lathyrus oleraceus

proof_lines: kcat is 0.047 sec(-1) for S-adenosyl-L-methionine. kcat is 0.038 sec(-1) for rubisco.


organism: Carapichea ipecacuanha

substrate_name: N-deacetylisoipecoside

proof_lines: kcat is 11.3x10(-3) sec(-1) with N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 20.4x10(-3) sec(-1) with 7-O-methyl-N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 0.28x10(-3) sec(-1) with cephaeline as substr

substrate: N-deacetylisoipecoside


substrate_name: cephaeline

substrate: cephaeline


proof_lines: kcat is 0.34x10(-3) sec(-1) with N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 3.8x10(-3) sec(-1) with demethylalangiside as substrate (PubMed:20061395). kcat is 2.3x10(-3) sec(-1) with redipecamine as substrate (PubMed:200


substrate_name: demethylalangiside

substrate: demethylalangiside


enzyme_display_name: caffeate O-methyltransferase

organism: Oryza sativa

substrate_name: N-acetylserotonin

enzyme: caffeate O-methyltransferase

substrate: N-acetylserotonin


enzyme_display_name: cycloartenol 24-C-methyltransferase

enzyme: cycloartenol 24-C-methyltransferase


substrate_name: Cycloartenol

substrate: Cycloartenol


substrate_name: fecosterol

substrate: fecosterol


substrate_name: dehydropollinastanol

proof_lines: pH 7.4, 35°C, substrate: 24(28)-methylenelophenol

substrate: dehydropollinastanol


substrate_name: Zymosterol

substrate: Zymosterol


substrate_name: obtusifoliol

substrate: obtusifoliol


proof_lines:
pH 7.5, 35°C
pH 7.4, 35°C, substrate cycloartenol


organism: Populus trichocarpa

proof_lines: isoform COMT1, in 50 mM Tris-HCl, pH 7.5, at 30°C


organism: Papaver somniferum

substrate_name: (R,S)-norcoclaurine

column_label: Row PSOMT2 / (R,S)-Norcoclaurine; column K m Substrate (uM).

normalized_value_unit_evidence: Km 0.01 mM

raw_value_unit_evidence: Table 3. Kinetic parameters of PSOMT1 and PSOMT2 for various substrates and co-substrate (AdoMet), row PSOMT2 / (R,S)-Norcoclaurine: Km substrate 10 uM.

row_label: PSOMT2 / (R,S)-Norcoclaurine

substrate: (R,S)-norcoclaurine


enzyme_display_name: corydaline synthase

organism: Corydalis cava

substrate_name: S-adenosyl-L-methionine

enzyme: corydaline synthase

substrate: S-adenosyl-L-methionine


substrate_name: Berberine

substrate: Berberine


substrate_name: NADPH

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


organism: Prototheca wickerhamii


substrate_name: desmosterol

substrate: desmosterol


substrate_name: lanosterol

substrate: lanosterol


substrate_name: parkeol

substrate: parkeol


enzyme_display_name: myricetin O-methyltransferase

substrate_name: caffeoyl-coenzyme A

assay_conditions_summary: cofactor CoA

proof_lines:
isoform ROMT-17
isoform ROMT-15

enzyme: myricetin O-methyltransferase

substrate: caffeoyl-coenzyme A


substrate_name: luteolin

substrate: luteolin


substrate_name: myricetin

proof_lines:
isoform ROMT-17
isoform ROMT-15
pH 7.5, 37°C

substrate: myricetin


substrate_name: tricetin

substrate: tricetin


organism: Glycine max

substrate_name: 24(28)-methylene lophenol

substrate: 24(28)-methylene lophenol


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


substrate_name: Cycloartenol

substrate: Cycloartenol


organism: Chlamydomonas reinhardtii

substrate_name: 24(28)-methylene cycloartenol

substrate: 24(28)-methylene cycloartenol


enzyme_display_name: (iso)eugenol O-methyltransferase

organism: Rosa chinensis

substrate_name: eugenol

enzyme: (iso)eugenol O-methyltransferase

substrate: eugenol


substrate_name: isoeugenol

substrate: isoeugenol


organism: Helianthus annuus


substrate_name: Zymosterol

substrate: Zymosterol


substrate_name: Agnosterol

substrate: Agnosterol


substrate_name: cyclobranol

substrate: cyclobranol


organism: Paracoccidioides brasiliensis

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


organism: Pimpinella anisum


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


assay_conditions_summary: pH 7.5; 308.15 K; buffer phosphate

proof_lines:
pH 7.5, 35°C, recombinant enzyme
pH 7.5, 35°C
at 35°C in phosphate buffer at pH 8.0


organism: Zea mays

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Flavin-dependent thymidylate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: dUMP

enzyme: Flavin-dependent thymidylate synthase

substrate: dUMP


substrate_name: NADPH

substrate: NADPH


organism: Clarkia breweri

proof_lines:
plant-purified enzyme
recombinant enzyme
Raw SKiD Env: Temp=-----, pH=-----


proof_lines:
recombinant enzyme
plant-purified enzyme
Raw SKiD Env: Temp=-----, pH=-----


substrate_name: sinapyl alcohol

proof_lines: pH 7.5, 30°C, recombinant enzyme mutant MOMT8

proof_lines: pH 7.5, 30°C, recombinant enzyme mutant MOMT9

proof_lines: pH 7.5, 30°C, recombinant enzyme mutant MOMT5

substrate: sinapyl alcohol


substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


enzyme_display_name: tabersonine 16-O-methyltransferase

organism: Catharanthus roseus

enzyme: tabersonine 16-O-methyltransferase


substrate_name: S-adenosyl-L-methionine with (R,S)-norcoclaurine as substrate

proof_lines: kcat is 0.08 sec(-1) with (R,S)-norcoclaurine as substrate. kcat is 0.02 sec(-1) with (R)-norprotosinomenine as substrate. kcat is 0.02 sec(-1) with (S)-norprotosinomenine as substrate. kcat is 0.03 sec(-1) with (R,S)-isoorientaline as subs


enzyme_display_name: thymidylate synthase (FAD)

organism: Thermotoga maritima

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

source_databases_merged: brenda skid uniprot

enzyme: thymidylate synthase (FAD)


organism: Asarum sieboldii

proof_lines: pH and temperature not specified in the publication


organism: Arabidopsis thaliana


organism: Homo sapiens


organism: Mus musculus


organism: Rattus norvegicus


organism: Nicotiana sp.

substrate_name: ribulose-1,5-bisphosphate carboxylase

substrate: ribulose-1,5-bisphosphate carboxylase


proof_lines: kcat is 2.47 sec(-1) for 2,3-dihydrotabersonine. kcat is 5.4 sec(-1) for S-adenosyl-L-methionine.


substrate_name: 5-hydroxyconiferyl aldehyde

proof_lines: pH 7.5, temperature not specified in the publication

substrate: 5-hydroxyconiferyl aldehyde


organism: Medicago sativa

proof_lines:
isozyme II
isozyme I


enzyme_display_name: Flavone 3'-O-methyltransferase 1

organism: Oryza sativa subsp. japonica

proof_lines: Measured at pH 7.5 and 37 degrees Celsius for all experiments.

enzyme: Flavone 3'-O-methyltransferase 1


enzyme_display_name: Caffeic acid 3-O-methyltransferase

enzyme: Caffeic acid 3-O-methyltransferase


enzyme_display_name: thioether S-methyltransferase

substrate_name: ethyl vinyl sulfide

smiles: CCSC=C

enzyme: thioether S-methyltransferase

substrate: ethyl vinyl sulfide


organism: Pisum sativum

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

proof_lines:
native enzyme
at pH 7.8 and 30°C
recombinant enzyme

source_databases_merged: sabio_rk brenda skid uniprot


organism: Carapichea ipecacuanha

substrate_name: redipecamine

proof_lines: kcat is 0.34x10(-3) sec(-1) with N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 3.8x10(-3) sec(-1) with demethylalangiside as substrate (PubMed:20061395). kcat is 2.3x10(-3) sec(-1) with redipecamine as substrate (PubMed:200

substrate: redipecamine


proof_lines: kcat is 11.3x10(-3) sec(-1) with N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 20.4x10(-3) sec(-1) with 7-O-methyl-N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 0.28x10(-3) sec(-1) with cephaeline as substr


organism: Papaver somniferum


organism: Paramecium bursaria Chlorella virus 1


proof_lines: kcat is 0.036 min(-1) for m7GpppAm capped mRNA (PubMed:31279659). kcat is 0.34 min(-1) for m7GpppAm dinucleotide (PubMed:31279659). kcat is 1.76 min(-1) for capped mRNA analog (at pH 5.4) (PubMed:33428944). kcat is 1.44 min(-1) for S-adenos


organism: Anopheles gambiae

substrate_name: biotin-S-farnesyl-L-cysteine

substrate: biotin-S-farnesyl-L-cysteine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Spodoptera frugiperda

proof_lines: with respect to farnesylated and Rce1-proteolyzed K-Ras protein as substrate

proof_lines: with respect to S-adenosyl-L-methionine as substrate


organism: Tribolium castaneum

proof_lines: kcat is 3.3 min(-1) for S-adenosyl-L-methionine. kcat is 1.4 min(-1) for biotin-S-farnesyl-L-cysteine (BFC).


organism: Streptomyces fradiae

proof_lines:
fixed substrate macrocin
fixed substrate S-adenosyl-L-methionine
fixed substrate lactenocin


organism: Lathyrus oleraceus

substrate_name: L-Lys

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

substrate: L-Lys


organism: Clarkia breweri

substrate_name: Caffeate; S-Adenosyl-L-methionine

substrate: Caffeate; S-Adenosyl-L-methionine


organism: Ocimum basilicum


organism: Triticum aestivum


substrate_name: Eugenol; S-Adenosyl-L-methionine

substrate: Eugenol; S-Adenosyl-L-methionine


substrate_name: S-Adenosyl-L-methionine; Chavicol

substrate: S-Adenosyl-L-methionine; Chavicol


organism: Chlamydia trachomatis

substrate_name: 5,10-Methylenetetrahydrofolate; H+; NADPH; dUMP


organism: Thermotoga maritima

substrate_name: H+; 5,10-Methylenetetrahydrofolate; NADPH; dUMP


enzyme_display_name: thiopurine S-methyltransferase

organism: Homo sapiens

substrate_name: S-Adenosyl-L-methionine; Mercaptopurine

enzyme: thiopurine S-methyltransferase

substrate: S-Adenosyl-L-methionine; Mercaptopurine


organism: Mus musculus


enzyme_display_name: Trans-aconitate 3-methyltransferase

substrate_name: trans-aconitate

enzyme: Trans-aconitate 3-methyltransferase

substrate: trans-aconitate


substrate_name: itaconate

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

column_label: Abstract reports itaconate, the decarboxylation product, was recognized poorly with a Km of 44 mM.

raw_value_unit_evidence: Km raw_value=44 mM raw_unit=mM

row_label: Saccharomyces cerevisiae TMT1 trans-aconitate methyltransferase / itaconate

table_label: PubMed XML abstract PMID 11695919

substrate: itaconate


substrate_name: isopropylmaleate

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

substrate: isopropylmaleate


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


substrate_name: Chavicol

column_label: Table 1 row EOMT1 / Chavicol; exported value set does not exactly match the explicit table row/cell values preserved here.

raw_value_unit_evidence: Export has kcat 0.0009 and derived kcat/Km 0.12857142857142856, but Table 1 reports kcat 8.7 x 10^-4 and kcat/Km column 0.13 for EOMT1 / Chavicol.

row_label: EOMT1 / Chavicol

table_label: Table 1. Properties of Basil Phenylpropanoid OMTs

substrate: Chavicol


column_label: Table 1 row CVOMT1 / Chavicol; columns Km for substrate (6 uM) and kcat (8.0 x 10^-4 s^-1); kcat/Km calculated from normalized kcat and Km cells.

normalized_value_unit_evidence: kcat normalized value: 0.0008; normalized unit: s^-1; km normalized value: 0.006; normalized unit: mM; kcat_over_km normalized value: 0.13333333333333333; normalized unit: s^-1 mM^-1

raw_value_unit_evidence: Table 1 CVOMT1 / Chavicol: Km for substrate 6 uM; kcat 8.0 x 10^-4 s^-1; printed kcat/Km column 0.13.

row_label: CVOMT1 / Chavicol


substrate_name: Eugenol

column_label: Table 1 row EOMT1 / Eugenol; exported value set does not exactly match the explicit table row/cell values preserved here.

raw_value_unit_evidence: Export has kcat 0.003 and kcat/Km 1.0, but Table 1 reports kcat 3.1 x 10^-3 and kcat/Km column 1.23 for EOMT1 / Eugenol.

row_label: EOMT1 / Eugenol

substrate: Eugenol


substrate_name: S-Adenosyl-L-methionine

column_label: Table 1 row EOMT1 / SAM Km column in Eugenol assay row; exported value set does not exactly match the explicit table row/cell values preserved here.

raw_value_unit_evidence: Export has kcat 0.003 and kcat/Km 0.6 for SAM, but Table 1 gives kcat 3.1 x 10^-3 and SAM Km 5 uM; derived kcat/SAM-Km is 0.62 s^-1 mM^-1.

substrate: S-Adenosyl-L-methionine


column_label: Table 1 row CVOMT1 with Km for SAM column 5 uM and kcat column 8.0 x 10^-4 s^-1; exported substrate is SAM, so kcat/Km is derived from normalized kcat and SAM Km cells.

normalized_value_unit_evidence: kcat normalized value: 0.0008; normalized unit: s^-1; km normalized value: 0.005; normalized unit: mM; kcat_over_km normalized value: 0.16; normalized unit: s^-1 mM^-1

raw_value_unit_evidence: Table 1 CVOMT1 row: Km for SAM 5 uM; substrate Chavicol; kcat 8.0 x 10^-4 s^-1.

row_label: CVOMT1 / SAM Km column in Chavicol assay row


substrate_name: isoeugenol

column_label: Table 1 row EOMT1 / t-Isoeugenol; exported value set does not exactly match the explicit table row/cell values preserved here.

normalized_value_unit_evidence: paper_kcat_s^-1: 0.0013; paper_km_mM: 0.01; paper_kcat_over_km_s^-1_mM^-1: 0.13

raw_value_unit_evidence: Export has kcat 0.001 and kcat/Km 0.1, but Table 1 reports kcat 1.3 x 10^-3 and kcat/Km column 0.13 for EOMT1 / t-Isoeugenol.

row_label: EOMT1 / t-Isoeugenol

substrate: isoeugenol


enzyme_display_name: Chavicol O-methyltransferase

substrate_name: chavicol

column_label: Table 1 row CVOMT1 / Chavicol; column Km for substrate (6 uM).

normalized_value_unit_evidence: km normalized value: 0.006; normalized unit: mM

raw_value_unit_evidence: Table 1 CVOMT1 / Chavicol: Km for substrate 6 uM.

enzyme: Chavicol O-methyltransferase

substrate: chavicol


enzyme_display_name: Eugenol O-methyltransferase

column_label: Table 1 row EOMT1 / Chavicol; column Km for substrate (7 uM).

normalized_value_unit_evidence: km normalized value: 0.007; normalized unit: mM

raw_value_unit_evidence: Table 1 EOMT1 / Chavicol: Km for substrate 7 uM.

enzyme: Eugenol O-methyltransferase


organism: Ammi majus

substrate_name: caffeate

proof_lines:
AmCOMT
BMT
5-hydroxyferulic acid

substrate: caffeate


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: 5-hydroxyferulic acid

substrate: 5-hydroxyferulic acid


substrate_name: caffeic acid methyl ester

substrate: caffeic acid methyl ester


substrate_name: caffeoyl coenzyme A

substrate: caffeoyl coenzyme A


substrate_name: esculetin

substrate: esculetin


substrate_name: daphnetin

substrate: daphnetin


enzyme_display_name: UniProt F6KV61

organism: Methanohalophilus portucalensis

enzyme: UniProt F6KV61


organism: Papaver somniferum

substrate_name: (R)-Norprotosinomenine

column_label: Row PSOMT2 / (R)-Norprotosinomenine; columns K m Substrate (uM), k cat Substrate (sec^-1), and k cat/Km Substrate (sec^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters of PSOMT1 and PSOMT2 for various substrates and co-substrate (AdoMet), row PSOMT2 / (R)-Norprotosinomenine: Km substrate 5 uM; kcat substrate 0.02 sec^-1; kcat/Km substrate 4.1 sec^-1 mM^-1.

row_label: PSOMT2 / (R)-Norprotosinomenine

substrate: (R)-Norprotosinomenine


substrate_name: (R,S)-Norcoclaurine

column_label: Row PSOMT2 / (R,S)-Norcoclaurine; columns K m Substrate (uM), k cat Substrate (sec^-1), and k cat/Km Substrate (sec^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters of PSOMT1 and PSOMT2 for various substrates and co-substrate (AdoMet), row PSOMT2 / (R,S)-Norcoclaurine: Km substrate 10 uM; kcat substrate 0.08 sec^-1; kcat/Km substrate 7.4 sec^-1 mM^-1.

substrate: (R,S)-Norcoclaurine


substrate_name: (S)-Norprotosinomenine

column_label: Row PSOMT2 / (S)-Norprotosinomenine; columns K m Substrate (uM), k cat Substrate (sec^-1), and k cat/Km Substrate (sec^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters of PSOMT1 and PSOMT2 for various substrates and co-substrate (AdoMet), row PSOMT2 / (S)-Norprotosinomenine: Km substrate 5 uM; kcat substrate 0.02 sec^-1; kcat/Km substrate 4 sec^-1 mM^-1.

row_label: PSOMT2 / (S)-Norprotosinomenine

substrate: (S)-Norprotosinomenine


organism: Arabidopsis thaliana

substrate_name: N-acetylserotonin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C296F with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

substrate: N-acetylserotonin