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


enzyme_display_name: indoleamine 2,3-dioxygenase

organism: Homo sapiens

substrate_name: L-Tryptophan

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

data_origin: experimental

enzyme: indoleamine 2,3-dioxygenase

substrate: L-Tryptophan

status: unverified

source: oed


organism: Aspergillus oryzae

substrate_name: D-Tryptophan

verification_status: verified

mutation_signature: Unknown

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

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, 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.

substrate: D-Tryptophan

status: verified


verification_status: corrected

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.

status: corrected


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.


organism: Oryzias latipes

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.


enzyme_display_name: chlorite O2-lyase

organism: Nitrospira defluvii

substrate_name: Chlorite

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

enzyme: chlorite O2-lyase

substrate: Chlorite


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

source_db: brenda

substrate: serotonin

source: brenda


substrate_name: tryptamine

substrate: tryptamine


organism: Ideonella dechloratans

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

sequence_source: multiple

smiles: [O-]Cl=O

proof_lines:
chlorite dismutase
Ideonella dechloratans
characterization

source_databases_merged: sabio_rk brenda uniprot


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).


organism: Mus musculus


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

source_db: skid

kcat_over_km_display: Not reported

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

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

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

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

source_databases_merged: skid uniprot

enzyme: Name not preserved

substrate: L-cysteine

source: skid


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

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

smiles: O=O

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

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


enzyme_display_name: Acireductone dioxygenase

substrate_name: oxygen (with Fe-ARD)

source_db: uniprot

kcat_display: Not reported

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

enzyme: Acireductone dioxygenase

substrate: oxygen (with Fe-ARD)

source: uniprot


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

organism: Homo sapiens

substrate_name: arachidonate

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

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-]

assay_conditions_summary: pH 7


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-]

assay_conditions_summary: pH 8

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

source_databases_merged: brenda skid

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

source_databases_merged: brenda uniprot

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

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


organism: Nitrobacter winogradskyi


enzyme_display_name: acetylacetone-cleaving enzyme

organism: Acinetobacter johnsonii

enzyme: acetylacetone-cleaving enzyme


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase

organism: Vigna unguiculata

proof_lines:
abamine
NCED
Spinacia oleracea

enzyme: 9-cis-epoxycarotenoid dioxygenase


organism: Danio rerio


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


substrate_name: L-Tryptophan

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

substrate: L-Tryptophan


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

km_display: Not reported

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


enzyme_display_name: indoleamine 2,3-dioxygenase

enzyme: indoleamine 2,3-dioxygenase


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

source_license: CC BY-NC-ND 4.0

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


ki_unit: mM


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


organism: Homo sapiens

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


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

organism: Homo sapiens

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


smiles: O=O

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

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

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

enzyme: tryptophan 2-monooxygenase

substrate: O2; L-Tryptophan


enzyme_display_name: UniProt Q9NWT6

organism: Homo sapiens

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

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


substrate_name: pentanesulfonic acid

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N97A to reconstruct the assayed variant sequence.

smiles: CCCCCS(=O)(=O)O

column_label: Table 2, Comparison of Steady-State Kinetic Parameters for Selected TauD Variants Using Alternative Sulfonates at Two pH Values; row PSA (6.9) N97A; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); PSA (6.9) N97A: kcat 1.7 +/- 0.2 s^-1; Km 630 +/- 270 uM; kcat/Km 0.0026 +/- 0.0014 uM^-1 s^-1. Normalized without derivation to kcat=1.7 s^-1; Km=0.63 mM; kcat/Km=2.6 s^-1*mM^-1.

substrate: pentanesulfonic acid


column_label: Table 2, Comparison of Steady-State Kinetic Parameters for Selected TauD Variants Using Alternative Sulfonates at Two pH Values; row PSA (8.0) N97A; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); PSA (8.0) N97A: kcat 2.83 +/- 1.25 s^-1; Km 1100 +/- 300 uM; kcat/Km 0.0025 +/- 0.0005 uM^-1 s^-1. Normalized without derivation to kcat=2.83 s^-1; Km=1.1 mM; kcat/Km=2.5 s^-1*mM^-1.


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 S158A to reconstruct the assayed variant sequence.

column_label: Table 2, Comparison of Steady-State Kinetic Parameters for Selected TauD Variants Using Alternative Sulfonates at Two pH Values; row PSA (6.9) S158A; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); PSA (6.9) S158A: kcat 3.97 +/- 1.0 s^-1; Km 602 +/- 274 uM; kcat/Km 0.0065 +/- 0.0045 uM^-1 s^-1. Normalized without derivation to kcat=3.97 s^-1; Km=0.602 mM; kcat/Km=6.5 s^-1*mM^-1.


column_label: Table 2 columns substrate (pH) and TauD variant, kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); row matched by substrate PSA, pH 6.9, and wild-type TauD.

normalized_value_unit_evidence: kcat 2.1 s^-1; Km 1.7 mM; printed kcat/Km 1.2 s^-1*mM^-1; quotient of printed kcat and Km is 1.235 s^-1*mM^-1.

row_label: PSA (6.9) wild type

table_label: Table 2, Comparison of Steady-State Kinetic Parameters for Selected TauD Variants Using Alternative Sulfonates at Two pH Values


column_label: Table 2 columns substrate (pH) and TauD variant, kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); row matched by substrate PSA, pH 8.0, and wild-type TauD.

normalized_value_unit_evidence: kcat 3.5 s^-1; Km 2.6 mM; printed kcat/Km 1.3 s^-1*mM^-1; quotient of printed kcat and Km is 1.346 s^-1*mM^-1.

row_label: PSA (8.0) wild type


substrate_name: 3-N-Morpholinopropanesulfonic acid

column_label: Table 2, Comparison of Steady-State Kinetic Parameters for Selected TauD Variants Using Alternative Sulfonates at Two pH Values; row MOPS (6.9) N97A; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); MOPS (6.9) N97A: kcat 0.59 +/- 0.25 s^-1; Km 236 +/- 136 uM; kcat/Km 0.0025 +/- 0.0024 uM^-1 s^-1. Normalized without derivation to kcat=0.59 s^-1; Km=0.236 mM; kcat/Km=2.5 s^-1*mM^-1.

substrate: 3-N-Morpholinopropanesulfonic acid


sequence_source: UniProtKB:P37610 current sequence matched to UniSave entry 39 sequence version 2 plus initiator methionine

column_label: Table 2, Comparison of Steady-State Kinetic Parameters for Selected TauD Variants Using Alternative Sulfonates at Two pH Values; row MOPS (6.9) S158A; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); MOPS (6.9) S158A: kcat 1.25 +/- 0.10 s^-1; Km 247 +/- 68 uM; kcat/Km 0.0050 +/- 0.0013 uM^-1 s^-1. Normalized without derivation to kcat=1.25 s^-1; Km=0.247 mM; kcat/Km=5.0 s^-1*mM^-1.


column_label: Table 2 columns substrate (pH) and TauD variant, kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); row matched by substrate MOPS, pH 6.9, and wild-type TauD.

normalized_value_unit_evidence: kcat 0.95 s^-1; Km 0.3 mM; printed kcat/Km 3.1 s^-1*mM^-1; quotient of printed kcat and Km is 3.167 s^-1*mM^-1.

row_label: MOPS (6.9) wild type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D94A to reconstruct the assayed variant sequence.

proof_lines: TauD taurine N95A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N95A to reconstruct the assayed variant sequence.

column_label: Table 1, Kinetic and Spectroscopic Parameters for Wild-Type TauD and Selected Variants; row N95A; taurine; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); N95A; taurine: kcat 0.83 +/- 0.05 s^-1; Km 1500 +/- 600 uM; kcat/Km 0.0006 +/- 0.0003 uM^-1 s^-1. Normalized without derivation to kcat=0.83 s^-1; Km=1.5 mM; kcat/Km=0.6 s^-1*mM^-1.

row_label: N95A; taurine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N95D to reconstruct the assayed variant sequence.

column_label: Table 1, Kinetic and Spectroscopic Parameters for Wild-Type TauD and Selected Variants; row N95D; taurine; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); N95D; taurine: kcat 1.75 +/- 0.7 s^-1; Km 1500 +/- 300 uM; kcat/Km 0.0012 +/- 0.0007 uM^-1 s^-1. Normalized without derivation to kcat=1.75 s^-1; Km=1.5 mM; kcat/Km=1.2 s^-1*mM^-1.

row_label: N95D; taurine


column_label: Table 1, Kinetic and Spectroscopic Parameters for Wild-Type TauD and Selected Variants; row N97A; taurine; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); N97A; taurine: kcat 3.8 +/- 0.5 s^-1; Km 44 +/- 17 uM; kcat/Km 0.09 +/- 0.04 uM^-1 s^-1. Normalized without derivation to kcat=3.8 s^-1; Km=0.044 mM; kcat/Km=90.0 s^-1*mM^-1.

row_label: N97A; taurine


column_label: Table 2, Comparison of Steady-State Kinetic Parameters for Selected TauD Variants Using Alternative Sulfonates at Two pH Values; row taurine (6.9) S158A; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); taurine (6.9) S158A: kcat 7.2 +/- 0.05 s^-1; Km 323 +/- 26 uM; kcat/Km 0.022 +/- 0.003 uM^-1 s^-1. Normalized without derivation to kcat=7.2 s^-1; Km=0.323 mM; kcat/Km=22.0 s^-1*mM^-1.

row_label: taurine (6.9) S158A


column_label: Table 1, Kinetic and Spectroscopic Parameters for Wild-Type TauD and Selected Variants; row S158A; taurine; columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1); S158A; taurine: kcat 6.3 +/- 0.8 s^-1; Km 100 +/- 20 uM; kcat/Km 0.06 +/- 0.02 uM^-1 s^-1. Normalized without derivation to kcat=6.3 s^-1; Km=0.1 mM; kcat/Km=60.0 s^-1*mM^-1.

row_label: S158A; taurine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W248F to reconstruct the assayed variant sequence.


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


substrate_name: 2-Oxoglutarate; O2; Gibberellin A20

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

substrate: 2-Oxoglutarate; O2; Gibberellin A20


organism: Triticum aestivum

substrate_name: Gibberellin A9; 2-Oxoglutarate; O2

substrate: Gibberellin A9; 2-Oxoglutarate; O2


substrate_name: 2-Oxoglutarate; O2; Taurine

substrate: 2-Oxoglutarate; O2; Taurine


organism: Nicotiana tabacum

substrate_name: oleic acid

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

proof_lines:
alpha-dioxygenase in tobacco
alpha-oxidation
oleic acid row not preserved

substrate: oleic acid


substrate_name: linolenic acid

proof_lines:
linolenic acid
alpha-dioxygenase in tobacco
alpha-oxidation

substrate: linolenic acid


substrate_name: linoleic acid

proof_lines:
alpha-dioxygenase in tobacco
alpha-oxidation
linoleic acid not preserved

substrate: linoleic acid


substrate_name: arachidonic acid

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

proof_lines:
alpha-dioxygenase in tobacco
alpha-oxidation
arachidonic acid not preserved

substrate: arachidonic acid


substrate_name: L-Tryptophan

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R98A to reconstruct the assayed variant sequence.

substrate: L-Tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R98K to reconstruct the assayed variant sequence.


organism: Escherichia coli (strain K12)

substrate_name: taurine (at pH 6.9)

column_label: Abstract reports taurine (Km = 55 microM) was the preferred substrate and alpha-ketoglutarate (Km = 11 microM) supported significant dioxygenase activity.

raw_value_unit_evidence: Km raw_value=55 microM raw_unit=microM

row_label: Escherichia coli TauD alpha-ketoglutarate-dependent taurine dioxygenase / taurine

table_label: PubMed XML abstract PMID 9287300

substrate: taurine (at pH 6.9)


substrate_name: 2-oxoglutarate (at pH 6.9)

raw_value_unit_evidence: Km raw_value=11 microM raw_unit=microM

row_label: Escherichia coli TauD alpha-ketoglutarate-dependent taurine dioxygenase / alpha-ketoglutarate

substrate: 2-oxoglutarate (at pH 6.9)


substrate_name: butanesulfonate (at pH 6.9)

substrate: butanesulfonate (at pH 6.9)


substrate_name: 3-(N-morpholino)propanesulfonate (at pH 6.9)


substrate_name: 1,3-dioxo-2-isoindolineethanesulfonate (at pH 6.9)


substrate_name: L-tryptophan

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K365M to reconstruct the assayed variant sequence.

substrate: L-tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W466F to reconstruct the assayed variant sequence.


column_label: Table 2 explicitly labels columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); matched 2OG row, kcat and kcat/Km columns for required metrics.

normalized_value_unit_evidence: Km normalized_value=0.0006 normalized_unit=mM; kcat normalized_value=0.19 normalized_unit=s^-1; kcat/Km normalized_value=320 normalized_unit=s^-1*mM^-1 from explicit table unit conversion (uM^-1 to mM^-1).

table_label: Table 2, Steady-state kinetic parameters for AspH


proof_lines:
pH 7.5, 20°C
pH 7.8, 30°C
Raw SKiD Env: Temp=20°C, pH=7.5


column_label: Table 2 explicitly labels columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1); matched O2 row, kcat and kcat/Km columns for required metrics.

normalized_value_unit_evidence: Km normalized_value=0.426 normalized_unit=mM; kcat normalized_value=0.23 normalized_unit=s^-1; kcat/Km normalized_value=0.54 normalized_unit=s^-1*mM^-1 from explicit table unit conversion (uM^-1 to mM^-1).


enzyme_display_name: Codeine O-demethylase

organism: Papaver somniferum

substrate_name: codeine

proof_lines: kcat is 0.095 sec(-1) with (S)-scoulerine as substrate.

enzyme: Codeine O-demethylase

substrate: codeine


substrate_name: thebaine

substrate: thebaine


proof_lines: The kinetic constants are determined for the recombinant FLAG-His-tagged protein.


enzyme_display_name: Hypoxia-inducible factor 1-alpha inhibitor


enzyme: Hypoxia-inducible factor 1-alpha inhibitor


substrate_name: ascorbate

substrate: ascorbate


substrate_name: L-hyoscyamine

substrate: L-hyoscyamine


substrate_name: L-Hyoscyamine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S14P/K97A to reconstruct the assayed variant sequence.

substrate: L-Hyoscyamine


substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: Prolyl hydroxylase EGLN2

substrate_name: HIF1A DLDLEMLAPYIPMDDDFQL peptide (at pH 7.5 and 37 degrees Celsius)

enzyme: Prolyl hydroxylase EGLN2


substrate_name: L-prolyl-[hypoxia-inducible factor alpha subunit]; O2; 2-Oxoglutarate


organism: Rattus norvegicus

substrate: HIF1A DLDLEMLAPYIPMDDDFQL peptide (at pH 7.5 and 37 degrees Celsius)


enzyme_display_name: thebaine 6-O-demethylase

substrate_name: O2; Thebaine; 2-Oxoglutarate

enzyme: thebaine 6-O-demethylase

substrate: O2; Thebaine; 2-Oxoglutarate


enzyme_display_name: Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3

substrate_name: N(1)-methyl-2'-deoxyadenosine in single-stranded DNA


enzyme_display_name: DNA oxidative demethylase ALKBH2

enzyme: DNA oxidative demethylase ALKBH2

substrate: N(1)-methyl-2'-deoxyadenosine in single-stranded DNA


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -15, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature D210G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: L-proline cis-3-hydroxylase 2

organism: Streptomyces sp

proof_lines: Comparison of both proline 3-hydroxylase isozymes shows that type II enzyme has 1.8-fold higher activity than type I upon L-proline, and 24-fold higher activity upon L-2-azetidinecarboxylic acid.

enzyme: L-proline cis-3-hydroxylase 2


enzyme_display_name: L-proline cis-3-hydroxylase 1

enzyme: L-proline cis-3-hydroxylase 1


enzyme_display_name: codeine 3-O-demethylase

substrate_name: Codeine; O2; 2-Oxoglutarate

enzyme: codeine 3-O-demethylase

substrate: Codeine; O2; 2-Oxoglutarate


substrate_name: L-proline

substrate: L-proline


organism: Homo sapiens

substrate_name: HIF1A (788-822) peptide

substrate: HIF1A (788-822) peptide


substrate_name: DESGLPQLTSYDAEVNAPIQGSRNLLQGEELLRALDQVN

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D210E with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

substrate: DESGLPQLTSYDAEVNAPIQGSRNLLQGEELLRALDQVN


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D210G with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 5-aminosalicylate 1,2-dioxygenase

organism: Comamonas sp

enzyme: 5-aminosalicylate 1,2-dioxygenase


substrate_name: gentisate

substrate: gentisate


enzyme_display_name: Thebaine 6-O-demethylase

substrate_name: oripavine

proof_lines:
thebaine 6-O-demethylase
codeine O-demethylase
Papaver somniferum

enzyme: Thebaine 6-O-demethylase

substrate: oripavine


enzyme_display_name: Alpha-dioxygenase PIOX

enzyme: Alpha-dioxygenase PIOX


substrate_name: dodecanoate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: dodecanoate


column_label: Official ScienceDirect Table 1; row Oxoglutarate; column Rat PHD-1 Km; raw value 25 uM; normalized value 0.025 mM; assay at pH 7.5 and 37 C with other components saturating and oxygen at air concentration.

normalized_value_unit_evidence: 25 uM converts exactly to 0.025 mM, matching the current exported Km 0.025 mM.

raw_value_unit_evidence: Table 1 row Oxoglutarate, column Rat PHD-1 Km: 25 uM.

row_label: Oxoglutarate

table_label: Official ScienceDirect full-text HTML Table 1: Kinetic constants for rat and human PHD-1 using substrate peptide HIF-19


substrate_name: L-ascorbate (at pH 7.5 and 37 degrees Celsius)

column_label: Official ScienceDirect Table 1; row Ascorbate; column Rat PHD-1 Km; raw value 55 uM; normalized value 0.055 mM; assay at pH 7.5 and 37 C with other components saturating and oxygen at air concentration.

normalized_value_unit_evidence: 55 uM converts exactly to 0.055 mM, matching the current exported Km 0.055 mM.

raw_value_unit_evidence: Table 1 row Ascorbate, column Rat PHD-1 Km: 55 uM.

row_label: Ascorbate


substrate_name: Fe(2+) (at pH 7.5 and 37 degrees Celsius)


substrate_name: DLDLEALAPYIPADDDFQL

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T387A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Table 2. Steady state kinetic constants with varied [CODD]; row_label: T387A / paper row Thr387->Ala; columns kcat (min^-1), KM (uM), and kcat/KM (uM^-1 min^-1).

raw_value_unit_evidence: Table 2. Steady state kinetic constants with varied [CODD] row Thr387->Ala: kcat 44.0 +/- 3 min^-1; KM 4.1 +/- 0.7 uM; kcat/KM 11.0 +/- 1 uM^-1 min^-1.

row_label: T387A / paper row Thr387->Ala

substrate: DLDLEALAPYIPADDDFQL


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T387N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Table 2. Steady state kinetic constants with varied [CODD]; row_label: T387N / paper row Thr387->Asn; columns kcat (min^-1), KM (uM), and kcat/KM (uM^-1 min^-1).

raw_value_unit_evidence: Table 2. Steady state kinetic constants with varied [CODD] row Thr387->Asn: kcat 0.9 +/- 0.1 min^-1; KM 1.4 +/- 0.2 uM; kcat/KM 0.7 +/- 0.1 uM^-1 min^-1.

row_label: T387N / paper row Thr387->Asn


column_label: Table 2. Steady state kinetic constants with varied [CODD]; row_label: WT-PHD2; columns kcat (min^-1), KM (uM), and kcat/KM (uM^-1 min^-1).

raw_value_unit_evidence: Table 2. Steady state kinetic constants with varied [CODD] row WT-PHD2: kcat 1.9 +/- 0.1 min^-1; KM 0.8 +/- 0.1 uM; kcat/KM 2.4 +/- 0.2 uM^-1 min^-1.


column_label: Table 3. Steady state kinetic parameters using O2 as the varied substrate; row_label: T387A / paper row Thr387->Ala; columns kcat (min^-1), KM (uM), and kcat/KM (uM^-1 min^-1).

raw_value_unit_evidence: Table 3. Steady state kinetic parameters using O2 as the varied substrate row Thr387->Ala: kcat 29.0 +/- 3 min^-1; KM 100.0 +/- 20 uM; kcat/KM 0.3 +/- 0.1 uM^-1 min^-1.


column_label: Table 3. Steady state kinetic parameters using O2 as the varied substrate; row_label: WT-PHD2; columns kcat (min^-1), KM (uM), and kcat/KM (uM^-1 min^-1).

raw_value_unit_evidence: Table 3. Steady state kinetic parameters using O2 as the varied substrate row WT-PHD2: kcat 8.0 +/- 0.7 min^-1; KM 530.0 +/- 90 uM; kcat/KM 0.015 +/- 0.001 uM^-1 min^-1.


column_label: Table 1. Steady state kinetics of WT-PHD2 and variants with varied [2OG]; row_label: T387A / paper row Thr387->Ala; columns kcat (min^-1), KM (uM), and kcat/KM (uM^-1 min^-1).

raw_value_unit_evidence: Table 1. Steady state kinetics of WT-PHD2 and variants with varied [2OG] row Thr387->Ala: kcat 32.9 +/- 1.4 min^-1; KM 12.0 +/- 1.6 uM; kcat/KM 2.7 +/- 0.3 uM^-1 min^-1.


column_label: Table 1. Steady state kinetics of WT-PHD2 and variants with varied [2OG]; row_label: T387N / paper row Thr387->Asn; columns kcat (min^-1), KM (uM), and kcat/KM (uM^-1 min^-1).

raw_value_unit_evidence: Table 1. Steady state kinetics of WT-PHD2 and variants with varied [2OG] row Thr387->Asn: kcat 1.0 +/- 0.1 min^-1; KM 0.7 +/- 0.1 uM; kcat/KM 1.5 +/- 0.2 uM^-1 min^-1.


column_label: Table 1. Steady state kinetics of WT-PHD2 and variants with varied [2OG]; row_label: WT-PHD2; columns kcat (min^-1), KM (uM), and kcat/KM (uM^-1 min^-1).

raw_value_unit_evidence: Table 1. Steady state kinetics of WT-PHD2 and variants with varied [2OG] row WT-PHD2: kcat 2.3 +/- 0.1 min^-1; KM 0.9 +/- 0.2 uM; kcat/KM 2.7 +/- 0.4 uM^-1 min^-1.


sequence_variant_note: Mutation signature D210E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +2, so it is treated as a source-provided variant sequence.


enzyme_display_name: Gibberellin 3-beta-dioxygenase 1

organism: Arabidopsis thaliana

enzyme: Gibberellin 3-beta-dioxygenase 1


enzyme_display_name: Gibberellin 3-beta-dioxygenase 2

enzyme: Gibberellin 3-beta-dioxygenase 2


enzyme_display_name: hyoscyamine (6S)-dioxygenase

enzyme: hyoscyamine (6S)-dioxygenase


enzyme_display_name: Gibberellin 3-beta-dioxygenase 2-1

enzyme: Gibberellin 3-beta-dioxygenase 2-1


enzyme_display_name: Phytanoyl-CoA dioxygenase, peroxisomal

substrate_name: phytanoyl-CoA (in presence of SCP2)

assay_conditions_summary: cofactor CoA

column_label: The official Cell article reports Michaelis-Menten kinetics in the presence of SCP-2 and gives KM = 29.5 +/- 1.7 uM, Kcat = 0.40 +/- 0.01 s^-1, and Kcat/KM = 1.34 x 10^4 M^-1 s^-1.

raw_value_unit_evidence: Km raw_value=29.5 +/- 1.7 raw_unit=uM

row_label: Prose segment: (3R,3S)-phytanoyl-CoA in presence of mature SCP-2

table_label: Cell Press article section: Kinetic Analyses of PAHX-Catalyzed Conversion of Phytanoyl-CoA

enzyme: Phytanoyl-CoA dioxygenase, peroxisomal

substrate: phytanoyl-CoA (in presence of SCP2)


substrate_name: hexadecanoyl-CoA (in presence of SCP2)

column_label: The official Cell article reports kinetic analysis of hexadecanoyl-CoA in the presence of SCP-2 with KM = 25.1 +/- 1 uM, Kcat = 0.044 +/- 0.0005 s^-1, and Kcat/KM = 1.75 x 10^3 M^-1 s^-1.

raw_value_unit_evidence: Km raw_value=25.1 +/- 1 raw_unit=uM

row_label: Prose segment: hexadecanoyl-CoA in presence of SCP-2

table_label: Cell Press article section: Hydroxylation of Straight-Chain Fatty Acyl-CoA Esters

substrate: hexadecanoyl-CoA (in presence of SCP2)


organism: Sphingobium herbicidovorans

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature R285A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; 303.15 K; buffer 100 mM imidazole

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'R285A'; column 'Range (uM)' = 200-4000; column 'Km (uM)' = 1550 +/- 220; column 'kcat (min^-1)' = 52 +/- 4; column 'kcat/Km (min^-1*uM^-1)' = 0.03.

normalized_value_unit_evidence: Km: printed Table 2 cell 1550 under the column head Km (uM); one uM is 0.001 mM, so 1550 / 1000 = 1.55 mM; the exported value is 1.55 mM. kcat: printed Table 2 cell 52 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 52 / 60 = 0.8666666666666667 s^-1; the exported value is 0.87 s^(-1). kcat/Km: printed Table 2 cell 0.03 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.03 * 1000 / 60 = 0.5 s^-1 mM^-1; the exported value is 0.5612903225806452 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row R285A: Km = 1550 uM (printed with its tolerance +/- 220); kcat = 52 min^-1 (printed with its tolerance +/- 4); kcat/Km = 0.03 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).

table_label: Table 2: Kinetic parameters of selected variant forms of RdpA and SdpA (Protein Science 2006, 15(6):1356-1368)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature F171A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'F171A'; column 'Range (uM)' = 200-4000; column 'Km (uM)' = 108 +/- 7; column 'kcat (min^-1)' = 175 +/- 2; column 'kcat/Km (min^-1*uM^-1)' = 1.62.

normalized_value_unit_evidence: Km: printed Table 2 cell 108 under the column head Km (uM); one uM is 0.001 mM, so 108 / 1000 = 0.108 mM; the exported value is 0.108 mM. kcat: printed Table 2 cell 175 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 175 / 60 = 2.9166666666666665 s^-1; the exported value is 2.9 s^(-1). kcat/Km: printed Table 2 cell 1.62 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 1.62 * 1000 / 60 = 27.000000000000004 s^-1 mM^-1; the exported value is 26.85185185185185 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row F171A: Km = 108 uM (printed with its tolerance +/- 7); kcat = 175 min^-1 (printed with its tolerance +/- 2); kcat/Km = 1.62 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature F171Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'F171Q'; column 'Range (uM)' = 62.5-4000; column 'Km (uM)' = 438 +/- 34; column 'kcat (min^-1)' = 203 +/- 4; column 'kcat/Km (min^-1*uM^-1)' = 0.46.

normalized_value_unit_evidence: Km: printed Table 2 cell 438 under the column head Km (uM); one uM is 0.001 mM, so 438 / 1000 = 0.438 mM; the exported value is 0.438 mM. kcat: printed Table 2 cell 203 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 203 / 60 = 3.3833333333333333 s^-1; the exported value is 3.38 s^(-1). kcat/Km: printed Table 2 cell 0.46 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.46 * 1000 / 60 = 7.666666666666668 s^-1 mM^-1; the exported value is 7.716894977168949 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row F171Q: Km = 438 uM (printed with its tolerance +/- 34); kcat = 203 min^-1 (printed with its tolerance +/- 4); kcat/Km = 0.46 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature I106A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'I106A'; column 'Range (uM)' = 500-4000; column 'Km (uM)' = 8900 +/- 2100; column 'kcat (min^-1)' = 238 +/- 42; column 'kcat/Km (min^-1*uM^-1)' = 0.03.

normalized_value_unit_evidence: Km: printed Table 2 cell 8900 under the column head Km (uM); one uM is 0.001 mM, so 8900 / 1000 = 8.9 mM; the exported value is 8.9 mM. kcat: printed Table 2 cell 238 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 238 / 60 = 3.966666666666667 s^-1; the exported value is 4.0 s^(-1). kcat/Km: printed Table 2 cell 0.03 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.03 * 1000 / 60 = 0.5 s^-1 mM^-1; the exported value is 0.449438202247191 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row I106A: Km = 8900 uM (printed with its tolerance +/- 2100); kcat = 238 min^-1 (printed with its tolerance +/- 42); kcat/Km = 0.03 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature V80A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'V80A'; column 'Range (uM)' = 200-4000; column 'Km (uM)' = 2300 +/- 1100; column 'kcat (min^-1)' = 248 +/- 56; column 'kcat/Km (min^-1*uM^-1)' = 0.11.

normalized_value_unit_evidence: Km: printed Table 2 cell 2300 under the column head Km (uM); one uM is 0.001 mM, so 2300 / 1000 = 2.3000000000000003 mM; the exported value is 2.3 mM. kcat: printed Table 2 cell 248 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 248 / 60 = 4.133333333333333 s^-1; the exported value is 4.13 s^(-1). kcat/Km: printed Table 2 cell 0.11 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.11 * 1000 / 60 = 1.8333333333333335 s^-1 mM^-1; the exported value is 1.7956521739130435 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row V80A: Km = 2300 uM (printed with its tolerance +/- 1100); kcat = 248 min^-1 (printed with its tolerance +/- 56); kcat/Km = 0.11 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature Q93A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'Q93A'; column 'Range (uM)' = 200-4000; column 'Km (uM)' = 2800 +/- 400; column 'kcat (min^-1)' = 260 +/- 21; column 'kcat/Km (min^-1*uM^-1)' = 0.09.

normalized_value_unit_evidence: Km: printed Table 2 cell 2800 under the column head Km (uM); one uM is 0.001 mM, so 2800 / 1000 = 2.8000000000000003 mM; the exported value is 2.8 mM. kcat: printed Table 2 cell 260 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 260 / 60 = 4.333333333333333 s^-1; the exported value is 4.33 s^(-1). kcat/Km: printed Table 2 cell 0.09 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.09 * 1000 / 60 = 1.5 s^-1 mM^-1; the exported value is 1.5464285714285715 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row Q93A: Km = 2800 uM (printed with its tolerance +/- 400); kcat = 260 min^-1 (printed with its tolerance +/- 21); kcat/Km = 0.09 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


enzyme_display_name: L-isoleucine 4-hydroxylase

organism: Bacillus mycoides

substrate_name: L-isoleucine

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -13, so it is treated as a source-provided variant sequence.

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

proof_lines: mutant N126H, pH 7, temperature not specified in the publication

enzyme: L-isoleucine 4-hydroxylase

substrate: L-isoleucine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T130K with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: mutant T130K, pH 7, 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.

column_label: Table 2 (The kinetic parameters of Ido using the substrates Ile and a-KG), enzyme row 'Bw Ido' whose Source column reads 'This work', substrate group Ile; column 'Km (mM)' = 2.38; column 'kcat (min-1)' = 28.83; column 'kcat/Km (min-1 mM-1)' = 12.15.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.38 mM; the printed Km column is already in mM, so no unit conversion applies and the exported value is 2.38 mM. kcat: printed Table 2 cell 28.83 min-1; 28.83 / 60 = 0.4805 s^-1, carried here at the exported precision as 0.481 s^-1. kcat/Km: printed Table 2 cell 12.15 min-1 mM-1; one min^-1 mM^-1 is 1 / 60 s^-1 mM^-1, so 12.15 / 60 = 0.2025 s^-1 mM^-1, and 0.2025 s^(-1)*mM^(-1) is the value this record installs.

raw_value_unit_evidence: Table 2, enzyme row Bw Ido, substrate group Ile: Km = 2.38 mM; kcat = 28.83 min-1; printed kcat/Km = 12.15 min-1 mM-1.

table_label: Table 2: The kinetic parameters of Ido using the substrates Ile and a-KG (Biotechnol Lett 2018, 40:1227-1235)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N126H/T130K with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: mutant N126H/T130K, pH 7, temperature not specified in the publication


column_label: Table 2 (The kinetic parameters of Ido using the substrates Ile and a-KG), enzyme row 'Bw Ido' whose Source column reads 'This work', substrate group a-KG; column 'Km (mM)' = 2.76; column 'kcat (min-1)' = 34.59; column 'kcat/Km (min-1 mM-1)' = 12.53.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.76 mM; the printed Km column is already in mM, so no unit conversion applies and the exported value is 2.76 mM. kcat: printed Table 2 cell 34.59 min-1; 34.59 / 60 = 0.5765 s^-1, carried here at the exported precision as 0.577 s^-1. kcat/Km: printed Table 2 cell 12.53 min-1 mM-1; one min^-1 mM^-1 is 1 / 60 s^-1 mM^-1, so 12.53 / 60 = 0.20883333333333332 s^-1 mM^-1, and 0.20883333333333332 s^(-1)*mM^(-1) is the value this record installs.

raw_value_unit_evidence: Table 2, enzyme row Bw Ido, substrate group a-KG: Km = 2.76 mM; kcat = 34.59 min-1; printed kcat/Km = 12.53 min-1 mM-1.


enzyme_display_name: xanthine dioxygenase

organism: Aspergillus nidulans

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q101A to reconstruct the assayed variant sequence.

enzyme: xanthine dioxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature N358A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q356A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K122A to reconstruct the assayed variant sequence.


substrate_name: xanthine

substrate: xanthine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D138A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C357A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E137A to reconstruct the assayed variant sequence.


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

column_label: Paper paragraph P37 states alpha-ketoadipic acid is a XanA cosubstrate and kinetic analyses gave kcat 7.6 s^-1 and Km 0.16 mM for this alternative cosubstrate.

normalized_value_unit_evidence: kcat normalized_value=7.6 normalized_unit=s^-1; Km normalized_value=0.16 normalized_unit=mM; kcat_over_km normalized_value=47.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7.6 raw_unit=s^-1; Km raw_value=0.16 raw_unit=mM; kcat/Km calculated from 7.6 s^-1 / 0.16 mM

row_label: E. coli-derived A. nidulans XanA with alpha-ketoadipic acid / 2-oxoadipate alternative cosubstrate

table_label: PMC author manuscript HTML, Results: alphaKG Analogues


column_label: Paper paragraph P31 states varied alphaKG concentrations gave Km 31.1 +/- 1.6 uM and kcat 66.5 s^-1 at 25 C, Figure 4A.

normalized_value_unit_evidence: kcat normalized_value=66.5 normalized_unit=s^-1; Km normalized_value=0.0311 normalized_unit=mM; kcat_over_km normalized_value=2138.2636655948554 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=66.5 raw_unit=s^-1; Km raw_value=31.1 +/- 1.6 raw_unit=uM; kcat/Km calculated from 66.5 s^-1 / 0.0311 mM

row_label: E. coli-derived A. nidulans XanA with varied alphaKG / 2-oxoglutarate

table_label: PMC author manuscript HTML, Results: Kinetic Analyses and Stoichiometry of XanA; Figure 4A


column_label: Paper paragraph P31 states varied xanthine concentrations gave Km 45.2 +/- 3.6 uM and kcat 71.4 s^-1, Figure 4B.

normalized_value_unit_evidence: kcat normalized_value=71.4 normalized_unit=s^-1; Km normalized_value=0.0452 normalized_unit=mM; kcat_over_km normalized_value=1579.6460176991152 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=71.4 raw_unit=s^-1; Km raw_value=45.2 +/- 3.6 raw_unit=uM; kcat/Km calculated from 71.4 s^-1 / 0.0452 mM

row_label: E. coli-derived A. nidulans XanA with varied xanthine

table_label: PMC author manuscript HTML, Results: Kinetic Analyses and Stoichiometry of XanA; Figure 4B


enzyme_display_name: [50S ribosomal protein L16]-arginine 3-hydroxylase

organism: Rhodothermus marinus

substrate_name: [50S ribosomal cyclic peptide 6KKPAEVRMGKGKG88-linker]-L-Arg82

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


enzyme: [50S ribosomal protein L16]-arginine 3-hydroxylase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q700X4 and applied mutation signature H208A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, variant row 'H208A'; column 'Range (uM)' = 500-4000; column 'Km (uM)' = 2900 +/- 960; column 'kcat (min^-1)' = 21 +/- 4; column 'kcat/Km (min^-1*uM^-1)' = 0.007.

normalized_value_unit_evidence: Km: printed Table 2 cell 2900 under the column head Km (uM); one uM is 0.001 mM, so 2900 / 1000 = 2.9 mM; the exported value is 2.9 mM. kcat: printed Table 2 cell 21 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 21 / 60 = 0.35 s^-1; the exported value is 0.35 s^(-1). kcat/Km: printed Table 2 cell 0.007 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.007 * 1000 / 60 = 0.11666666666666668 s^-1 mM^-1; the exported value is 0.12068965517241378 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, variant row H208A: Km = 2900 uM (printed with its tolerance +/- 960); kcat = 21 min^-1 (printed with its tolerance +/- 4); kcat/Km = 0.007 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q700X4 and applied mutation signature G97I/N98G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, variant row 'G97I/N98G'; column 'Range (uM)' = 250-4000; column 'Km (uM)' = 1100 +/- 270; column 'kcat (min^-1)' = 42 +/- 4.4; column 'kcat/Km (min^-1*uM^-1)' = 0.04.

normalized_value_unit_evidence: Km: printed Table 2 cell 1100 under the column head Km (uM); one uM is 0.001 mM, so 1100 / 1000 = 1.1 mM; the exported value is 1.1 mM. kcat: printed Table 2 cell 42 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 42 / 60 = 0.7 s^-1; the exported value is 0.7 s^(-1). kcat/Km: printed Table 2 cell 0.04 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.04 * 1000 / 60 = 0.6666666666666667 s^-1 mM^-1; the exported value is 0.6363636363636362 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, variant row G97I/N98G: Km = 1100 uM (printed with its tolerance +/- 270); kcat = 42 min^-1 (printed with its tolerance +/- 4.4); kcat/Km = 0.04 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q700X4 and applied mutation signature R207A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, variant row 'R207A'; column 'Range (uM)' = 250-4000; column 'Km (uM)' = 2500 +/- 400; column 'kcat (min^-1)' = 238 +/- 20; column 'kcat/Km (min^-1*uM^-1)' = 0.1.

normalized_value_unit_evidence: Km: printed Table 2 cell 2500 under the column head Km (uM); one uM is 0.001 mM, so 2500 / 1000 = 2.5 mM; the exported value is 2.5 mM. kcat: printed Table 2 cell 238 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 238 / 60 = 3.966666666666667 s^-1; the exported value is 3.97 s^(-1). kcat/Km: printed Table 2 cell 0.1 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.1 * 1000 / 60 = 1.666666666666667 s^-1 mM^-1; the exported value is 1.588 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, variant row R207A: Km = 2500 uM (printed with its tolerance +/- 400); kcat = 238 min^-1 (printed with its tolerance +/- 20); kcat/Km = 0.1 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q700X4 and applied mutation signature E69A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, variant row 'E69A'; column 'Range (uM)' = 31-4000; column 'Km (uM)' = 91 +/- 14; column 'kcat (min^-1)' = 241 +/- 8; column 'kcat/Km (min^-1*uM^-1)' = 2.65.

normalized_value_unit_evidence: Km: printed Table 2 cell 91 under the column head Km (uM); one uM is 0.001 mM, so 91 / 1000 = 0.091 mM; the exported value is 0.091 mM. kcat: printed Table 2 cell 241 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 241 / 60 = 4.016666666666667 s^-1; the exported value is 4.0 s^(-1). kcat/Km: printed Table 2 cell 2.65 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 2.65 * 1000 / 60 = 44.16666666666667 s^-1 mM^-1; the exported value is 43.956043956043956 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, variant row E69A: Km = 91 uM (printed with its tolerance +/- 14); kcat = 241 min^-1 (printed with its tolerance +/- 8); kcat/Km = 2.65 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, Wild type row; column 'Range (uM)' = 31-4000; column 'Km (uM)' = 161 +/- 20; column 'kcat (min^-1)' = 1010 +/- 44; column 'kcat/Km (min^-1*uM^-1)' = 6.24.

normalized_value_unit_evidence: Km: printed Table 2 cell 161 under the column head Km (uM); one uM is 0.001 mM, so 161 / 1000 = 0.161 mM; the exported value is 0.161 mM. kcat: printed Table 2 cell 1010 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 1010 / 60 = 16.833333333333332 s^-1; the exported value is 16.83 s^(-1). kcat/Km: printed Table 2 cell 6.24 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 6.24 * 1000 / 60 = 104.00000000000001 s^-1 mM^-1; the exported value is 104.53416149068322 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, Wild type row: Km = 161 uM (printed with its tolerance +/- 20); kcat = 1010 min^-1 (printed with its tolerance +/- 44); kcat/Km = 6.24 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


enzyme_display_name: uridine-5'-phosphate dioxygenase

organism: Streptomyces sp.

substrate_name: UMP

proof_lines: kcat is 92 min(-1) with 2-oxoglutarate as substrate. kcat is 76 min(-1) with UMP as substrate.

enzyme: uridine-5'-phosphate dioxygenase

substrate: UMP


enzyme_display_name: Uridine-5'-phosphate dioxygenase

organism: Amycolatopsis sp

proof_lines: kcat is 95 min(-1) with UMP as substrate. kcat is 78 min(-1) with 2-oxoglutarate as substrate. kcat is 9.0 min(-1) with pyruvate as substrate. kcat is 17 min(-1) with 2-oxoadipate as substrate.

enzyme: Uridine-5'-phosphate dioxygenase


substrate_name: pyruvate

substrate: pyruvate


organism: Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / CCUG 56400 / KCTC 2939 / LMG 18315 / NBRC 16415 / MH)

substrate_name: alpha-ketoglutarate (at pH 6.75 and 30 degrees Celsius)

column_label: PMID 16820480 Table 5, SdpA alpha-Ketoglutarate row, Km (uM) = 19.6 +/- 2.5.

normalized_value_unit_evidence: Km normalized_value=0.0196 mM.

raw_value_unit_evidence: Table 5 row SdpA / alpha-Ketoglutarate, Km column: 19.6 +/- 2.5 uM.

row_label: alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase / alpha-Ketoglutarate (8-1,000 uM)

table_label: Table 5. Kinetic parameters of alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase and alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase


organism: Delftia acidovorans

substrate_name: alpha-ketoglutarate (at pH 6 and 30 degrees Celsius)

assay_conditions_summary: pH 6

proof_lines: kcat is 65.2 min(-1) for dioxygenase activity with (RS)-2-(4-chlorophenoxy)propionate (at pH 6 and 30 degrees Celsius). kcat is 55.2 min(-1) for dioxygenase activity with R-2,4-DP (at pH 6 and 30 degrees Celsius). kcat is 50 min(-1) for dio

proof_lines: kcat is 114.2 min(-1) for dioxygenase activity with R-2,4-MCPP (at pH 6.75 and 30 degrees Celsius). kcat is 135.6 min(-1) for dioxygenase activity with alpha-ketoglutarate (at pH 6.75 and 30 degrees Celsius). kcat is 170.1 min(-1) for dioxy


substrate_name: alpha-ketoglutarate (at pH 6 and 25 degrees Celsius)

proof_lines: kcat is 50 min(-1) for dioxygenase activity with S-2,4-DP (at pH 6 and 25 degrees Celsius). kcat is 46 min(-1) for dioxygenase activity with S-2,4-MCPP (at pH 6 and 25 degrees Celsius). kcat is 36 min(-1) for dioxygenase activity with 2,4-D


substrate_name: 2,4-D (at pH 6 and 25 degrees Celsius)

substrate: 2,4-D (at pH 6 and 25 degrees Celsius)


column_label: Abstract oxygen sentence reports 159 microM for SdpA.

raw_value_unit_evidence: Km raw_value=159 raw_unit=microM

row_label: SdpA oxygen cosubstrate assay

table_label: PubMed abstract PMID 16820480


substrate_name: 2,4-dichlorophenoxyacetate (at pH 6 and 30 degrees Celsius)


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature N358A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; buffer 50 mM MOPS

column_label: Table 2; XanA sample row N358A; substrate column group 2-Oxoglutarate; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.

table_label: Table 2: Substrate, cosubstrate, and substrate analog kinetic parameters of XanA and selected variants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q101A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row Q101A; substrate column group 2-Oxoglutarate; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.

table_label: Table 2


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature Q356A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row Q356A; substrate column group 2-Oxoglutarate; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


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

column_label: Table 2; XanA sample row WT; substrate column group 2-Oxoglutarate; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.

row_label: WT


column_label: PMID 16820480 Table 5, SdpA (S)-Mecoprop row, Km (uM) = 132 +/- 17.7.

normalized_value_unit_evidence: Km normalized_value=0.132 mM.

raw_value_unit_evidence: Table 5 row SdpA / (S)-Mecoprop, Km column: 132 +/- 17.7 uM.

row_label: alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase / (S)-Mecoprop (50-2,000 uM)


column_label: PMID 16820480 Table 5, SdpA (S)-Dichlorprop row, Km (uM) = 494.8 +/- 43.9.

normalized_value_unit_evidence: Km normalized_value=0.4948 mM; exported 0.495 mM is rounded from the printed cell.

raw_value_unit_evidence: Table 5 row SdpA / (S)-Dichlorprop, Km column: 494.8 +/- 43.9 uM.

row_label: alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase / (S)-Dichlorprop (120-2,000 uM)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature F171A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'F171A'; column 'Range (uM)' = 200-4000; column 'Km (uM)' = 108 +/- 7; column 'kcat (min^-1)' = 175 +/- 2; column 'kcat/Km (min^-1*uM^-1)' = 1.62.

normalized_value_unit_evidence: Km: printed Table 2 cell 108 under the column head Km (uM); one uM is 0.001 mM, so 108 / 1000 = 0.108 mM; the exported value is 0.108 mM. kcat: printed Table 2 cell 175 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 175 / 60 = 2.9166666666666665 s^-1; the exported value is 2.9 s^(-1). kcat/Km: printed Table 2 cell 1.62 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 1.62 * 1000 / 60 = 27.000000000000004 s^-1 mM^-1; the exported value is 26.85185185185185 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row F171A: Km = 108 uM (printed with its tolerance +/- 7); kcat = 175 min^-1 (printed with its tolerance +/- 2); kcat/Km = 1.62 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).