sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12530 and applied mutation signature L367E to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme characteristics of different mutants), row 'L367E'; column 'kcat, s^-1' = 2.2 +/- 0.2; column 'kcat/KM^S, s^-1 uM^-1' with the footnote '*S, linoleic acid.' = 0.26 +/- 0.06; column 'KM^O2, uM' = 9.0 +/- 2.1; column 'kcat/KM^O2, s^-1 uM^-1' = 0.24 +/- 0.06.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.2 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 2.2 s^(-1). Km: printed Table 1 cell 9.0 uM; 9.0 / 1000 = 0.009 mM; the exported value is 0.009 mM. kcat/Km: printed Table 1 cell 0.24 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.24 x 1000 = 240.0 s^-1 mM^-1. The quotient of the same row's two printed component cells is 2.2 / 0.009 = 244.44444444444449 s^-1 mM^-1, which is the exported catalytic efficiency; that quotient expressed in the printed unit is 0.2444444444444445 s^-1 uM^-1, and the printed cell 0.24 is that quotient rounded to the two decimals the table prints.

row_label: Table 1, row 'L367E'


enzyme_display_name: arachidonate 15-lipoxygenase

organism: Oryctolagus cuniculus

source_db: brenda

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12530 and applied mutation signature L367W to reconstruct the assayed variant sequence.

smiles: O=O

mutation_type: substitution

assay_conditions_summary: pH 7.4; buffer 13S-HpODE (2 uM) in 0.1 M potassium phosphate

column_label: Table 1 (Enzyme characteristics of different mutants), row 'L367W'; column 'kcat, s^-1' = 4.4 +/- 0.2; column 'kcat/KM^S, s^-1 uM^-1' with the footnote '*S, linoleic acid.' = 0.48 +/- 0.05; column 'KM^O2, uM' = 7.0 +/- 3.2; column 'kcat/KM^O2, s^-1 uM^-1' = 0.63 +/- 0.29.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.4 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 4.4 s^(-1). Km: printed Table 1 cell 7.0 uM; 7.0 / 1000 = 0.007 mM; the exported value is 0.007 mM. kcat/Km: printed Table 1 cell 0.63 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.63 x 1000 = 630.0 s^-1 mM^-1. The quotient of the same row's two printed component cells is 4.4 / 0.007 = 628.5714285714286 s^-1 mM^-1, which is the exported catalytic efficiency; that quotient expressed in the printed unit is 0.6285714285714286 s^-1 uM^-1, and the printed cell 0.63 is that quotient rounded to the two decimals the table prints.

row_label: Table 1, row 'L367W'

table_label: Table 1: Enzyme characteristics of different mutants (Proc Natl Acad Sci U S A 2007, 104(33):13319-13324)

data_origin: experimental

enzyme: arachidonate 15-lipoxygenase

status: verified

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12530 and applied mutation signature L367F to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme characteristics of different mutants), row 'L367F'; column 'kcat, s^-1' = 5.6 +/- 0.4; column 'kcat/KM^S, s^-1 uM^-1' with the footnote '*S, linoleic acid.' = 0.73 +/- 0.07; column 'KM^O2, uM' = 40.1 +/- 3.8; column 'kcat/KM^O2, s^-1 uM^-1' = 0.14 +/- 0.02.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.6 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 5.6 s^(-1). Km: printed Table 1 cell 40.1 uM; 40.1 / 1000 = 0.0401 mM; the exported value is 0.0401 mM. kcat/Km: printed Table 1 cell 0.14 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.14 x 1000 = 140.0 s^-1 mM^-1. The quotient of the same row's two printed component cells is 5.6 / 0.0401 = 139.6508728179551 s^-1 mM^-1, which is the exported catalytic efficiency; that quotient expressed in the printed unit is 0.1396508728179551 s^-1 uM^-1, and the printed cell 0.14 is that quotient rounded to the two decimals the table prints.

row_label: Table 1, row 'L367F'


mutation_signature: Unknown

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

column_label: Table 1 (Enzyme characteristics of different mutants), row 'WT'; column 'kcat, s^-1' = 13.7 +/- 0.4; column 'kcat/KM^S, s^-1 uM^-1' with the footnote '*S, linoleic acid.' = 0.74 +/- 0.08; column 'KM^O2, uM' = 5.2 +/- 2.4; column 'kcat/KM^O2, s^-1 uM^-1' = 2.63 +/- 1.22.

normalized_value_unit_evidence: kcat: printed Table 1 cell 13.7 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 13.7 s^(-1). Km: printed Table 1 cell 5.2 uM; 5.2 / 1000 = 0.0052 mM; the exported value is 0.0052 mM. kcat/Km: printed Table 1 cell 2.63 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.63 x 1000 = 2630.0 s^-1 mM^-1. The quotient of the same row's two printed component cells is 13.7 / 0.0052 = 2634.6153846153848 s^-1 mM^-1, which is the exported catalytic efficiency; that quotient expressed in the printed unit is 2.6346153846153846 s^-1 uM^-1, and the printed cell 2.63 is that quotient rounded to the two decimals the table prints.

row_label: Table 1, row 'WT'


enzyme_display_name: hydroxyquinol 1,2-dioxygenase

organism: Sporotrichum pulverulentum

substrate_name: Hydroxyquinol

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

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

enzyme: hydroxyquinol 1,2-dioxygenase

substrate: Hydroxyquinol

status: unverified


enzyme_display_name: arachidonate 12-lipoxygenase

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

proof_lines: pH 7.4, mutant L367K, with substrate linoleic acid

enzyme: arachidonate 12-lipoxygenase


proof_lines: pH 7.4, mutant L367E, with substrate linoleic acid


proof_lines: pH 7.4, mutant L367W, with substrate linoleic acid


proof_lines: pH 7.4, mutant L367F, with substrate linoleic acid


substrate_name: arachidonic acid

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R403L to reconstruct the assayed variant sequence.

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

substrate: arachidonic acid


substrate_name: methyl arachidonate

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

substrate: methyl arachidonate


substrate_name: linoleic acid

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

substrate: linoleic acid


enzyme_display_name: UniProt O15296

organism: Homo sapiens

substrate_name: arachidonate

source_db: skid

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

sequence_source: multiple

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

proof_lines: kcat is 2 sec(-1) for (5Z,8Z,11Z,14Z)-eicosatetraenoate. kcat is 2.1 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine. kcat is 2 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine. kcat is 2 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatet

source_databases_merged: skid uniprot

enzyme: UniProt O15296

substrate: arachidonate

source: skid


enzyme_display_name: Polyunsaturated fatty acid lipoxygenase ALOX15B

substrate_name: linoleate (isoform A at pH 7.4 and 20 degrees Celsius)

source_db: uniprot

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

source: uniprot


substrate_name: (5Z,8Z,11Z,14Z)-eicosatetraenoate (isoform A at pH 7.4 and 20 degrees Celsius)

smiles: CCC=CCC=CCC=CCC=CCCCCCCC(=O)[O-]

enzyme: Polyunsaturated fatty acid lipoxygenase ALOX15B


enzyme_display_name: Polyunsaturated fatty acid lipoxygenase ALOX15

proof_lines: kcat is 22.2 sec(-1) with (5Z,8Z,11Z,14Z)-eicosatetraenoate as substrate (PubMed:15123652). kcat is 1.34 sec(-1) with (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate as substrate (PubMed:15123652).


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

enzyme: Polyunsaturated fatty acid lipoxygenase ALOX15


proof_lines: kcat is 14.4 sec(-1) with (9Z,12Z)-octadecadienoate as substrate.


smiles: CCCCCC=CCC=CCC=CC=CC(CCCC(=O)[O-])O


smiles: CCCCCC=CCC=CCC=CC=CC(CCCC(=O)[O-])OO


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F353L to reconstruct the assayed variant sequence.


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


organism: Sus scrofa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M367V with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


substrate_name: anandamide (Sf9-expressed enzyme)

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

substrate: anandamide (Sf9-expressed enzyme)


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


organism: Pseudomonas aeruginosa

kcat_over_km_origin: calculated

proof_lines: pH 6.5, 22°C, recombinant His6-tagged enzyme

source_databases_merged: brenda skid


proof_lines: pH 7.5, 22°C, recombinant His6-tagged enzyme

proof_lines: pH 7.0, 22°C, recombinant His6-tagged enzyme


assay_conditions_summary: buffer HEPES

source_databases_merged: brenda uniprot


enzyme_display_name: UniProt Q5PXQ6

organism: Pimelobacter simplex

proof_lines: 5-chlorohydroxyquinols and 6-chloro-chlorohydroxyquinols are also substrates.

enzyme: UniProt Q5PXQ6


enzyme_display_name: arachidonate 5-lipoxygenase

assay_conditions_summary: pH 7.5; 294.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, HPLC analysis, 8-HETE formation

proof_lines: pH 7.5, 25°C, UV?Vis spectrophotometric analysis

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: arachidonate 5-lipoxygenase


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

proof_lines: pH 7.5, 21°C, recombinant enzyme, with 0.2 mM ATP


substrate_name: O2; Arachidonate

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

substrate: O2; Arachidonate


substrate_name: Linoleate; O2

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

source_databases_merged: sabio_rk skid uniprot

substrate: Linoleate; O2


substrate_name: Arachidonate; O2

substrate: Arachidonate; O2


sequence_variant_note: Mutation signature L353L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Polyunsaturated fatty acid lipoxygenase ALOX12

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row pl12-LO / Arachidonic acid; Km 9.5 +/- 0.7 uM; normalized km 0.0095 mM; enzyme label: human platelet-type 12-LO

row_label: pl12-LO / Arachidonic acid


substrate_name: N-arachidonoylglycine

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

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row pl12-LO / N-Arachidonyl glycine; Km 10.1 +/- 0.8 uM; normalized km 0.0101 mM; enzyme label: human platelet-type 12-LO

row_label: pl12-LO / N-Arachidonyl glycine

enzyme: Polyunsaturated fatty acid lipoxygenase ALOX12

substrate: N-arachidonoylglycine


substrate_name: N-arachidonoyl-L-alanine

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

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row pl12-LO / N-Arachidonyl alanine; Km 15.7 +/- 0.8 uM; normalized km 0.0157 mM; enzyme label: human platelet-type 12-LO

row_label: pl12-LO / N-Arachidonyl alanine

substrate: N-arachidonoyl-L-alanine


substrate_name: N-arachidonoyl-gamma-aminobutyric acid

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

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row pl12-LO / N-Arachidonyl-gamma-aminobutyric acid; Km 10.9 +/- 0.5 uM; normalized km 0.0109 mM; enzyme label: human platelet-type 12-LO

substrate: N-arachidonoyl-gamma-aminobutyric acid


substrate_name: 1-linoleoyl lysophosphatidic acid

source_databases_merged: brenda skid uniprot

substrate: 1-linoleoyl lysophosphatidic acid


proof_lines: pH 7.5, 25°C, UV-Vis spectrophotometric analysis

source_databases_merged: sabio_rk brenda uniprot


organism: Nocardioides simplex

substrate_name: Benzene-1,2,4-triol; O2

substrate: Benzene-1,2,4-triol; O2


verification_status: corrected

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row h15-LO-2 / N-Arachidonyl glycine; Km 11.0 +/- 0.4 uM; normalized km 0.011 mM; enzyme label: human 15-LO-2

row_label: h15-LO-2 / N-Arachidonyl glycine

status: corrected


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row h15-LO-2 / N-Arachidonyl alanine; Km 6 +/- 3 uM; normalized km 0.006 mM; enzyme label: human 15-LO-2

row_label: h15-LO-2 / N-Arachidonyl alanine


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row h15-LO-2 / N-Arachidonyl-gamma-aminobutyric acid; Km 8 +/- 2 uM; normalized km 0.008 mM; enzyme label: human 15-LO-2


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row lk12-LO / Arachidonic acid; Km 7.8 +/- 1.3 uM; normalized km 0.0078 mM; enzyme label: porcine leukocyte-type 12-LO

row_label: lk12-LO / Arachidonic acid


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row lk12-LO / N-Arachidonyl glycine; Km 8.0 +/- 0.7 uM; normalized km 0.008 mM; enzyme label: porcine leukocyte-type 12-LO

row_label: lk12-LO / N-Arachidonyl glycine


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row lk12-LO / N-Arachidonyl-gamma-aminobutyric acid; Km 7.8 +/- 0.7 uM; normalized km 0.0078 mM; enzyme label: porcine leukocyte-type 12-LO


organism: Rhodococcus sp

substrate_name: catechol (at pH 8.1 and 8 degrees Celsius)

proof_lines:
Rhodococcus ohp operon
catechol


substrate_name: 3-methylcatechol (at pH 8.1 and 8 degrees Celsius)


enzyme_display_name: cysteamine dioxygenase

substrate_name: cysteamine

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

smiles: C(CS)N

enzyme: cysteamine dioxygenase

substrate: cysteamine


smiles: O=O


source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L183E/L187E to reconstruct the assayed variant sequence.

smiles: CCCCC/C=C\C/C=C\C/C=C\C/C=C\CCCC(=O)O

source: oed


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

assay_conditions_summary: pH 7.4; buffer HEPES

column_label: Results prose/Table 1 reports linoleic acid Km 12.1 microM and Vm 545 units/mg protein for reticulocyte LOX.

raw_value_unit_evidence: Km raw_value=12.1 microM raw_unit=microM

row_label: rabbit reticulocyte lipoxygenase / linoleic acid

table_label: ScienceDirect full text Table 1 / Results prose


substrate_name: dilinoleoyl phosphatidylcholine

substrate: dilinoleoyl phosphatidylcholine


enzyme_display_name: UniProt O32085

organism: Bacillus subtilis

substrate_name: L-cysteine

km_display: Not reported

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

column_label: Table 1 columns CDO construct, pH optimum, Cysteine Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row YubC.

normalized_value_unit_evidence: kcat 0.39 s^-1; Km 3.0 mM; printed kcat/Km 0.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row YubC: Cysteine Km 3.0 mM; kcat 0.39 s^-1; kcat/Km 0.1 mM^-1 s^-1.

row_label: YubC (Bacillus subtilis CDO homolog)

table_label: Table 1, comparison of molecular properties and kinetic parameters of purified eukaryotic and bacterial CDOs

enzyme: UniProt O32085

substrate: L-cysteine


substrate_name: cysteine

substrate: cysteine


enzyme_display_name: cysteine dioxygenase

substrate_name: L-Cysteine

enzyme: cysteine dioxygenase

substrate: L-Cysteine


substrate_name: eicosa-5,8,11,14,17-pentaenoate (at pH 7.0 and 37 degrees Celsius)

assay_conditions_summary: pH 7


enzyme_display_name: pyrogallol 1,2-oxygenase

substrate_name: 1,2,3-Trihydroxybenzene; O2

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

enzyme: pyrogallol 1,2-oxygenase

substrate: 1,2,3-Trihydroxybenzene; O2


organism: Streptomyces coelicolor

column_label: Table 1 columns CDO construct, pH optimum, Cysteine Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row SCO5772.

normalized_value_unit_evidence: kcat 0.30 s^-1; Km 3.8 mM; printed kcat/Km 0.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row SCO5772: Cysteine Km 3.8 mM; kcat 0.30 s^-1; kcat/Km 0.1 mM^-1 s^-1.

row_label: SCO5772 (Streptomyces coelicolor A3(2) CDO homolog)


column_label: Table 1 columns CDO construct, pH optimum, Cysteine Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row SCO3035.

normalized_value_unit_evidence: kcat 0.33 s^-1; Km 1.2 mM; printed kcat/Km 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row SCO3035: Cysteine Km 1.2 mM; kcat 0.33 s^-1; kcat/Km 0.3 mM^-1 s^-1.

row_label: SCO3035 (Streptomyces coelicolor A3(2) CDO homolog)


substrate_name: linoleate

smiles: CCCCC/C=C\C/C=C\CCCCCCCC(=O)O

proof_lines:
11-thialinoleic acid
human reticulocyte 15-lipoxygenase-1
linoleic acid

substrate: linoleate


substrate_name: arachidonate

proof_lines:
human 12-lipoxygenase
human 15-lipoxygenase-1
human 15-lipoxygenase-2

substrate: arachidonate


enzyme_display_name: UniProt P32440

organism: Methanothermobacter marburgensis

enzyme: UniProt P32440


substrate_name: linoleic acid

substrate: linoleic acid


enzyme_display_name: catechol 1,2-dioxygenase

organism: Corynebacterium glutamicum

substrate_name: catechol

column_label: Abstract reports Km and Vmax were 4.24 micromol l(-1) and 3.7 micromol l(-1) min(-1) mg(-1).

raw_value_unit_evidence: Km raw_value=4.24 micromol l(-1) raw_unit=microM

row_label: Catechol 1,2-dioxygenase / catechol

table_label: PubMed XML abstract PMID 15168857

enzyme: catechol 1,2-dioxygenase

substrate: catechol


organism: Stenotrophomonas maltophilia

assay_conditions_summary: pH 8


organism: Cupriavidus campinensis


enzyme_display_name: 2-aminoethanethiol dioxygenase

organism: Mus musculus

assay_conditions_summary: pH 8; buffer 50 mM Tris borate

column_label: Official ScienceDirect article page, Figure 4D legend and Results paragraph, cysteamine concentration-dependence assay at pH 8.0, reports Km = 3.8 mM for ADO protein.

normalized_value_unit_evidence: Paper Figure 4D/Results Km is 3.8 mM, matching the export Km 3.8 mM.

raw_value_unit_evidence: Figure 4D legend and Results paragraph report Km = 3.8 mM for cysteamine dioxygenase activity of ADO.

row_label: wild-type ADO with cysteamine at pH 8.0

table_label: Figure 4. Kinetic analyses of purified wild-type ADO protein

enzyme: 2-aminoethanethiol dioxygenase


enzyme_display_name: persulfide dioxygenase

organism: Acidithiobacillus caldus

substrate_name: glutathione

enzyme: persulfide dioxygenase

substrate: glutathione


enzyme_display_name: UniProt O31266

organism: Paenarthrobacter nitroguajacolicus

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=5°C, pH=6.5
Raw SKiD Env: Temp=5°C, pH=10.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt O31266


enzyme_display_name: UniProt B3U4H7

organism: Nitrospira defluvii

substrate_name: Chlorite

smiles: [O-]Cl=O

enzyme: UniProt B3U4H7

substrate: Chlorite


enzyme_display_name: UniProt B8HNS6

organism: Cyanothece sp. PCC 7425

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=25°C, pH=5

enzyme: UniProt B8HNS6


enzyme_display_name: UniProt Q8PDA8

organism: Xanthomonas campestris

enzyme: UniProt Q8PDA8


substrate_name: L-tryptophan

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

substrate: L-tryptophan


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


organism: Bacillus cereus

column_label: Table 1 columns CDO construct, pH optimum, Cysteine Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row BC2617.

normalized_value_unit_evidence: kcat 2.0 s^-1; Km 5.7 mM; printed kcat/Km 0.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row BC2617: Cysteine Km 5.7 mM; kcat 2.0 s^-1; kcat/Km 0.4 mM^-1 s^-1.

row_label: BC2617 (Bacillus cereus ATCC 14579 CDO homolog)


organism: Homo sapiens

substrate_name: S-carboxymethyl-L-cysteine

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

proof_lines:
human hepatic cytosol
S-oxidations
l-Cysteine

substrate: S-carboxymethyl-L-cysteine


organism: Pseudomonas aeruginosa

smiles: O=C([O-])CCS


enzyme_display_name: indoleamine 2,3-dioxygenase

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

proof_lines: H55A mutant enzyme, O2 not present at a saturating level

enzyme: indoleamine 2,3-dioxygenase


proof_lines: H55S mutant enzyme, O2 not present at a saturating level


proof_lines: pH and temperature not specified in the publication


substrate_name: L-Trp

substrate: L-Trp


enzyme_display_name: 4-hydroxymandelate synthase

substrate_name: 4-nitrophenylpyruvic acid

enzyme: 4-hydroxymandelate synthase

substrate: 4-nitrophenylpyruvic acid


substrate_name: 2-oxo-4-phenylbutanoic acid

substrate: 2-oxo-4-phenylbutanoic acid


substrate_name: phenylpyruvic acid

substrate: phenylpyruvic acid


organism: Blepharisma stoltei

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme H127E


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


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme N127T


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme E132H


proof_lines: HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication


proof_lines: HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication


proof_lines: HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication


proof_lines: HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication


proof_lines: HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication


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


enzyme_display_name: chlorite O2-lyase

proof_lines:
mutant enzyme Q74E, at pH 9.0 and 30°C
mutant enzyme Q74E, at pH 7.0 and 30°C
mutant enzyme Q74E, at pH 5.0 and 30°C

enzyme: chlorite O2-lyase


proof_lines:
wild type enzyme, at pH 9.0 and 30°C
wild type enzyme, at pH 7.0 and 30°C
wild type enzyme, at pH 5.0 and 30°C


proof_lines:
mutant enzyme Q74V, at pH 9.0 and 30°C
mutant enzyme Q74V, at pH 7.0 and 30°C
mutant enzyme Q74V, at pH 5.0 and 30°C


enzyme_display_name: UniProt A0A0M3KL46

organism: Magnetospirillum sp.

proof_lines:
Raw SKiD Env: Temp=10°C, pH=6.5
Raw SKiD Env: Temp=10°C, pH=6
Raw SKiD Env: Temp=10°C, pH=5.5

enzyme: UniProt A0A0M3KL46


substrate_name: D-tryptophan

substrate: D-tryptophan


organism: Paenarthrobacter ilicis


proof_lines: 30°C, pH 8.0, with 3-hydroxy-2-methyl-1H-quinolin-4-one


organism: Micromonospora sp.


substrate_name: serotonin

substrate: serotonin


substrate_name: indole

substrate: indole


organism: Arabidopsis thaliana

substrate_name: 3-(4-Hydroxyphenyl)pyruvate; O2

substrate: 3-(4-Hydroxyphenyl)pyruvate; O2


organism: Azospira oryzae

substrate_name: chloride

substrate: chloride


organism: Dechloromonas agitata


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Pseudomonas fluorescens


organism: Klebsiella pneumoniae


organism: Nitrobacter winogradskyi


organism: Anopheles gambiae


organism: Branchiostoma floridae


organism: Brevibacillus brevis


organism: Cyanothece sp. PCC 7425


organism: Delftia acidovorans

proof_lines:
pH 7.0
activated by 0.033 mM Cd2+


organism: Gallus gallus

substrate_name: O2; L-Tryptophan

substrate: O2; L-Tryptophan


organism: Meriones unguiculatus

proof_lines:
indoleamine 2,3-dioxygenase
pH 6.5, 37°C


organism: Monosiga brevicollis


organism: Haliotis diversicolor


organism: Mus musculus

assay_conditions_summary: pH 7.4; 310.15 K; buffer 100 mM phosphate; cofactor NADPH

proof_lines: IDO2, pH and temperature not specified in the publication


organism: Pelodiscus sinensis japonicus


organism: Streptomyces parvulus


assay_conditions_summary: pH 7.5; 310.15 K; buffer 100 mM phosphate; cofactor NADPH

proof_lines:
pH 7.5, 37°C, 5 min incubation time
pH 6.5, 37°C
37°C, pH 6.5


organism: Nematostella vectensis


organism: Paenarthrobacter nitroguajacolicus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E224A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196K with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196K/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant Y196K/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196R with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196R/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant Y196R/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196A/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant Y196A/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S101A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S101A/C69S with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant S101A/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H102Q with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H102Q/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant H102Q/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S220N with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S220N/C69S with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant S220N/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F219Y with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F219Y/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant F219Y/C69S


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C69S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E224A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E224A/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant E224A/C69S


organism: Amycolatopsis orientalis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T214P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I216N with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S201A to reconstruct the assayed variant sequence.


enzyme_display_name: acetylacetone-cleaving enzyme

organism: Acinetobacter johnsonii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y70F to reconstruct the assayed variant sequence.

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

enzyme: acetylacetone-cleaving enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F59A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F115A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F119A to reconstruct the assayed variant sequence.


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


assay_conditions_summary: pH 7.5; buffer 20 mM Tris/HCl

proof_lines: wild type enzyme, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y70A/R80A/E98A to reconstruct the assayed variant sequence.

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

proof_lines: pH 7.5, 25°C, recombinant mutant Y70A/R80A/E98A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y70F/R80A/E98A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant Y70F/R80A/E98A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E98Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E98A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80A/E98A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant R80A/E98A


sequence_variant_note: Mutation signature T107A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y70A to reconstruct the assayed variant sequence.


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

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


organism: Nitrospira defluvii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R137A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R137K with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt P14902

organism: Homo sapiens

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

proof_lines: Catalytic efficiency for L-tryptophan is 150 times higher than for D-tryptophan.

enzyme: UniProt P14902


enzyme_display_name: Indoleamine 2,3-dioxygenase 1

proof_lines: Catalytic efficiency for L-tryptophan is 90 times higher than for D-tryptophan.

enzyme: Indoleamine 2,3-dioxygenase 1


organism: Oryctolagus cuniculus

substrate_name: D-Trp

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

assay_conditions_summary: pH 6

substrate: D-Trp


smiles: CCCC(=O)C(=CO)O

proof_lines:
Co2+ bound enzyme, pH 7.0, 25°C
Ni2+ bound enzyme, pH 7.0, 25°C


organism: Pseudomonas putida

substrate_name: O2; 3-Hydroxy-1H-quinolin-4-one

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

substrate: O2; 3-Hydroxy-1H-quinolin-4-one


organism: Anolis carolinensis

substrate_name: L-Tryptophan; O2

substrate: L-Tryptophan; O2


organism: Aspergillus oryzae

assay_conditions_summary: pH 6.5; 310.15 K; buffer 500 ul of 50 mM potassium phosphate

column_label: Table 1: Kinetic parameters of bacterially-expressed fungal IDOs (J Mol Evol 2011, volume 72, pages 160-168); printed column heads enzyme form | pH | L-Trp VmaxTON (min^-1) | L-Trp Km | L-Trp VmaxTON/Km (uM^-1/min) | D-Trp VmaxTON (min^-1) | D-Trp Km (mM) | D-Trp VmaxTON/Km (uM^-1/min); the table footnote defines TON as turnover number (mol of product/mol of holoenzyme/min). Table 1, enzyme-form row A. oryzae IDOa at pH 6.5, L-Trp column group; column VmaxTON (min^-1) = 50.4; column Km (uM) = 154; column VmaxTON/Km (uM^-1/min) = 0.3. captured primary segment: A. oryzae IDOa | L-Trp | kcat (VmaxTON) 50.4 min^-1 | Km 154 uM | kcat/Km (VmaxTON/Km) 0.3 uM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 154 uM; 1 uM is 0.001 mM, so 154 / 1000 = 0.154 mM; the exported value is 0.154 mM. kcat: printed Table 1 cell 50.4 min^-1; 1 min^-1 is 1/60 s^-1, so 50.4 / 60 = 0.84 s^(-1); the exported value is 0.84 s^(-1). kcat/Km: printed Table 1 cell 0.3 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.3 x 1000 / 60 = 5.0 s^(-1)*mM^(-1). The live export row carries no catalytic-efficiency field, so this pass exports none; the printed cell is transcribed in the typed kcat_over_km_provenance only.

raw_value_unit_evidence: Table 1, enzyme-form row A. oryzae IDOa at pH 6.5, L-Trp column group: Km = 154 uM; kcat (printed VmaxTON) = 50.4 min^-1; printed kcat/Km (printed VmaxTON/Km) = 0.3 uM^-1 min^-1.


organism: Branchiostoma floridae


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E69Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E69Q, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C


proof_lines: native enzyme, using 0.09 mM 1,1,1-trifluoro-pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C


proof_lines:
apparent value at 25°C
Strep-tagged enzyme
recombinant enzyme


organism: Ornithorhynchus anatinus


organism: Danio rerio


organism: Monodelphis domestica


organism: Monosiga brevicollis


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D120A to reconstruct the assayed variant sequence.

proof_lines: QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication


organism: Dechloromonas aromatica (nom. nud.)

substrate_name: Chlorite

proof_lines: kcat is 4.53 min(-1) with chlorite as substrate.

substrate: Chlorite


enzyme_display_name: Chlorite dismutase

organism: Ideonella dechloratans

enzyme: Chlorite dismutase


organism: Stutzerimonas chloritidismutans

proof_lines: 100 mM sodium phosphate buffer, pH 6.0, 25°C


organism: Oryzias latipes


organism: Saccharomyces cerevisiae


organism: Sulculus diversicolor


organism: Xenopus laevis


organism: Klebsiella oxytoca

substrate_name: O2; 1,2-Dihydroxyhex-1-en-3-one

column_label: Table 3 columns are ARD and ARD'. In the ARD column, KmII (uM)=50 and kcat (s^-1)=5.0 x 10^2; Figure 1 caption identifies ARD (Ni2+) initial velocity versus II at constant O2.

normalized_value_unit_evidence: KmII normalized_value=0.05 normalized_unit=mM; kcat normalized_value=500 normalized_unit=s^-1

raw_value_unit_evidence: KmII raw_value=50 raw_unit=uM; kcat raw_value=5.0 x 10^2 raw_unit=s^-1

row_label: ARD column; KmII row and kcat row

table_label: ACS PDF page 5 / journal page 6383, Table 3: Kinetic Constants of ARD and ARD'

substrate: O2; 1,2-Dihydroxyhex-1-en-3-one


organism: Oryza sativa

substrate_name: 1,2-Dihydroxy-3-ketopent-1-ene; O2

substrate: 1,2-Dihydroxy-3-ketopent-1-ene; O2


organism: Acinetobacter johnsonii


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase

organism: Vigna unguiculata

enzyme: 9-cis-epoxycarotenoid dioxygenase


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase 1, chloroplastic

organism: Zea mays

substrate_name: 9-cis antheraxanthin

proof_lines: Vmax with 9-cis violaxanthin as substrate is more than twice the Vmax with 9-cis neoxanthin as substrate.

substrate: 9-cis antheraxanthin


enzyme_display_name: Acireductone dioxygenase

organism: Mus musculus

substrate_name: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one (using iron as cofactor)

proof_lines: kcat is 114.3 sec(-1) with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using iron as cofactor) (PubMed:26858196). kcat is 7.55 sec(-1) with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using cobalt as cofa

enzyme: Acireductone dioxygenase


substrate_name: 9-cis violaxanthin

column_label: ScienceDirect HTML, Table 1, row 9cViol, column Km (uM).

raw_value_unit_evidence: Table 1 9cViol Km (uM): 58 uM

table_label: Table 1

enzyme: 9-cis-epoxycarotenoid dioxygenase 1, chloroplastic

substrate: 9-cis violaxanthin


organism: Homo sapiens

column_label: Table 3 (journal page 2161), row 'IDO1, 1-Me-D-Trp': column 'kcat (s-1)' = 0.095; column 'Km (lM)' = 660; the table prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.095 s^-1 needs no conversion and is the exported 0.095 s^(-1). Km: printed Table 3 cell 660 uM divided by 1000 is 0.66 mM. kcat/Km: Table 3 prints no ratio cell for this row, so the ratio is the exact quotient of the same row's two printed cells, 0.095 / 0.66 = 0.14393939393939392 s^-1 mM^-1.

raw_value_unit_evidence: The reviewed primary row is in Table 3, journal page 2161. The printed enzyme/substrate row is IDO1, 1-Me-D-Trp. The assay enzyme is recombinant human IDO1. The varied substrate is 1-Me-D-Trp. The Table 3 assay condition is 100 mM KPi pH 6.5, 25 C, aerobic. Table 3, IDO1, 1-Me-D-Trp: kcat 0.095 s^-1. Table 3, IDO1, 1-Me-D-Trp: Km 660 uM. Table 3 prints kcat and Km only for IDO1, 1-Me-D-Trp and carries no catalytic-efficiency column, so this paper prints no ratio cell for that row.

row_label: IDO1, 1-Me-D-Trp

table_label: Table 3: kinetic parameters, journal page 2161


proof_lines:
indoleamine 2,3-dioxygenase-2
substrate specificity
tryptophan derivatives


column_label: Table 1 (journal page 2158), row 'IDO2, 5-F-D,L-Trp': column 'kcat (s-1)' = 0.049; column 'Km (lM)' = 1768; column 'kcat/Km (M-1s-1)' = 28.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.049 s^-1 needs no conversion and is the exported 0.049 s^(-1). Km: printed Table 1 cell 1768 uM divided by 1000 is 1.768 mM. kcat/Km: printed Table 1 cell 28 M^-1 s^-1 multiplied by 0.001 is 0.028 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.049 / 1.768, is 0.027714932126696835 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 5-F-D,L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 5-F-D,L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 5-F-D,L-Trp: kcat 0.049 s^-1. Table 1, IDO2, 5-F-D,L-Trp: Km 1768 uM. Table 1, IDO2, 5-F-D,L-Trp: printed kcat/Km 28 M^-1 s^-1.

row_label: IDO2, 5-F-D,L-Trp

table_label: Table 1: kinetic parameters, journal page 2158


column_label: Table 1 (journal page 2158), row 'IDO2, 5-MeO-D,L-Trp': column 'kcat (s-1)' = 0.161; column 'Km (lM)' = 547; column 'kcat/Km (M-1s-1)' = 294.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.161 s^-1 needs no conversion and is the exported 0.161 s^(-1). Km: printed Table 1 cell 547 uM divided by 1000 is 0.547 mM. kcat/Km: printed Table 1 cell 294 M^-1 s^-1 multiplied by 0.001 is 0.294 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.161 / 0.547, is 0.29433272394881166 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 5-MeO-D,L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 5-MeO-D,L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 5-MeO-D,L-Trp: kcat 0.161 s^-1. Table 1, IDO2, 5-MeO-D,L-Trp: Km 547 uM. Table 1, IDO2, 5-MeO-D,L-Trp: printed kcat/Km 294 M^-1 s^-1.

row_label: IDO2, 5-MeO-D,L-Trp


column_label: Table 1 (journal page 2158), row 'IDO2, 5-Me-D,L-Trp': column 'kcat (s-1)' = 0.36; column 'Km (lM)' = 1570; column 'kcat/Km (M-1s-1)' = 229.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.36 s^-1 needs no conversion and is the exported 0.36 s^(-1). Km: printed Table 1 cell 1570 uM divided by 1000 is 1.57 mM. kcat/Km: printed Table 1 cell 229 M^-1 s^-1 multiplied by 0.001 is 0.229 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.36 / 1.57, is 0.22929936305732482 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 5-Me-D,L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 5-Me-D,L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 5-Me-D,L-Trp: kcat 0.36 s^-1. Table 1, IDO2, 5-Me-D,L-Trp: Km 1570 uM. Table 1, IDO2, 5-Me-D,L-Trp: printed kcat/Km 229 M^-1 s^-1.

row_label: IDO2, 5-Me-D,L-Trp


column_label: Table 1 (journal page 2158), row 'IDO2, 6-Me-D,L-Trp': column 'kcat (s-1)' = 0.108; column 'Km (lM)' = 3457; column 'kcat/Km (M-1s-1)' = 31.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.108 s^-1 needs no conversion and is the exported 0.108 s^(-1). Km: printed Table 1 cell 3457 uM divided by 1000 is 3.457 mM. kcat/Km: printed Table 1 cell 31 M^-1 s^-1 multiplied by 0.001 is 0.031 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.108 / 3.457, is 0.031240960370263235 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 6-Me-D,L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 6-Me-D,L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 6-Me-D,L-Trp: kcat 0.108 s^-1. Table 1, IDO2, 6-Me-D,L-Trp: Km 3457 uM. Table 1, IDO2, 6-Me-D,L-Trp: printed kcat/Km 31 M^-1 s^-1.

row_label: IDO2, 6-Me-D,L-Trp


substrate_name: D-Tryptophan

substrate: D-Tryptophan


column_label: Table 1 (journal page 2158), row 'IDO2, 1-Me-L-Trp': column 'kcat (s-1)' = 0.011; column 'Km (lM)' = 696; column 'kcat/Km (M-1s-1)' = 16.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.011 s^-1 needs no conversion and is the exported 0.011 s^(-1). Km: printed Table 1 cell 696 uM divided by 1000 is 0.696 mM. kcat/Km: printed Table 1 cell 16 M^-1 s^-1 multiplied by 0.001 is 0.016 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.011 / 0.696, is 0.015804597701149427 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 1-Me-L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 1-Me-L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 1-Me-L-Trp: kcat 0.011 s^-1. Table 1, IDO2, 1-Me-L-Trp: Km 696 uM. Table 1, IDO2, 1-Me-L-Trp: printed kcat/Km 16 M^-1 s^-1.

row_label: IDO2, 1-Me-L-Trp


substrate_name: L-Tryptophan

column_label: Table 1 (journal page 2158), row 'IDO2, L-Trp': column 'kcat (s-1)' = 0.103; column 'Km (lM)' = 6809; column 'kcat/Km (M-1s-1)' = 15.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.103 s^-1 needs no conversion and is the exported 0.103 s^(-1). Km: printed Table 1 cell 6809 uM divided by 1000 is 6.809 mM. kcat/Km: printed Table 1 cell 15 M^-1 s^-1 multiplied by 0.001 is 0.015 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.103 / 6.809, is 0.015127037744162138 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, L-Trp: kcat 0.103 s^-1. Table 1, IDO2, L-Trp: Km 6809 uM. Table 1, IDO2, L-Trp: printed kcat/Km 15 M^-1 s^-1.

row_label: IDO2, L-Trp

substrate: L-Tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14902 and applied mutation signature F163A to reconstruct the assayed variant sequence.

column_label: Table 1 (Summary of Reduction Potentials and Steady-State and Presteady-State Constants for hIDO and Site-Directed Variants), site-directed variant row 'F163A'; column 'kcat (s-1)' = 0.040 ± 0.002; column 'KM (uM)' = 68 ± 6; Table 1 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.040 s-1; already in s^-1, no unit conversion applies; the paper value is 0.04 s^(-1). Km: printed Table 1 cell 68 uM; 68 / 1000 = 0.068 mM; the paper value is 0.068 mM. kcat/Km: Table 1 carries no kcat/KM column, so the paper value 0.5882352941176471 s^(-1)*mM^(-1) is not a printed cell; it is the quotient of this row's own two printed cells in canonical units, 0.04 / 0.068 = 0.5882352941176471, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, site-directed variant row 'F163A': column 'kcat (s-1)' = 0.040 ± 0.002; column 'KM (uM)' = 68 ± 6; Table 1 prints no kcat/KM cell for this row.

table_label: Table 1: Summary of Reduction Potentials and Steady-State and Presteady-State Constants for hIDO and Site-Directed Variants (J. Am. Chem. Soc. 2012, 134(6):3034-3041)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14902 and applied mutation signature F164A to reconstruct the assayed variant sequence.

column_label: Table 1 (Summary of Reduction Potentials and Steady-State and Presteady-State Constants for hIDO and Site-Directed Variants), site-directed variant row 'F164A'; column 'kcat (s-1)' = 0.68 ± 0.03; column 'KM (uM)' = 160 ± 10; Table 1 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.68 s-1; already in s^-1, no unit conversion applies; the paper value is 0.68 s^(-1). Km: printed Table 1 cell 160 uM; 160 / 1000 = 0.16 mM; the paper value is 0.16 mM. kcat/Km: Table 1 carries no kcat/KM column, so the paper value 4.25 s^(-1)*mM^(-1) is not a printed cell; it is the quotient of this row's own two printed cells in canonical units, 0.68 / 0.16 = 4.25, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, site-directed variant row 'F164A': column 'kcat (s-1)' = 0.68 ± 0.03; column 'KM (uM)' = 160 ± 10; Table 1 prints no kcat/KM cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14902 and applied mutation signature F226A to reconstruct the assayed variant sequence.

column_label: Table 1 (Summary of Reduction Potentials and Steady-State and Presteady-State Constants for hIDO and Site-Directed Variants), site-directed variant row 'F226A'; column 'kcat (s-1)' = 0.12 ± 0.01; column 'KM (uM)' = 310 ± 20; Table 1 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.12 s-1; already in s^-1, no unit conversion applies; the paper value is 0.12 s^(-1). Km: printed Table 1 cell 310 uM; 310 / 1000 = 0.31 mM; the paper value is 0.31 mM. kcat/Km: Table 1 carries no kcat/KM column, so the paper value 0.3870967741935484 s^(-1)*mM^(-1) is not a printed cell; it is the quotient of this row's own two printed cells in canonical units, 0.12 / 0.31 = 0.3870967741935484, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, site-directed variant row 'F226A': column 'kcat (s-1)' = 0.12 ± 0.01; column 'KM (uM)' = 310 ± 20; Table 1 prints no kcat/KM cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14902 and applied mutation signature F226Y to reconstruct the assayed variant sequence.

column_label: Table 1 (Summary of Reduction Potentials and Steady-State and Presteady-State Constants for hIDO and Site-Directed Variants), site-directed variant row 'F226Y'; column 'kcat (s-1)' = 6.0 ± 0.3; column 'KM (uM)' = 160 ± 10; Table 1 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.0 s-1; already in s^-1, no unit conversion applies; the paper value is 6.0 s^(-1). Km: printed Table 1 cell 160 uM; 160 / 1000 = 0.16 mM; the paper value is 0.16 mM. kcat/Km: Table 1 carries no kcat/KM column, so the paper value 37.5 s^(-1)*mM^(-1) is not a printed cell; it is the quotient of this row's own two printed cells in canonical units, 6.0 / 0.16 = 37.5, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, site-directed variant row 'F226Y': column 'kcat (s-1)' = 6.0 ± 0.3; column 'KM (uM)' = 160 ± 10; Table 1 prints no kcat/KM cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14902 and applied mutation signature F227A to reconstruct the assayed variant sequence.

column_label: Table 1 (Summary of Reduction Potentials and Steady-State and Presteady-State Constants for hIDO and Site-Directed Variants), site-directed variant row 'F227A'; column 'kcat (s-1)' = 0.40 ± 0.02; column 'KM (uM)' = 15 ± 2; Table 1 carries no kcat/KM column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.40 s-1; already in s^-1, no unit conversion applies; the paper value is 0.4 s^(-1). Km: printed Table 1 cell 15 uM; 15 / 1000 = 0.015 mM; the paper value is 0.015 mM. kcat/Km: Table 1 carries no kcat/KM column, so the paper value 26.666666666666668 s^(-1)*mM^(-1) is not a printed cell; it is the quotient of this row's own two printed cells in canonical units, 0.4 / 0.015 = 26.666666666666668, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, site-directed variant row 'F227A': column 'kcat (s-1)' = 0.40 ± 0.02; column 'KM (uM)' = 15 ± 2; Table 1 prints no kcat/KM cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S167A to reconstruct the assayed variant sequence.


organism: Aspergillus oryzae

column_label: Table 1: Kinetic parameters of bacterially-expressed fungal IDOs (J Mol Evol 2011, volume 72, pages 160-168); printed column heads enzyme form | pH | L-Trp VmaxTON (min^-1) | L-Trp Km | L-Trp VmaxTON/Km (uM^-1/min) | D-Trp VmaxTON (min^-1) | D-Trp Km (mM) | D-Trp VmaxTON/Km (uM^-1/min); the table footnote defines TON as turnover number (mol of product/mol of holoenzyme/min). Table 1, enzyme-form row A. oryzae IDOa at pH 6.5, D-Trp column group; column VmaxTON (min^-1) = 21.9; column Km (mM) = 5.8; column VmaxTON/Km (uM^-1/min) = 3.8 x 10^-3. captured primary segment: A. oryzae IDOa | D-Trp | kcat (VmaxTON) 21.9 min^-1 | Km 5.8 mM | kcat/Km (VmaxTON/Km) 3.8 x 10^-3 uM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 5.8 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 5.8 mM; the exported value is 5.8 mM. kcat: printed Table 1 cell 21.9 min^-1; 1 min^-1 is 1/60 s^-1, so 21.9 / 60 = 0.365 s^(-1); the exported value is 0.365 s^(-1). kcat/Km: printed Table 1 cell 3.8 x 10^-3 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 3.8 x 10^-3 x 1000 / 60 = 0.06333333333333334 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.365 / 5.8 = 0.06293103448275862 s^-1 mM^-1, the exported value, and 21.9 / 5.8 mM = 0.003776 uM^-1 min^-1 rounds to the printed catalytic-efficiency cell 3.8 x 10^-3 uM^-1 min^-1.

raw_value_unit_evidence: Table 1, enzyme-form row A. oryzae IDOa at pH 6.5, D-Trp column group: Km = 5.8 mM; kcat (printed VmaxTON) = 21.9 min^-1; printed kcat/Km (printed VmaxTON/Km) = 3.8 x 10^-3 uM^-1 min^-1.


assay_conditions_summary: pH 7.5; 310.15 K; buffer 500 ul of 50 mM potassium phosphate

column_label: Table 1: Kinetic parameters of bacterially-expressed fungal IDOs (J Mol Evol 2011, volume 72, pages 160-168); printed column heads enzyme form | pH | L-Trp VmaxTON (min^-1) | L-Trp Km | L-Trp VmaxTON/Km (uM^-1/min) | D-Trp VmaxTON (min^-1) | D-Trp Km (mM) | D-Trp VmaxTON/Km (uM^-1/min); the table footnote defines TON as turnover number (mol of product/mol of holoenzyme/min). Table 1, enzyme-form row A. oryzae IDObeta at pH 7.5, D-Trp column group; column VmaxTON (min^-1) = 373.6; column Km (mM) = 40.2; column VmaxTON/Km (uM^-1/min) = 9.2 x 10^-3. captured primary segment: A. oryzae IDObeta | D-Trp | kcat (VmaxTON) 373.6 min^-1 | Km 40.2 mM | kcat/Km (VmaxTON/Km) 9.2 x 10^-3 uM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 40.2 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 40.2 mM; the exported value is 40.2 mM. kcat: printed Table 1 cell 373.6 min^-1; 1 min^-1 is 1/60 s^-1, so 373.6 / 60 = 6.226666666666667 s^(-1); the exported value is 6.227 s^(-1), the same printed cell carried at the export's three-decimal precision. kcat/Km: printed Table 1 cell 9.2 x 10^-3 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 9.2 x 10^-3 x 1000 / 60 = 0.15333333333333335 s^(-1)*mM^(-1). The exported value is 0.1549004975124378 s^(-1)*mM^(-1), the quotient of the exported kcat 6.227 and Km 40.2.

raw_value_unit_evidence: Table 1, enzyme-form row A. oryzae IDObeta at pH 7.5, D-Trp column group: Km = 40.2 mM; kcat (printed VmaxTON) = 373.6 min^-1; printed kcat/Km (printed VmaxTON/Km) = 9.2 x 10^-3 uM^-1 min^-1.


column_label: Table 1: Kinetic parameters of bacterially-expressed fungal IDOs (J Mol Evol 2011, volume 72, pages 160-168); printed column heads enzyme form | pH | L-Trp VmaxTON (min^-1) | L-Trp Km | L-Trp VmaxTON/Km (uM^-1/min) | D-Trp VmaxTON (min^-1) | D-Trp Km (mM) | D-Trp VmaxTON/Km (uM^-1/min); the table footnote defines TON as turnover number (mol of product/mol of holoenzyme/min). Table 1, enzyme-form row A. oryzae IDOa at pH 6.5, L-Trp column group; column VmaxTON (min^-1) = 50.4; column Km (uM) = 154; column VmaxTON/Km (uM^-1/min) = 0.3. captured primary segment: A. oryzae IDOa | L-Trp | kcat (VmaxTON) 50.4 min^-1 | Km 154 uM | kcat/Km (VmaxTON/Km) 0.3 uM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 154 uM; 1 uM is 0.001 mM, so 154 / 1000 = 0.154 mM; the exported value is 0.154 mM. kcat: printed Table 1 cell 50.4 min^-1; 1 min^-1 is 1/60 s^-1, so 50.4 / 60 = 0.84 s^(-1); the exported value is 0.84 s^(-1). kcat/Km: printed Table 1 cell 0.3 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.3 x 1000 / 60 = 5.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.84 / 0.154 = 5.454545454545454 s^-1 mM^-1, the exported value, and 50.4 / 154 uM = 0.327273 uM^-1 min^-1 rounds to the printed catalytic-efficiency cell 0.3 uM^-1 min^-1.

raw_value_unit_evidence: Table 1, enzyme-form row A. oryzae IDOa at pH 6.5, L-Trp column group: Km = 154 uM; kcat (printed VmaxTON) = 50.4 min^-1; printed kcat/Km (printed VmaxTON/Km) = 0.3 uM^-1 min^-1.


column_label: Table 1: Kinetic parameters of bacterially-expressed fungal IDOs (J Mol Evol 2011, volume 72, pages 160-168); printed column heads enzyme form | pH | L-Trp VmaxTON (min^-1) | L-Trp Km | L-Trp VmaxTON/Km (uM^-1/min) | D-Trp VmaxTON (min^-1) | D-Trp Km (mM) | D-Trp VmaxTON/Km (uM^-1/min); the table footnote defines TON as turnover number (mol of product/mol of holoenzyme/min). Table 1, enzyme-form row A. oryzae IDObeta at pH 7.5, L-Trp column group; column VmaxTON (min^-1) = 1913.2; column Km (mM) = 1.4; column VmaxTON/Km (uM^-1/min) = 1.36. captured primary segment: A. oryzae IDObeta | L-Trp | kcat (VmaxTON) 1913.2 min^-1 | Km 1.4 mM | kcat/Km (VmaxTON/Km) 1.36 uM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 1.4 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.4 mM; the exported value is 1.4 mM. kcat: printed Table 1 cell 1913.2 min^-1; 1 min^-1 is 1/60 s^-1, so 1913.2 / 60 = 31.886666666666667 s^(-1); the exported value is 31.887 s^(-1), the same printed cell carried at the export's three-decimal precision. kcat/Km: printed Table 1 cell 1.36 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 1.36 x 1000 / 60 = 22.66666666666667 s^(-1)*mM^(-1). The exported value is 22.776428571428575 s^(-1)*mM^(-1), the quotient of the exported kcat 31.887 and Km 1.4.

raw_value_unit_evidence: Table 1, enzyme-form row A. oryzae IDObeta at pH 7.5, L-Trp column group: Km = 1.4 mM; kcat (printed VmaxTON) = 1913.2 min^-1; printed kcat/Km (printed VmaxTON/Km) = 1.36 uM^-1 min^-1.


organism: Paenarthrobacter nitroguajacolicus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D126A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H251A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T168S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S175T to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D120A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D219A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S95A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S95C with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


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


organism: Nitrospira defluvii

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.


sequence_variant_note: Mutation signature R137K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Oryctolagus cuniculus

substrate_name: serotonin


substrate_name: tryptamine

substrate: tryptamine


organism: Ideonella dechloratans

proof_lines:
chlorite dismutase
Ideonella dechloratans
characterization


proof_lines:
chlorite dismutase
Ideonella dechloratans
purified enzyme


organism: Cyanothece sp. PCC 7425

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q74E with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q74V with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Anolis carolinensis

sequence_variant_note: Mutation signature S171T could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R173A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R173K with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae


organism: Monodelphis domestica


organism: Ornithorhynchus anatinus


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S171T to reconstruct the assayed variant sequence.

proof_lines:
IDO variants
Ser or Thr substitutions
L-Trp affinity


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T171S to reconstruct the assayed variant sequence.


enzyme_display_name: Name not preserved

organism: Rattus norvegicus

substrate_name: L-cysteine

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

column_label: Prose section Kinetic Analysis and Metal Incorporation reports kcat and apparent KM; no table row supports the expected s^-1 value.

raw_value_unit_evidence: The section reports kcat 3.6 min^-1 and apparent KM 2.1 mM for the iron-enriched/no-EDTA preparation.

row_label: iron-enriched/no-EDTA recombinant mouse CDO preparation

table_label: Kinetic Analysis and Metal Incorporation prose

enzyme: Name not preserved

substrate: L-cysteine


column_label: Prose section Kinetic Analysis and Metal Incorporation reports the only primary kcat/KM pairings found for this paper.

normalized_value_unit_evidence: Paper kcat values normalize to 0.03 s^-1 and 0.06 s^-1; paper KM values are 3.4 mM and 2.1 mM; no primary 0.12 s^-1 or 0.002 mM evidence was found.

raw_value_unit_evidence: The section reports kcat 1.8 min^-1 and apparent KM 3.4 mM for the structure-determination enzyme, and kcat 3.6 min^-1 with apparent KM 2.1 mM for the iron-enriched/no-EDTA enzyme.

row_label: structure-determination and iron-enriched/no-EDTA recombinant mouse CDO preparations


organism: Klebsiella oxytoca

column_label: Table 3 columns are ARD and ARD'. In the ARD column, KmO2 (uM)=110 and kcat (s^-1)=5.0 x 10^2; surrounding kinetic text says the secondary plot against O2 concentration yields the pertinent kinetic constants.

normalized_value_unit_evidence: KmO2 normalized_value=0.11 normalized_unit=mM; kcat normalized_value=500 normalized_unit=s^-1; kcat_over_km normalized_value=4545.454545454545 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: KmO2 raw_value=110 raw_unit=uM; kcat raw_value=5.0 x 10^2 raw_unit=s^-1; kcat_over_km computed from exact primary cells 5.0 x 10^2 s^-1 / 0.110 mM

row_label: ARD column; KmO2 row and kcat row


substrate_name: oxygen (with Fe-ARD)

column_label: Table 3 columns are ARD and ARD'. In the ARD' column, KmO2 (uM)=47; Figure 2 caption identifies ARD' (Fe2+) initial velocity versus II at constant O2.

raw_value_unit_evidence: KmO2 raw_value=47 raw_unit=uM

row_label: ARD' column; KmO2 row

substrate: oxygen (with Fe-ARD)


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Aspergillus niger

proof_lines: protocatechuate 3,4 ring-cleavage dioxygenase

enzyme: protocatechuate 3,4-dioxygenase


enzyme_display_name: cysteine dioxygenase

substrate_name: L-Cysteine

enzyme: cysteine dioxygenase

substrate: L-Cysteine


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonate

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonate


enzyme_display_name: Polyunsaturated fatty acid lipoxygenase ALOX12

substrate_name: arachidonate (at pH 7.0 and 37 degrees Celsius)

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


substrate_name: docosahexaenoate

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

enzyme: Polyunsaturated fatty acid lipoxygenase ALOX12

substrate: docosahexaenoate


substrate_name: leukotriene A4 (at pH 7.4)

column_label: Figure 5 defines the LTA4 pH 7.4 assay and Table 1 lists LTA4 Km as 7.9 microM.

raw_value_unit_evidence: Table 1 row LTA4 reports Km 7.9 microM for recombinant human platelet 6His-12-LO.

row_label: LTA4 substrate for recombinant human platelet 6His-12-LO

table_label: Table 1, Kinetic constants of transformations catalysed by recombinant 12-LO

substrate: leukotriene A4 (at pH 7.4)


substrate_name: linoleate (at pH 8.0 and 25 degrees Celsius)

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

column_label: Results prose reports linoleic acid metabolism with Km 9 microM, and Fig. 5 defines the linoleic acid kinetic-analysis assay context.

raw_value_unit_evidence: Results prose for linoleic acid metabolism reports Km 9 microM.

row_label: recombinant human platelet 6His-12-lipoxygenase with linoleic acid (18:2)

table_label: Results prose and Fig. 5 kinetic-analysis context


substrate: arachidonate (at pH 7.0 and 37 degrees Celsius)


column_label: Figure 5 defines the LTA4 pH 7.4 assay and Table 1 lists LTA4 Km as 7.9 +/- 0.8 microM.

raw_value_unit_evidence: Km raw_value=7.9 +/- 0.8 raw_unit=microM


enzyme_display_name: arachidonate 15-lipoxygenase

substrate_name: arachidonic acid

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

enzyme: arachidonate 15-lipoxygenase

substrate: arachidonic acid


assay_conditions_summary: pH 8; 298.15 K; buffer linoleic acid substrate in 50 mM sodium phosphate

raw_value_unit_evidence: Km raw_value=9 raw_unit=microM; PDF text extraction renders the micro symbol as pM in this OCR layer

table_label: Results prose and Fig. 5 kinetic-analysis context, Wiley PDF page 4 / article page 848

substrate: linoleate (at pH 8.0 and 25 degrees Celsius)


enzyme_display_name: arachidonate 5-lipoxygenase

proof_lines:
5- and 15(omega-6)-lipoxygenases
human polymorphonuclear leukocytes

enzyme: arachidonate 5-lipoxygenase


enzyme_display_name: Polyunsaturated fatty acid 5-lipoxygenase

smiles: CCCCCC=CCC=CCC=CC=CC(CCCC(=O)[O-])OO


enzyme: Polyunsaturated fatty acid 5-lipoxygenase


enzyme_display_name: gentisate 1,2-dioxygenase

organism: Martelella sp. AD-3

enzyme: gentisate 1,2-dioxygenase


organism: Klebsiella pneumoniae

substrate_name: gentisate

substrate: gentisate


organism: Arthrobacter sp.


organism: Rhizorhabdus dicambivorans


enzyme_display_name: Homogentisate 1,2-dioxygenase

organism: Mus musculus

substrate_name: homogentisate

column_label: Abstract states the Km for its natural substrate HGA is 188 microM.

raw_value_unit_evidence: Km raw_value=188 raw_unit=microM

row_label: murine liver homogentisate 1,2-dioxygenase with homogentisate

table_label: PubMed abstract PMID 7705358

enzyme: Homogentisate 1,2-dioxygenase

substrate: homogentisate


enzyme_display_name: chlorite O2-lyase

substrate_name: Chlorite

enzyme: chlorite O2-lyase

substrate: Chlorite


organism: Nitrobacter winogradskyi


enzyme_display_name: acetylacetone-cleaving enzyme

organism: Acinetobacter johnsonii

smiles: O=O

enzyme: acetylacetone-cleaving enzyme


organism: Vigna unguiculata

proof_lines:
abamine
NCED
Spinacia oleracea


enzyme_display_name: indoleamine 2,3-dioxygenase

organism: Danio rerio

enzyme: indoleamine 2,3-dioxygenase


organism: Homo sapiens


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S167A to reconstruct the assayed variant sequence.


substrate_name: L-tryptophan

substrate: L-tryptophan


proof_lines:
L-tryptophan
IDO2
lower vertebrates


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F270G to reconstruct the assayed variant sequence.


enzyme_display_name: Indoleamine 2,3-dioxygenase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Indoleamine 2,3-dioxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S167H to reconstruct the assayed variant sequence.


organism: Branchiostoma floridae


organism: Monosiga brevicollis


organism: Nematostella vectensis


organism: Xenopus laevis


organism: Sulculus diversicolor

proof_lines:
Sulculus diversicolor
indoleamine 2,3-dioxygenase
L-Tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T163S to reconstruct the assayed variant sequence.


enzyme_display_name: Acireductone dioxygenase 1

organism: Oryza sativa subsp. indica

substrate_name: O(2) (using iron as cofactor)

enzyme: Acireductone dioxygenase 1

substrate: O(2) (using iron as cofactor)


enzyme_display_name: catechol 1,2-dioxygenase

organism: Acinetobacter radioresistens

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

proof_lines: mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication

enzyme: catechol 1,2-dioxygenase


proof_lines: mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication


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

proof_lines: wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication


substrate_name: catechol

substrate: catechol


proof_lines: wild type enzyme, in100 mM Tris-HCl pH 8.5, temperature not specified in the publication


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


enzyme_display_name: catechol 2,3-dioxygenase

organism: Stutzerimonas stutzeri

enzyme: catechol 2,3-dioxygenase


proof_lines:
wildtype
wild type enzyme, pH 7.5, 25°C


enzyme_display_name: UniProt Q9ZFE7

organism: Klebsiella oxytoca

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

enzyme: UniProt Q9ZFE7


organism: Rhodococcus opacus

substrate_name: protocatechuate

substrate: protocatechuate


proof_lines:
in 50 mM Tris/HCl, pH 7.2, 25°C
at pH 7.2 and 45°C


substrate_name: Hydroxyquinol

substrate: Hydroxyquinol


substrate_name: 2,3-Dihydroxybenzoic acid

substrate: 2,3-Dihydroxybenzoic acid


substrate_name: pyrogallol

substrate: pyrogallol


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Ectopseudomonas oleovorans

substrate_name: gallate

enzyme: protocatechuate 3,4-dioxygenase

substrate: gallate


substrate_name: caffeic acid

substrate: caffeic acid


substrate_name: catechin

substrate: catechin


substrate_name: L-Dopa

substrate: L-Dopa


substrate_name: D-tryptophan

proof_lines: H303A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min

substrate: D-tryptophan


proof_lines: H16A, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min

proof_lines: H16A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min


proof_lines: K352A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min


proof_lines: V109A mutant, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min


proof_lines: wild type, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min


enzyme_display_name: UniProt F8TW83

organism: Sphingomonas sp.

substrate_name: hydroquinone

enzyme: UniProt F8TW83

substrate: hydroquinone


enzyme_display_name: UniProt A0A128A3G4

organism: Candidatus Nitrosotalea devanaterra

enzyme: UniProt A0A128A3G4


organism: Pseudomonas putida


proof_lines:
mutant enzyme Y447H
Y447H mutant enzyme


organism: Acinetobacter sp.


mutation_type: deletion


organism: Cupriavidus necator


substrate_name: tetrachlorocatechol

substrate: tetrachlorocatechol


substrate_name: oxygen

substrate: oxygen


enzyme_display_name: UniProt Q6J1Z5

organism: Comamonas testosteroni

enzyme: UniProt Q6J1Z5


proof_lines: for the mutant enzyme Y408H, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions


proof_lines: for the mutant enzyme Y408E, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions


proof_lines: for the mutant enzyme Y408F, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions


proof_lines: for the mutant enzyme Y408C, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions


proof_lines:
oxygen electrode at pH 8.3
recombinant enzyme
native enzyme


proof_lines: for the wild-type enzyme, at 25°C in 50 mM Tris and 2 mM beta-mercaptoethanol, pH 8.5 under saturating protocatechuate and O2 conditions


proof_lines:
native enzyme
recombinant enzyme
at pH 8.3, spectrophotometric


enzyme_display_name: UniProt D0E8I5

organism: uncultured bacterium HF130_AEPn_1

enzyme: UniProt D0E8I5


enzyme_display_name: UniProt Q8KLK7

organism: Streptomyces toyocaensis

enzyme: UniProt Q8KLK7


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


enzyme_display_name: UniProt P9WNC5

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WNC5


proof_lines: rate dependent on the nucleophilic reactivity


organism: Homo sapiens

proof_lines: pH 7.0, 25°C, versus L-tryptophan and O2


assay_conditions_summary: pH 7.5; 298.15 K; buffer PBS; cofactor NADPH

proof_lines:
pH 7.5, 25°C, recombinant enzyme IDO2
pH 7.0
pH 7.0, normal atmospheric conditions


proof_lines:
pH 7.5, 25°C, recombinant enzyme IDO2
pH 6.5, 25°C, recombinant enzyme IDO1


proof_lines: 50 mM potassium phosphate, pH 6.5, 10 mM ascorbic acid, 0.01 mM methylene blue, 0.1 mg catalase, 37°C, 10 min


enzyme_display_name: fatty acid alpha-dioxygenase

organism: Crocosphaera subtropica

substrate_name: 13-methyltetradecanoic acid

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

enzyme: fatty acid alpha-dioxygenase

substrate: 13-methyltetradecanoic acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


enzyme_display_name: 3-carboxyethylcatechol 2,3-dioxygenase

organism: Escherichia coli

substrate_name: 2,3-dihydroxycinnamic acid

enzyme: 3-carboxyethylcatechol 2,3-dioxygenase

substrate: 2,3-dihydroxycinnamic acid


enzyme_display_name: UniProt W6JQJ6

organism: Pseudomonas sp. AIU 813

substrate_name: L-arginine

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

enzyme: UniProt W6JQJ6

substrate: L-arginine


substrate_name: L-lysine

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

substrate: L-lysine


substrate_name: L-ornithine

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

substrate: L-ornithine


enzyme_display_name: UniProt P06617

organism: Pseudomonas savastanoi

substrate_name: L-tryptophan

enzyme: UniProt P06617

substrate: L-tryptophan


enzyme_display_name: tryptophan 2-monooxygenase

substrate_name: L-Methionine

enzyme: tryptophan 2-monooxygenase

substrate: L-Methionine


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


enzyme_display_name: Cypridina-luciferin 2-monooxygenase

organism: Vargula hilgendorfii

substrate_name: Cypridina luciferin

enzyme: Cypridina-luciferin 2-monooxygenase

substrate: Cypridina luciferin


substrate_name: Luciferin

substrate: Luciferin


enzyme_display_name: UniProt P08659

organism: Photinus pyralis

substrate_name: D-luciferin

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.8
Raw SKiD Env: Temp=25°C, pH=7.5

enzyme: UniProt P08659

substrate: D-luciferin


substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

substrate: lauric acid


enzyme_display_name: UniProt P13129

organism: Luciola cruciata

enzyme: UniProt P13129


enzyme_display_name: UniProt A0A3F2YLV6

organism: Amydetes vivianii

substrate_name: D-firefly luciferin

enzyme: UniProt A0A3F2YLV6

substrate: D-firefly luciferin


substrate_name: ATP

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.8

substrate: ATP


substrate_name: linoleic acid

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

substrate: linoleic acid


enzyme_display_name: 4-vinylguaiacol dioxygenase

organism: Caulobacter segnis

substrate_name: isoeugenol

enzyme: 4-vinylguaiacol dioxygenase

substrate: isoeugenol


enzyme_display_name: 3-mercaptopropionate dioxygenase

organism: Azotobacter vinelandii

proof_lines: mutant Y159F, 37°C, pH not specified in the publication

enzyme: 3-mercaptopropionate dioxygenase


proof_lines: mutant H157N, 37°C, pH not specified in the publication


proof_lines: wild-type, 20°C, pH not specified in the publication


enzyme_display_name: 5-aminosalicylate 1,2-dioxygenase

organism: Comamonas thiooxydans

enzyme: 5-aminosalicylate 1,2-dioxygenase


substrate_name: gentisate

substrate: gentisate


enzyme_display_name: UniProt P32021

organism: Pseudomonas syringae

enzyme: UniProt P32021


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H116Q to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H168Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H169Q with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H268Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H284Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H305Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H309Q with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H335Q to reconstruct the assayed variant sequence.


organism: Pseudomonas savastanoi pv. phaseolicola


enzyme_display_name: lysine 2-monooxygenase

organism: Pseudomonas fluorescens

proof_lines: dehydrogenation with phenazine methosulfate

enzyme: lysine 2-monooxygenase


substrate_name: phenazine methosulfate

proof_lines: dehydrogenation of alanine and propylamine

substrate: phenazine methosulfate


substrate_name: arginine

substrate: arginine


substrate_name: alanine

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

substrate: alanine


substrate_name: ornithine

substrate: ornithine


substrate_name: L-ornithine

substrate: L-ornithine


substrate_name: L-lysine

substrate: L-lysine


substrate_name: L-arginine

substrate: L-arginine


enzyme_display_name: UniProt Q9QXN5

organism: Mus musculus

substrate_name: myo-inositol

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

enzyme: UniProt Q9QXN5

substrate: myo-inositol


enzyme_display_name: UniProt Q9UGB7

enzyme: UniProt Q9UGB7


enzyme_display_name: isoeugenol monooxygenase

organism: Prodigiosinella confusarubida

enzyme: isoeugenol monooxygenase


organism: Thermothelomyces thermophilus


enzyme_display_name: arginine 2-monooxygenase

organism: Streptomyces griseus

substrate_name: canavanine

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

enzyme: arginine 2-monooxygenase

substrate: canavanine


substrate_name: homoarginine

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

substrate: homoarginine


proof_lines:
monooxygenation of L-lysine
oxidation of L-ornithine


enzyme_display_name: lactate 2-monooxygenase

organism: Mycolicibacterium phlei

substrate_name: (S)-lactate

enzyme: lactate 2-monooxygenase

substrate: (S)-lactate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: (hydroxymethyl)phosphonate dioxygenase

organism: Gimesia maris

substrate_name: (hydroxymethyl)phosphonate

proof_lines: kcat is 0.55 sec(-1) with hydroxymethylphosphonate as substrate. kcat is 2.5 sec(-1) with (R)-2-amino-1-hydroxyethylphosphonic acid as substrate. kcat is 1.54 sec(-1) with (R)-1-hydroxyethylphosphonic acid as substrate.

enzyme: (hydroxymethyl)phosphonate dioxygenase

substrate: (hydroxymethyl)phosphonate


substrate_name: (R)-1-hydroxyethylphosphonic acid

smiles: CC(O)P(=O)(O)O

substrate: (R)-1-hydroxyethylphosphonic acid


organism: Pseudomonas nitroreducens


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K83R with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K95R with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L273F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K83R/K95R/L273F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K83R/K95R/L273F, at pH 8.0 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K83R/K95R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K83R/K95R, at pH 8.0 and 30°C


organism: Cupriavidus necator

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

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


organism: Mycolicibacterium smegmatis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G99A to reconstruct the assayed variant sequence.

proof_lines:
calculated constant, G99A mutant
observed constant, G99A mutant


proof_lines:
observed constant, G99A mutant
calculated constant, G99A mutant


organism: Pseudomonas aeruginosa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G95C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; buffer pH 6


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

assay_conditions_summary: pH 8.5; buffer pH 8

proof_lines:
wild-type, TRIS buffer pH 8.5, 37°C
wild-type, TRIS buffer pH 8.0, 37°C
wild-type, PIPES buffer pH 7.5, 37°C


enzyme_display_name: tryptophan 2'-dioxygenase

substrate_name: L-tryptophan

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

proof_lines:
TSO I
TSO II

enzyme: tryptophan 2'-dioxygenase

substrate: L-tryptophan


proof_lines:
TSO I
+ skatole
TSO II


substrate_name: N-Acetyl-L-tryptophanamide

substrate: N-Acetyl-L-tryptophanamide


enzyme_display_name: Hydroxymethylphosphonate dioxygenase

organism: Gimesia maris (strain ATCC 29201 / DSM 8797 / 534-30)

enzyme: Hydroxymethylphosphonate dioxygenase


enzyme_display_name: UniProt O75936

organism: Homo sapiens

enzyme: UniProt O75936


smiles: C[N+](C)(C)CCCC(=O)O

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7


enzyme_display_name: UniProt O15460

enzyme: UniProt O15460


substrate_name: ascorbate

substrate: ascorbate


enzyme_display_name: UniProt Q96KS0

enzyme: UniProt Q96KS0


enzyme_display_name: UniProt Q9GZT9

enzyme: UniProt Q9GZT9


organism: Pseudomonas putida

substrate_name: isoeugenol

substrate: isoeugenol


enzyme_display_name: UniProt Q88CC1

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

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7
kcat is 330 min(-1).

enzyme: UniProt Q88CC1


enzyme_display_name: 3-mercaptopropionate dioxygenase

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: cysteine (at 37 degrees Celsius)

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

proof_lines: kcat is 0.11 sec(-1) with 3-mercaptopropionate as substrate. kcat is 0.021 sec(-1) with cysteine as substrate (at 37 degrees Celsius).

enzyme: 3-mercaptopropionate dioxygenase

substrate: cysteine (at 37 degrees Celsius)


enzyme_display_name: UniProt O60568

enzyme: UniProt O60568


enzyme_display_name: UniProt Q7RYZ9

organism: Neurospora crassa

enzyme: UniProt Q7RYZ9


substrate_name: thymine

substrate: thymine


enzyme_display_name: flavanone 3-dioxygenase

organism: x Ascocenda

substrate_name: naringenin

enzyme: flavanone 3-dioxygenase

substrate: naringenin


substrate_name: (2R)-2-sulfanylbutanedioic acid

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

proof_lines: mutant Q62R, pH not specified in the publication, temperature not specified in the publication

substrate: (2R)-2-sulfanylbutanedioic acid


enzyme_display_name: 5-aminosalicylate 1,2-dioxygenase

organism: Comamonas sp

enzyme: 5-aminosalicylate 1,2-dioxygenase


enzyme_display_name: Isoeugenol monooxygenase

enzyme: Isoeugenol monooxygenase


enzyme_display_name: fatty acid alpha-dioxygenase

organism: Arabidopsis thaliana

enzyme: fatty acid alpha-dioxygenase


organism: Oryza sativa subsp. japonica


enzyme_display_name: tryptophan 2-monooxygenase

organism: Pseudomonas savastanoi

substrate_name: O2; L-Tryptophan

enzyme: tryptophan 2-monooxygenase

substrate: O2; L-Tryptophan


enzyme_display_name: UniProt Q9NWT6

smiles: O=O

enzyme: UniProt Q9NWT6


enzyme_display_name: lactate 2-monooxygenase

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y152F to reconstruct the assayed variant sequence.

enzyme: lactate 2-monooxygenase


enzyme_display_name: L-lactate 2-monooxygenase

enzyme: L-lactate 2-monooxygenase


substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

assay_conditions_summary: pH 8; buffer increasing fatty acid concentrations in 0.1 M Tris

column_label: PMID 10455113 / DOI 10.1074/jbc.274.35.24503, Table II, row Palmitic acid, Arabidopsis pFASTBAC-ara.N38086 Km = 11 uM.

raw_value_unit_evidence: Table II row Palmitic acid, pFASTBAC-ara.N38086 Km column = 11 uM.

row_label: Palmitic acid

table_label: Table II: Kinetic constants of recombinant oxygenases

substrate: palmitic acid


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

assay_conditions_summary: pH 7.8; buffer increasing fatty acid concentrations in 0.1 M Tris

column_label: PMID 10455113 / DOI 10.1074/jbc.274.35.24503, Table II, row Oleic acid, Arabidopsis pFASTBAC-ara.N38086 Km = 13 uM.

raw_value_unit_evidence: Table II row Oleic acid, pFASTBAC-ara.N38086 Km column = 13 uM.

row_label: Oleic acid

substrate: oleic acid


substrate_name: linoleic acid

column_label: PMID 10455113 / DOI 10.1074/jbc.274.35.24503, Table II, row Linoleic acid, Arabidopsis pFASTBAC-ara.N38086 Km = 17 uM.

raw_value_unit_evidence: Table II row Linoleic acid, pFASTBAC-ara.N38086 Km column = 17 uM.

row_label: Linoleic acid

substrate: linoleic acid


substrate_name: linolenic acid

smiles: CCC=CCC=CCC=CCCCCCCCC(=O)O

column_label: PMID 10455113 / DOI 10.1074/jbc.274.35.24503, Table II, row Linolenic acid, Arabidopsis pFASTBAC-ara.N38086 Km = 18 uM.

raw_value_unit_evidence: Table II row Linolenic acid, pFASTBAC-ara.N38086 Km column = 18 uM.

row_label: Linolenic acid

substrate: linolenic acid


enzyme_display_name: hyoscyamine (6S)-dioxygenase

organism: Anisodus tanguticus

substrate_name: hyoscyamine

enzyme: hyoscyamine (6S)-dioxygenase

substrate: hyoscyamine


organism: Brugmansia sanguinea

substrate_name: L-hyoscyamine

substrate: L-hyoscyamine


organism: Datura metel


enzyme_display_name: gibberellin 2beta-dioxygenase

organism: Phaseolus vulgaris

substrate_name: [2,3-3H2]gibberellin 9

proof_lines:
isoenzyme II
isoenzyme I

enzyme: gibberellin 2beta-dioxygenase

substrate: [2,3-3H2]gibberellin 9


enzyme_display_name: lysine 2-monooxygenase

organism: Pseudomonas sp. AIU 813

substrate_name: L-lysine

sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238A to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238A / L-lysine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1799-1809.

normalized_value_unit_evidence: Monooxygenase kcat 2.7 s^-1; Monooxygenase Km 0.26 mM; Monooxygenase kcat/Km 10 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 2.7 ± 0.4 s^-1; Monooxygenase Km 0.26 ± 0.02 mM; Monooxygenase kcat/Km 10 ± 1 s^-1 mM^-1

row_label: D238A / L-lysine / Monooxygenase

table_label: PMID 29511608 Table 2. Kinetic parameters of wild-type and mutant enzymes of l-AAO/MOG

enzyme: lysine 2-monooxygenase

substrate: L-lysine


sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238E to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238E / L-lysine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1833-1843.

normalized_value_unit_evidence: Monooxygenase kcat 8.1 s^-1; Monooxygenase Km 0.043 mM; Monooxygenase kcat/Km 190 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 8.1 ± 0.6 s^-1; Monooxygenase Km 0.043 ± 0.001 mM; Monooxygenase kcat/Km 190 ± 10 s^-1 mM^-1

row_label: D238E / L-lysine / Monooxygenase


sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238F to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238F / L-lysine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1856-1866.

normalized_value_unit_evidence: Monooxygenase kcat 0.80 s^-1; Monooxygenase Km 0.072 mM; Monooxygenase kcat/Km 11 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 0.80 ± 0.04 s^-1; Monooxygenase Km 0.072 ± 0.003 mM; Monooxygenase kcat/Km 11 ± 1 s^-1 mM^-1

row_label: D238F / L-lysine / Monooxygenase


column_label: PMID 29511608 Table 2; row WT / L-lysine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1766-1775.

normalized_value_unit_evidence: Monooxygenase kcat 4.5 s^-1; Monooxygenase Km 0.061 mM; Monooxygenase kcat/Km 74 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 4.5 ± 0.1 s^-1; Monooxygenase Km 0.061 ± 0.006 mM; Monooxygenase kcat/Km 74 ± 5 s^-1 mM^-1

row_label: WT / L-lysine / Monooxygenase


substrate_name: L-Ornithine

column_label: PMID 29511608 Table 2; row D238A / L-Ornithine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1811-1820.

normalized_value_unit_evidence: Monooxygenase kcat 0.29 s^-1; Monooxygenase Km 0.31 mM; Monooxygenase kcat/Km 0.94 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 0.29 ± 0.01 s^-1; Monooxygenase Km 0.31 ± 0.01 mM; Monooxygenase kcat/Km 0.94 ± 0.04 s^-1 mM^-1

row_label: D238A / L-Ornithine / Monooxygenase

substrate: L-Ornithine


column_label: PMID 29511608 Table 2; row D238E / L-Ornithine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1845-1854.

normalized_value_unit_evidence: Monooxygenase kcat 2.3 s^-1; Monooxygenase Km 0.061 mM; Monooxygenase kcat/Km 32 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 2.3 ± 0.2 s^-1; Monooxygenase Km 0.061 ± 0.004 mM; Monooxygenase kcat/Km 32 ± 2 s^-1 mM^-1

row_label: D238E / L-Ornithine / Monooxygenase


substrate_name: L-Arginine

column_label: PMID 29511608 Table 2; row D238A / L-Arginine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1822-1831.

normalized_value_unit_evidence: Monooxygenase kcat 2.8 s^-1; Monooxygenase Km 0.42 mM; Monooxygenase kcat/Km 6.7 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 2.8 ± 0.4 s^-1; Monooxygenase Km 0.42 ± 0.04 mM; Monooxygenase kcat/Km 6.7 ± 0.3 s^-1 mM^-1

row_label: D238A / L-Arginine / Monooxygenase

substrate: L-Arginine


column_label: PMID 29511608 Table 2; row D238F / L-Arginine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1868-1877.

normalized_value_unit_evidence: Monooxygenase kcat 1.2 s^-1; Monooxygenase Km 0.090 mM; Monooxygenase kcat/Km 13 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 1.2 ± 0.29 s^-1; Monooxygenase Km 0.090 ± 0.004 mM; Monooxygenase kcat/Km 13 ± 1 s^-1 mM^-1

row_label: D238F / L-Arginine / Monooxygenase


column_label: PMID 29511608 Table 2; row WT / L-Arginine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1788-1797.

normalized_value_unit_evidence: Monooxygenase kcat 1.6 s^-1; Monooxygenase Km 0.067 mM; Monooxygenase kcat/Km 24 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 1.6 ± 0.2 s^-1; Monooxygenase Km 0.067 ± 0.005 mM; Monooxygenase kcat/Km 24 ± 1 s^-1 mM^-1

row_label: WT / L-Arginine / Monooxygenase


column_label: PMID 29511608 Table 2; row WT / L-Ornithine; monooxygenase columns kcat, Km, kcat/Km; PMC article HTML lines 1777-1786.

normalized_value_unit_evidence: Monooxygenase kcat 6.7 s^-1; Monooxygenase Km 0.033 mM; Monooxygenase kcat/Km 200 s^-1 mM^-1

raw_value_unit_evidence: Monooxygenase kcat 6.7 ± 0.6 s^-1; Monooxygenase Km 0.033 ± 0.001 mM; Monooxygenase kcat/Km 200 ± 10 s^-1 mM^-1

row_label: WT / L-Ornithine / Monooxygenase


enzyme_display_name: taurine dioxygenase

organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y73I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y73I, in the presence of taurine

enzyme: taurine dioxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W98I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W98I, in the presence of taurine


substrate_name: taurine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H255E with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

substrate: taurine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H255Q with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


organism: Atropa belladonna


organism: Anisodus acutangulus


substrate_name: L-Hyoscyamine; O2; 2-Oxoglutarate

substrate: L-Hyoscyamine; O2; 2-Oxoglutarate


organism: Hyoscyamus niger


organism: Pisum sativum

substrate_name: O2; 2-Oxoglutarate; Gibberellin A20

substrate: O2; 2-Oxoglutarate; Gibberellin A20


enzyme_display_name: gibberellin 3beta-dioxygenase

enzyme: gibberellin 3beta-dioxygenase


substrate_name: Gibberellin A9; O2; 2-Oxoglutarate

substrate: Gibberellin A9; O2; 2-Oxoglutarate


enzyme_display_name: peptide-aspartate beta-dioxygenase

organism: Homo sapiens

substrate_name: [thioether-linked cyclic peptide hFX-CP101-119]-L-aspartate

proof_lines: pH and temperature not specified in the publication

enzyme: peptide-aspartate beta-dioxygenase


substrate_name: Taurine

column_label: Table 1 columns TauD variant, kcat (s^-1), taurine Km (uM), and kcat/Km (uM^-1 s^-1); row matched by wild-type TauD and taurine substrate.

normalized_value_unit_evidence: kcat 12.5 s^-1; Km 0.058 mM; printed kcat/Km 220 s^-1*mM^-1; quotient of printed kcat and Km is 215.51724137931032 s^-1*mM^-1.

row_label: wild type; taurine

table_label: Table 1, Kinetic and Spectroscopic Parameters for Wild-Type TauD and Selected Variants

substrate: Taurine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P37610 current sequence matched to UniSave entry 39 sequence version 2 plus initiator methionine and applied mutation signature Y256F to reconstruct the assayed variant sequence.

column_label: Table 1, Kinetic and Spectroscopic Parameters for Wild-Type TauD and Selected Variants; row Y256F; taurine; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); Y256F; taurine: kcat 6.2 +/- 0.3 s^-1; Km 122 +/- 17 uM; kcat/Km 0.05 +/- 0.01 uM^-1 s^-1. Normalized without derivation to kcat=6.2 s^-1; Km=0.122 mM; kcat/Km=50.0 s^-1*mM^-1.

row_label: Y256F; taurine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y73I to reconstruct the assayed variant sequence.

column_label: Table 1, Kinetic and Spectroscopic Parameters for Wild-Type TauD and Selected Variants; row Y73I; taurine; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); Y73I; taurine: kcat 7.3 +/- 0.6 s^-1; Km 243 +/- 33 uM; kcat/Km 0.030 +/- 0.007 uM^-1 s^-1. Normalized without derivation to kcat=7.3 s^-1; Km=0.243 mM; kcat/Km=30.0 s^-1*mM^-1.

row_label: Y73I; taurine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y73S to reconstruct the assayed variant sequence.

column_label: Table 1, Kinetic and Spectroscopic Parameters for Wild-Type TauD and Selected Variants; row Y73S; taurine; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); Y73S; taurine: kcat 11.0 +/- 2.0 s^-1; Km 630 +/- 200 uM; kcat/Km 0.018 +/- 0.009 uM^-1 s^-1. Normalized without derivation to kcat=11.0 s^-1; Km=0.63 mM; kcat/Km=18.0 s^-1*mM^-1.

row_label: Y73S; taurine