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


enzyme_display_name: taurine dioxygenase

organism: Escherichia coli

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

mutation_type: substitution

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.

data_origin: experimental

enzyme: taurine dioxygenase

status: corrected

source: oed


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.


mutation_signature: Unknown

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

column_label: Table 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

verification_status: verified

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

status: verified


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


verification_status: unverified

status: unverified


substrate_name: Taurine

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

substrate: Taurine


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.


enzyme_display_name: gibberellin 3beta-dioxygenase

organism: Pisum sativum

substrate_name: 2-Oxoglutarate; O2; Gibberellin A20

kcat_display: Not reported

kcat_over_km_display: Not reported

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

sequence_source: multiple

enzyme: gibberellin 3beta-dioxygenase

substrate: 2-Oxoglutarate; O2; Gibberellin A20


organism: Triticum aestivum

substrate_name: Gibberellin A9; 2-Oxoglutarate; O2

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

substrate: Gibberellin A9; 2-Oxoglutarate; O2


substrate_name: 2-Oxoglutarate; O2; Taurine

substrate: 2-Oxoglutarate; O2; Taurine


enzyme_display_name: fatty acid alpha-dioxygenase

organism: Nicotiana tabacum

substrate_name: oleic acid

source_db: brenda

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

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

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

enzyme: fatty acid alpha-dioxygenase

substrate: oleic acid

source: brenda


substrate_name: linolenic acid

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

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

substrate: linolenic acid


substrate_name: linoleic acid

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

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


enzyme_display_name: tryptophan 2-monooxygenase

organism: Pseudomonas savastanoi

substrate_name: L-Tryptophan

kcat_over_km_origin: calculated

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

enzyme: tryptophan 2-monooxygenase

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)

source_db: uniprot

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)

source: uniprot


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)


smiles: O=O


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.


enzyme_display_name: peptide-aspartate beta-dioxygenase

organism: Homo sapiens

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

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

source_databases_merged: brenda skid

enzyme: peptide-aspartate beta-dioxygenase


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).


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


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


enzyme_display_name: UniProt Q9NWT6

source_db: skid

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

source_databases_merged: skid uniprot

enzyme: UniProt Q9NWT6

source: skid


enzyme_display_name: Hypoxia-inducible factor 1-alpha inhibitor


enzyme: Hypoxia-inducible factor 1-alpha inhibitor


substrate_name: ascorbate

substrate: ascorbate


enzyme_display_name: hyoscyamine (6S)-dioxygenase

organism: Anisodus acutangulus

substrate_name: L-hyoscyamine

assay_conditions_summary: pH 8

enzyme: hyoscyamine (6S)-dioxygenase

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

ki_unit: mM

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.

assay_conditions_summary: pH 7


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


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

km_display: Not reported

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


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

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


organism: Hyoscyamus niger


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_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.

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

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

source_databases_merged: brenda uniprot


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.


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).


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 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).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature R285A 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 '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).


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

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, Wild type row; column 'Range (uM)' = 100-4000; column 'Km (uM)' = 380 +/- 28; column 'kcat (min^-1)' = 252 +/- 5; column 'kcat/Km (min^-1*uM^-1)' = 0.66.

normalized_value_unit_evidence: Km: printed Table 2 cell 380 under the column head Km (uM); one uM is 0.001 mM, so 380 / 1000 = 0.38 mM; the exported value is 0.38 mM. kcat: printed Table 2 cell 252 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 252 / 60 = 4.2 s^-1; the exported value is 4.2 s^(-1). kcat/Km: printed Table 2 cell 0.66 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.66 * 1000 / 60 = 11.000000000000002 s^-1 mM^-1; the exported value is 11.052631578947368 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, Wild type row: Km = 380 uM (printed with its tolerance +/- 28); kcat = 252 min^-1 (printed with its tolerance +/- 5); kcat/Km = 0.66 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: PMCID PMC2242530 Table 2 image 1356tbl2.jpg; row SdpA E69A; columns Km, kcat, and kcat/Km for the matching mecoprop enantiomer.

raw_value_unit_evidence: Table 2 SdpA E69A with (S)-mecoprop: Km 91 +/- 14 uM, kcat 241 +/- 8 min^-1, kcat/Km 2.65 min^-1 uM^-1.

row_label: SdpA E69A with (S)-2-(4-chloro-2-methylphenoxy)propanoate

table_label: Table 2. Kinetic parameters of selected variant forms of RdpA and SdpA


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.

row_label: Table 2, SdpA block, (S)-mecoprop columns, variant row G97I/N98G


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.

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).


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.

row_label: Table 2, SdpA block, (S)-mecoprop columns, variant row R207A


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.

row_label: Table 2, SdpA block, (S)-mecoprop columns, Wild type row


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

column_label: Table 2; XanA sample row C357A; 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.


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

column_label: Table 2; XanA sample row D138A; 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.


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature C357A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row C357A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature D138A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row D138A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature E137A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row E137A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature K122A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row K122A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


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


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature Q101A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row Q101A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


column_label: Table 2; XanA sample row Q356A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


column_label: Table 2; XanA sample row WT; substrate column group 9-methylxanthine; 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.


column_label: PMID 16820480 Table 5, RdpA alpha-Ketoglutarate row, Km (uM) = 2.8 +/- 0.8.

normalized_value_unit_evidence: Km normalized_value=0.0028 mM; exported 0.003 mM is rounded from the printed cell.

raw_value_unit_evidence: Table 5 row RdpA / alpha-Ketoglutarate, Km column: 2.8 +/- 0.8 uM.

row_label: alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase / alpha-Ketoglutarate (7-1,900 uM)


proof_lines:
pH 6.8, 30°C
Raw SKiD Env: Temp=30°C, pH=6.8


column_label: PMID 16820480 Table 5, RdpA (R)-Dichlorprop row, Km (uM) = 163.7 +/- 13.5.

normalized_value_unit_evidence: Km normalized_value=0.1637 mM; exported 0.164 mM is rounded from the printed cell.

raw_value_unit_evidence: Table 5 row RdpA / (R)-Dichlorprop, Km column: 163.7 +/- 13.5 uM.

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


column_label: Table 2; XanA sample row C357A; substrate column group xanthine; 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.


column_label: Table 2; XanA sample row D138A; substrate column group xanthine; 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.


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

column_label: Table 2; XanA sample row E137A; substrate column group xanthine; 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.


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

column_label: Table 2; XanA sample row K122A; substrate column group xanthine; 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.


column_label: Table 2; XanA sample row N358A; substrate column group xanthine; 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.


column_label: Table 2; XanA sample row Q101A; substrate column group xanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


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

column_label: Table 2; XanA sample row Q356A; substrate column group xanthine; 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.


column_label: Table 2; XanA sample row WT; substrate column group xanthine; 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.


column_label: Table 2; XanA sample row E137A; 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.


column_label: Table 2; XanA sample row K122A; 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.


organism: Bacillus thuringiensis

substrate_name: L-leucine

column_label: PMID 22448874 PDF page 7, printed page 102, Table 2, L-Leu row, IDO column: Km 2.3 +/- 0.4 mM; kcat 7.5 +/- 0.3 min^-1; kcat/Km 3.2 +/- 0.4 mM^-1 min^-1.

normalized_value_unit_evidence: Table 2 L-Leu/IDO: Km normalized_value=2.3 normalized_unit=mM; kcat normalized_value=0.125 normalized_unit=s^-1; printed kcat/Km normalized_value=0.05333333333333334 normalized_unit=s^-1*mM^-1. The paper's min^-1 footnote requires division by 60.

raw_value_unit_evidence: L-Leu/IDO: Km raw_value=2.3 +/- 0.4 raw_unit=mM; kcat raw_value=7.5 +/- 0.3 raw_unit=min^-1; kcat/Km raw_value=3.2 +/- 0.4 raw_unit=mM^-1*min^-1.

row_label: L-Leu; IDO column

table_label: Table 2. Kinetic parameters of L-amino acid hydroxylation (PDF page 7 of 9; printed page 102)

substrate: L-leucine


substrate_name: L-Methionine

column_label: PMID 22448874 PDF page 7, printed page 102, Table 2, L-Met row, IDO column: Km 3.2 +/- 0.3 mM; kcat 33 +/- 1 min^-1; kcat/Km 10 +/- 1 mM^-1 min^-1.

normalized_value_unit_evidence: Table 2 L-Met/IDO: Km normalized_value=3.2 normalized_unit=mM; kcat normalized_value=0.55 normalized_unit=s^-1; printed kcat/Km normalized_value=0.16666666666666666 normalized_unit=s^-1*mM^-1. The paper's min^-1 footnote requires division by 60.

raw_value_unit_evidence: L-Met/IDO: Km raw_value=3.2 +/- 0.3 raw_unit=mM; kcat raw_value=33 +/- 1 raw_unit=min^-1; kcat/Km raw_value=10 +/- 1 raw_unit=mM^-1*min^-1.

row_label: L-Met; IDO column

substrate: L-Methionine


substrate_name: L-Isoleucine

substrate: L-Isoleucine


substrate_name: (RS)-2-(m-chlorophenoxy)propionate (at pH 6 and 25 degrees Celsius)


substrate_name: S-2,4-MCPP (at pH 6.75 and 30 degrees Celsius)

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


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

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


substrate_name: Unknown


enzyme_display_name: 3-mercaptopropionate dioxygenase

organism: Cupriavidus necator

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

column_label: Primary article prose immediately before Figure 4 gives the 3MP row; Figure 4 caption gives CdoA 3MP substrate concentration range and assay conditions.

normalized_value_unit_evidence: CSV values match after unit normalization: kcat 0.82 s^-1, Km 5.7 mM, kcat/Km 0.143859649122807 s^-1 mM^-1, matching rounded paper 0.144.

raw_value_unit_evidence: Paper reports CdoA with 3MP: maximal specific activity 2.2 umol 3SP/mg protein/min, Km 5.7 mM, kcat 0.82 s^-1, kcat/Km 0.144 s^-1 mM^-1.

row_label: CdoA with 3MP

table_label: PMC article prose, Results: Characterization of CdoA

enzyme: 3-mercaptopropionate dioxygenase


enzyme_display_name: UniProt Q9GZT9

organism: Homo sapiens

enzyme: UniProt Q9GZT9


sequence_variant_note: Mutation signature L27I/E80D/G169H/S182D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Prolyl hydroxylase EGLN2

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

enzyme: Prolyl hydroxylase EGLN2


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


organism: Pseudomonas aeruginosa


enzyme_display_name: mRNA N1-methyladenine demethylase

organism: Escherichia coli

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

proof_lines: mutant enzyme D135I, pH and temperature not specified in the publication

enzyme: mRNA N1-methyladenine demethylase


proof_lines: mutant enzyme D135N, pH and temperature not specified in the publication


proof_lines: mutant enzyme E136L, pH and 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, pH and temperature not specified in the publication


enzyme_display_name: ectoine hydroxylase

organism: Virgibacillus salexigens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A163C/S244C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

enzyme: ectoine hydroxylase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N261A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A163C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S244C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S205A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P198A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F263Y with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V265T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V265A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S165A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F242Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V265L to reconstruct the assayed variant sequence.


enzyme_display_name: isoeugenol monooxygenase

organism: Pseudomonas putida

substrate_name: isoeugenol

enzyme: isoeugenol monooxygenase

substrate: isoeugenol


enzyme_display_name: validamycin A dioxygenase

organism: Streptomyces hygroscopicus subsp. limoneus

proof_lines: pH 7.2, 30°C, obtained from Hanes-Woolf plot

proof_lines: kcat is 0.97 min(-1) for validamycin A as substrate (at pH 7.2).

enzyme: validamycin A dioxygenase


substrate_name: validamycin A

substrate: validamycin A


organism: Streptomyces coelicolor

substrate_name: ectoine

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

substrate: ectoine


enzyme_display_name: L-proline cis-4-hydroxylase

organism: Sinorhizobium meliloti

substrate_name: L-homophenylalanine

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

enzyme: L-proline cis-4-hydroxylase

substrate: L-homophenylalanine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W40M to reconstruct the assayed variant sequence.

proof_lines: 20°C, pH not specified in the publication, mutant enzyme W40M


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W40M/I103L to reconstruct the assayed variant sequence.

proof_lines: 20°C, pH not specified in the publication, mutant enzyme W40M/I103L


organism: Sphingopyxis alaskensis

source_databases_merged: brenda skid uniprot


column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row S. alaskensis | column Km [mM 2-oxoglutarate] = 2.7 mM 2-oxoglutarate

normalized_value_unit_evidence: km 2.7 mM

raw_value_unit_evidence: km 2.7 mM 2-oxoglutarate

row_label: S. alaskensis


proof_lines: kcat is 7.7 sec(-1) for ectoin as substrate (at pH 7.5 and 32 degrees Celsius).


organism: Halomonas elongata

proof_lines: kcat is 2.8 sec(-1) for ectoin as substrate (at pH 8 and 32 degrees Celsius).


organism: Mesorhizobium loti

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5
kcat is 24 sec(-1).


proof_lines:
pH 7.5, 25°C
kcat is 25 sec(-1).


enzyme_display_name: Ectoine dioxygenase

organism: Stutzerimonas stutzeri (strain A1501)

substrate_name: 2-oxoglutarate (at pH 7.5 and 35 degrees Celsius)

proof_lines: kcat is 8.9 sec(-1) for ectoin as substrate (at pH 7.5 and 35 degrees Celsius).

enzyme: Ectoine dioxygenase


substrate_name: ectoine (at pH 7.5 and 35 degrees Celsius)


enzyme_display_name: Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3

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


organism: Streptantibioticus cattleyicolor

substrate_name: L-proline

column_label: Official Springer Table 2 row ScaEctD / L-Pro gives Km (mM)=17 +/- 2.2 and kcat (s^-1)=1.1 x 10^-1 +/- 0.1 x 10^-1.

normalized_value_unit_evidence: Km normalized_value=17.0 normalized_unit=mM; kcat normalized_value=0.11 normalized_unit=s^-1.

raw_value_unit_evidence: Km raw_value=17 +/- 2.2 raw_unit=mM; kcat raw_value=1.1 x 10^-1 +/- 0.1 x 10^-1 raw_unit=s^-1

row_label: ScaEctD / L-Pro

table_label: Table 2, Kinetic parameters of hydroxylases for ectoine and l-Pro hydroxylation

substrate: L-proline


enzyme_display_name: L-proline trans-4-hydroxylase

organism: Streptomyces griseoviridis

enzyme: L-proline trans-4-hydroxylase


enzyme_display_name: mRNA N6-methyladenine demethylase

substrate_name: 3-Methyluracil in RNA; 2-Oxoglutarate; O2

proof_lines: kcat is 8.78 min(-1) for m(7)Gppp(m6A(m))CA mRNA. kcat is 7.77 min(-1) for m(7)Gppp(m6A)CA mRNA. kcat is 0.54 min(-1) for GG(m6A)CU mRNA. kcat is 0.46 min(-1) for m(7)GpppAC(m6) mRNA.

enzyme: mRNA N6-methyladenine demethylase


substrate_name: L-homoectoine

proof_lines: kcat is 1.2 sec(-1) for ectoin as substrate (at pH 8 and 40 degrees Celsius).

substrate: L-homoectoine


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

substrate: Unknown


organism: Alkalilimnicola ehrlichii

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. ehrlichii | column kcat [s^-1] = 1.2 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. ehrlichii | column Km [mM ectoine] = 9.0 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. ehrlichii | column kcat/Km [mM^-1 s^-1] = 0.13 mM^-1 s^-1

raw_value_unit_evidence: kcat 1.2 s^-1; km 9.0 mM ectoine; kcat_over_km 0.13 mM^-1 s^-1

row_label: A. ehrlichii


column_label: Table 2 row A. ehrlichii, column K_m [mM 2-oxoglutarate], reports 5.0+/-0.3.

raw_value_unit_evidence: Km raw_value=5.0 uncertainty=+/-0.3 raw_unit=mM

table_label: PMC3979721 Table 2, Kinetic parameters of the analyzed ectoine hydroxylases


table_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases


enzyme_display_name: fatty acid alpha-dioxygenase

organism: Lathyrus oleraceus

substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

enzyme: fatty acid alpha-dioxygenase

substrate: lauric acid


organism: Acidiphilium cryptum

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. cryptum | column kcat [s^-1] = 3.4 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. cryptum | column Km [mM ectoine] = 10.0 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. cryptum | column kcat/Km [mM^-1 s^-1] = 0.34 mM^-1 s^-1

raw_value_unit_evidence: kcat 3.4 s^-1; km 10.0 mM ectoine; kcat_over_km 0.34 mM^-1 s^-1

row_label: A. cryptum


column_label: Table 2 row A. cryptum, column K_m [mM 2-oxoglutarate], reports 4.1+/-0.4.

raw_value_unit_evidence: Km raw_value=4.1 uncertainty=+/-0.4 raw_unit=mM


organism: Oryza sativa subsp. japonica

column_label: Full text reports the FLO7 homolog displayed Km 0.55 mM and Vmax 0.89 mM/min/uM enzyme for 2OA.

raw_value_unit_evidence: Km raw_value=0.55 mM raw_unit=mM

row_label: Oryza sativa FLO7 homolog / 2-oxoadipate

table_label: PMC full text kinetic prose PMID 32523014


column_label: Official Springer Table 2 row HeEctD / L-Pro gives Km (mM)=5.5 +/- 0.6, kcat (s^-1)=2.9 x 10^-2 +/- 0.1 x 10^-2, and kcat/Km (s^-1 mM^-1)=5.3 x 10^-3.

normalized_value_unit_evidence: Km normalized_value=5.5 normalized_unit=mM; kcat normalized_value=0.029 normalized_unit=s^-1; kcat_over_km paper_normalized_value=0.0053 normalized_unit=s^-1*mM^-1; exported derived value=0.005272727272727273 is rounding-consistent with the printed table values.

raw_value_unit_evidence: Km raw_value=5.5 +/- 0.6 raw_unit=mM; kcat raw_value=2.9 x 10^-2 +/- 0.1 x 10^-2 raw_unit=s^-1; kcat_over_km raw_value=5.3 x 10^-3 raw_unit=s^-1 mM^-1

row_label: HeEctD / L-Pro


enzyme_display_name: 2-oxoethane-1-sulfonamide synthase

organism: Streptomyces sp

substrate_name: L-cysteine

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

enzyme: 2-oxoethane-1-sulfonamide synthase

substrate: L-cysteine


enzyme_display_name: UniProt O75164

organism: Homo sapiens

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt O75164


enzyme_display_name: Gibberellin 2-beta-dioxygenase 1

organism: Pisum sativum

column_label: Abstract reports PsGA2OX1 displayed a Km of 0.024 microM and Vmax of 4.4 pkat/mg toward GA20.

raw_value_unit_evidence: Km raw_value=0.024 microM raw_unit=microM

row_label: Recombinant Pisum sativum PsGA2OX1 / GA20

table_label: PubMed XML abstract PMID 16181493

enzyme: Gibberellin 2-beta-dioxygenase 1


organism: Streptomyces cattleya

column_label: Official Springer Table 2 row ScaEctD / Ectoine gives Km (mM)=1.7 +/- 0.1, kcat (s^-1)=5.5 x 10^-1 +/- 0.1 x 10^-1, and kcat/Km (s^-1 mM^-1)=3.3 x 10^-1.

normalized_value_unit_evidence: Km normalized_value=1.7 normalized_unit=mM; kcat normalized_value=0.55 normalized_unit=s^-1; kcat_over_km paper_normalized_value=0.33 normalized_unit=s^-1*mM^-1; exported derived value=0.3235294117647059 is rounding-consistent with the printed table values.

raw_value_unit_evidence: Km raw_value=1.7 +/- 0.1 raw_unit=mM; kcat raw_value=5.5 x 10^-1 +/- 0.1 x 10^-1 raw_unit=s^-1; kcat_over_km raw_value=3.3 x 10^-1 raw_unit=s^-1 mM^-1

row_label: ScaEctD / Ectoine


enzyme_display_name: hyoscyamine (6S)-dioxygenase

organism: Hyoscyamus niger

substrate_name: L-hyoscyamine

enzyme: hyoscyamine (6S)-dioxygenase

substrate: L-hyoscyamine


enzyme_display_name: Phytanoyl-CoA dioxygenase, peroxisomal

enzyme: Phytanoyl-CoA dioxygenase, peroxisomal


enzyme_display_name: Gibberellin 3-beta-dioxygenase 4

organism: Arabidopsis thaliana

enzyme: Gibberellin 3-beta-dioxygenase 4


organism: Sphingopyxis alaskensis

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row S. alaskensis | column kcat [s^-1] = 1.2 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row S. alaskensis | column Km [mM ectoine] = 9.8 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row S. alaskensis | column kcat/Km [mM^-1 s^-1] = 0.12 mM^-1 s^-1

raw_value_unit_evidence: kcat 1.2 s^-1; km 9.8 mM ectoine; kcat_over_km 0.12 mM^-1 s^-1


organism: Paenibacillus lautus

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row P. lautus | column kcat [s^-1] = 1.6 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row P. lautus | column Km [mM ectoine] = 9.5 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row P. lautus | column kcat/Km [mM^-1 s^-1] = 0.17 mM^-1 s^-1

raw_value_unit_evidence: kcat 1.6 s^-1; km 9.5 mM ectoine; kcat_over_km 0.17 mM^-1 s^-1

row_label: P. lautus


enzyme_display_name: Alpha-ketoglutarate-dependent xanthine dioxygenase xanA

organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

substrate_name: 9-methylxanthine (at 25 degrees Celsius)

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


organism: Virgibacillus salexigens

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row V. salexigens | column kcat [s^-1] = 7.7 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row V. salexigens | column Km [mM ectoine] = 5.9 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row V. salexigens | column kcat/Km [mM^-1 s^-1] = 1.31 mM^-1 s^-1

raw_value_unit_evidence: kcat 7.7 s^-1; km 5.9 mM ectoine; kcat_over_km 1.31 mM^-1 s^-1

row_label: V. salexigens


organism: Mesorhizobium loti

proof_lines:
Mesorhizobium loti
L-proline cis-4-hydroxylase
L-proline


enzyme_display_name: 4-chlorophenylacetate 3,4-dioxygenase

organism: Pseudomonas sp.

substrate_name: ferrocytochrome c

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

assay_conditions_summary: cofactor NADH

enzyme: 4-chlorophenylacetate 3,4-dioxygenase

substrate: ferrocytochrome c


substrate_name: reduced 2,6-dichlorophenolindophenol

substrate: reduced 2,6-dichlorophenolindophenol


substrate_name: NADH

substrate: NADH


organism: Sinorhizobium meliloti


enzyme_display_name: alkyl sulfatase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: alpha-ketoglutarate (at pH 7 and 25 degrees Celsius)

proof_lines: kcat is 21.8 min(-1) with alpha-ketoglutarate and 2-EHS as substrates (at pH 7 and 25 degrees Celsius).

enzyme: alkyl sulfatase


enzyme_display_name: 4-sulfobenzoate 3,4-dioxygenase

organism: Comamonas testosteroni

enzyme: 4-sulfobenzoate 3,4-dioxygenase


enzyme_display_name: naphthalene 1,2-dioxygenase

organism: Corynebacterium renale

enzyme: naphthalene 1,2-dioxygenase


substrate_name: Naphthalene

substrate: Naphthalene


enzyme_display_name: phthalate 4,5-dioxygenase

substrate_name: terephthalate

column_label: Table 1 columns substrate, kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1), and coupling; row Terephthalate.

normalized_value_unit_evidence: Km 90 uM = 0.09 mM; kcat 2.0 s^-1; same-row central-value ratio 2.0/0.09 = 22.22222222222222 s^-1*mM^-1, matching table-rounded 22 mM^-1 s^-1.

raw_value_unit_evidence: Table 1 row Terephthalate reports kcat 2.0 +/- 0.1 s^-1, Km 90 +/- 12 uM, kcat/Km 22 +/- 4 mM^-1 s^-1, coupling 5.0 +/- 0.2.

row_label: Terephthalate

table_label: Table 1: Apparent steady-state kinetic parameters of PDOKF1 for different substrates

enzyme: phthalate 4,5-dioxygenase

substrate: terephthalate


substrate_name: Phthalate

column_label: Table 1 columns substrate, kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1), and coupling; row Phthalate.

raw_value_unit_evidence: Table 1 row Phthalate reports kcat 2.1 +/- 0.1 s^-1, Km 3.6 +/- 0.4 uM, kcat/Km 583 +/- 87 mM^-1 s^-1, coupling 1.0 +/- 0.4.

row_label: Phthalate

substrate: Phthalate


organism: Streptomyces griseoviridis


enzyme_display_name: taurine dioxygenase

organism: Escherichia coli

enzyme: taurine dioxygenase


substrate_name: taurine

substrate: taurine


substrate_name: MOPS

substrate: MOPS


substrate_name: pentanesulfonic acid

smiles: CCCCCS(=O)(=O)[O-]

substrate: pentanesulfonic acid


substrate_name: butanesulfonic acid

smiles: CCCCS(=O)(=O)O

substrate: butanesulfonic acid


substrate_name: hexanesulfonic acid

smiles: CCCCCCS(=O)(=O)O

substrate: hexanesulfonic acid


enzyme_display_name: peptide-aspartate beta-dioxygenase

organism: Bos taurus

enzyme: peptide-aspartate beta-dioxygenase


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


organism: Sphingomonas sp.

substrate_name: biphenyl

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM potassium phosphate; cofactor NADH

proof_lines: at 30°C in reaction mixtures containing 0.00013 mM ht-PhnI and 0.5 mM NADH in 50 mM potassium phosphate buffer, pH 7.0

substrate: biphenyl


enzyme_display_name: UniProt P39662

organism: Cupriavidus necator

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

enzyme: UniProt P39662


enzyme_display_name: Flavohemoprotein

organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

substrate_name: NO

smiles: [No]

enzyme: Flavohemoprotein

substrate: NO


enzyme_display_name: tryptophan 2-monooxygenase

organism: Pseudomonas savastanoi

substrate_name: L-tryptophan

enzyme: tryptophan 2-monooxygenase

substrate: L-tryptophan


proof_lines: pH 8.3, 25°C, cosubstrate: O2, wild-type


substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens

substrate_name: DLDLEALAPYIPADDDFQL

substrate: DLDLEALAPYIPADDDFQL


proof_lines: wild type isoform PHD2, at pH 7.0 and 37°C


substrate_name: tryptophan

substrate: tryptophan


enzyme_display_name: persulfide dioxygenase

substrate_name: S-sulfanylglutathione

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

enzyme: persulfide dioxygenase

substrate: S-sulfanylglutathione


enzyme_display_name: cytochrome-c3 hydrogenase

organism: Nitratidesulfovibrio vulgaris

substrate_name: ferricytochrome c

enzyme: cytochrome-c3 hydrogenase

substrate: ferricytochrome c


substrate_name: mutant cytochrome c3 Y65A

substrate: mutant cytochrome c3 Y65A


substrate_name: mutant cytochrome c3 K10M

substrate: mutant cytochrome c3 K10M


substrate_name: mutant cytochrome c3 K26M

substrate: mutant cytochrome c3 K26M


substrate_name: mutant cytochrome c3 Y66L

substrate: mutant cytochrome c3 Y66L


enzyme_display_name: protocatechuate 3,4-dioxygenase

proof_lines: apparent Ki, inhibition is not freely reversible

enzyme: protocatechuate 3,4-dioxygenase


enzyme_display_name: 2,3-dihydroxybenzoate 3,4-dioxygenase

enzyme: 2,3-dihydroxybenzoate 3,4-dioxygenase


substrate_name: D,L-3-phenyl-2-hydrazinopropanoic acid

substrate: D,L-3-phenyl-2-hydrazinopropanoic acid


substrate_name: L-alanine

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

substrate: L-alanine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


enzyme_display_name: 3-carboxyethylcatechol 2,3-dioxygenase

enzyme: 3-carboxyethylcatechol 2,3-dioxygenase


substrate_name: 2,3-dihydroxycinnamic acid

substrate: 2,3-dihydroxycinnamic acid


enzyme_display_name: UniProt P20586

organism: Pseudomonas aeruginosa

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=7.5

enzyme: UniProt P20586


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=8


enzyme_display_name: UniProt Q83XK4

organism: Methylophaga aminisulfidivorans

substrate_name: indole

enzyme: UniProt Q83XK4

substrate: indole


enzyme_display_name: UniProt O15229

substrate_name: NADPH

enzyme: UniProt O15229

substrate: NADPH


enzyme_display_name: catechol 1,2-dioxygenase

organism: Acinetobacter radioresistens

substrate_name: catechol

enzyme: catechol 1,2-dioxygenase

substrate: catechol


proof_lines: mutant enzyme A72G, in100 mM Tris-HCl pH 8.5, temperature not specified in the publication


proof_lines:
pH 8.0, 35°C, mutant A72S
mutant A72S


enzyme_display_name: coenzyme F420 hydrogenase

organism: Methanobacterium formicicum

substrate_name: coenzyme F420

enzyme: coenzyme F420 hydrogenase

substrate: coenzyme F420


substrate_name: coenzyme F0

substrate: coenzyme F0


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: methyl viologen

substrate: methyl viologen


enzyme_display_name: gibberellin 2beta-dioxygenase

organism: Phaseolus vulgaris

substrate_name: alpha-ketoglutarate

enzyme: gibberellin 2beta-dioxygenase

substrate: alpha-ketoglutarate


enzyme_display_name: cyclohexanone monooxygenase

organism: Acinetobacter sp.

substrate_name: cis-hex-2-enyl phenyl selenide

enzyme: cyclohexanone monooxygenase

substrate: cis-hex-2-enyl phenyl selenide


substrate_name: 2-methylcyclohexyl boronic acid

substrate: 2-methylcyclohexyl boronic acid


substrate_name: phenyl propargyl selenide

substrate: phenyl propargyl selenide


substrate_name: n-Octylboronic acid

smiles: B(CCCCCCCC)(O)O

substrate: n-Octylboronic acid


substrate_name: n-Butylboronic acid

smiles: B(CCCC)(O)O

substrate: n-Butylboronic acid


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


substrate_name: phenylboronic acid

substrate: phenylboronic acid


substrate_name: Phenyl methyl selenide

substrate: Phenyl methyl selenide


substrate_name: Phenyl allyl sulfide

substrate: Phenyl allyl sulfide


substrate_name: Thiane sulfoxide

substrate: Thiane sulfoxide


substrate_name: ethyl p-tolyl sulfide

substrate: ethyl p-tolyl sulfide


substrate_name: triethyl phosphite

smiles: CCOP(OCC)OCC

substrate: triethyl phosphite


substrate_name: Iodide

substrate: Iodide


enzyme_display_name: UniProt C0STX7

organism: Rhodococcus sp. HI-31

substrate_name: cyclohexanone

enzyme: UniProt C0STX7

substrate: cyclohexanone


substrate_name: NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A245G/A288V with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


enzyme_display_name: 3-hydroxybenzoate 4-monooxygenase

organism: Comamonas testosteroni

substrate_name: m-Hydroxybenzoate

enzyme: 3-hydroxybenzoate 4-monooxygenase

substrate: m-Hydroxybenzoate


enzyme_display_name: UniProt Q0SFK6

organism: Rhodococcus jostii

enzyme: UniProt Q0SFK6


substrate_name: NADH

substrate: NADH


organism: Methanothermobacter thermautotrophicus

substrate_name: coenzyme F420

substrate: coenzyme F420


substrate_name: coenzyme F0

proof_lines: equal turnover in reverse reaction under anaerobic conditions

substrate: coenzyme F0


substrate_name: methyl viologen

proof_lines:
pH 7.2
pH 9

substrate: methyl viologen


smiles: [HH]

assay_conditions_summary: pH 9

proof_lines:
+ methyl viologen, pH 9
+ coenzyme F0, pH 7.2


enzyme_display_name: catechol 2,3-dioxygenase

organism: Pseudomonas sp.

proof_lines:
strain 1YB2, pH 7.5, 25°C
strain 1YdBTEX2, pH 7.5, 25°C

enzyme: catechol 2,3-dioxygenase


substrate_name: catechol

proof_lines:
strain 1YB2, pH 7.5, 25°C
strain 1YdBTEX2, pH 7.5, 25°C
hybrid enzyme, pH 7.5, 25°C

substrate: catechol


enzyme_display_name: UniProt P29477

organism: Mus musculus

substrate_name: L-arginine

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

enzyme: UniProt P29477

substrate: L-arginine


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


enzyme_display_name: arachidonate 12-lipoxygenase

organism: Sus scrofa

substrate_name: arachidonic acid

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

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonic acid


proof_lines: wild type enzyme and mutant enzyme M338L


enzyme_display_name: UniProt O06647

organism: Pseudomonas nitroreducens

enzyme: UniProt O06647


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


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Agrobacterium tumefaciens

enzyme: protocatechuate 3,4-dioxygenase


substrate_name: protocatechuate

proof_lines:
protocatechuate 3,4-dioxygenase type II
protocatechuate 3,4-dioxygenase type I

substrate: protocatechuate


enzyme_display_name: nitric-oxide synthase (NADPH)

organism: Nicotiana tabacum

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

enzyme: nitric-oxide synthase (NADPH)


substrate_name: Unknown

substrate: Unknown


organism: Aspergillus niger

substrate_name: anthranilic acid

assay_conditions_summary: pH 8.2; cofactor NADPH

substrate: anthranilic acid


enzyme_display_name: 2-hydroxybiphenyl 3-monooxygenase

substrate_name: indole

enzyme: 2-hydroxybiphenyl 3-monooxygenase

substrate: indole


proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme H48A


proof_lines: pH 7.5, temperature not specified in the publication R242A


proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme D117A


substrate_name: guaiacol

substrate: guaiacol


assay_conditions_summary: cofactor NADPH

proof_lines:
reaction with NADH and O2
reaction with NADPH and O2


proof_lines: reaction with 2,2'-dihydroxybiphenyl and O2


proof_lines:
reaction with NADPH and O2
reaction with NADH and O2
reaction with NADH or NADPH and O2


smiles: O=O

proof_lines: reaction with 2-hydroxybiphenyl and NADH


enzyme_display_name: anhydrotetracycline 6-monooxygenase

organism: Kitasatospora aureofaciens

substrate_name: anhydrotetracycline

enzyme: anhydrotetracycline 6-monooxygenase

substrate: anhydrotetracycline


enzyme_display_name: nitric-oxide synthase

organism: Aiptasia pallida

substrate_name: NADPH; L-Arginine; O2

enzyme: nitric-oxide synthase

substrate: NADPH; L-Arginine; O2


proof_lines: turnover rate refers to the enzyme monomer and not to the tetramer


enzyme_display_name: leukotriene-E4 20-monooxygenase

organism: Rattus norvegicus

enzyme: leukotriene-E4 20-monooxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R242A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NADH