enzyme_display_name: chlorobenzene dihydrodiol dehydrogenase

organism: Xanthobacter flavus

substrate_name: 3,6-dichlorobenzene cis-dihydrodiol

enzyme: chlorobenzene dihydrodiol dehydrogenase

substrate: 3,6-dichlorobenzene cis-dihydrodiol


substrate_name: NAD+

source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

proof_lines: pH 8.0, 30°C, cosubstrate: 3,6-dichlorobenzene cis-dihydrodiol

proof_lines: pH 8.0, 30°C, cosubstrate: benzene cis-dihydrodiol

substrate: NAD+

status: unverified

source: brenda


substrate_name: benzene cis-dihydrodiol

substrate: benzene cis-dihydrodiol


enzyme_display_name: hydroxycinnamoyl-CoA reductase

organism: Malus domestica

assay_conditions_summary: 308.15 K; cofactor CoA

enzyme: hydroxycinnamoyl-CoA reductase


substrate_name: NADPH

assay_conditions_summary: 308.15 K; cofactor NADPH

substrate: NADPH


substrate_name: trans-feruloyl-CoA

substrate: trans-feruloyl-CoA


enzyme_display_name: meromycolic acid enoyl-[acyl-carrier-protein] reductase

organism: Mycobacterium tuberculosis

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

mutation_type: substitution

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


enzyme: meromycolic acid enoyl-[acyl-carrier-protein] reductase


proof_lines:
pH 7.5, 25°C, wild-type enzyme
pH 6.8, 25°C, wild-type enzyme


kcat_display: Not reported

assay_conditions_summary: pH 6.8; 298.15 K; cofactor CoA


substrate_name: trans-2-octenoyl-[acyl-carrier protein]

substrate: trans-2-octenoyl-[acyl-carrier protein]


substrate_name: NADH

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH

proof_lines: pH 6.8, 25°C, cosubstrate: trans-2-hexadecenoyl-CoA, wild-type enzyme

proof_lines: pH 6.8, 25°C, cosubstrate: trans-2-dodecenoyl-CoA, wild-type enzyme

proof_lines: pH 6.8, 25°C, cosubstrate: trans-2-octenoyl-CoA, wild-type enzyme

substrate: NADH


proof_lines: pH 6.8, 25°C, cosubstrate: trans-2-octenoyl-[acyl-carrier protein], mutant enzyme S94A

proof_lines: pH 6.8, 25°C, cosubstrate: trans-2-octenoyl-CoA, mutant enzyme S94A


enzyme_display_name: 2-methylene-furan-3-one reductase

organism: Solanum lycopersicum

protein_accession_database: UniProt

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H2P with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: 0.1 M Na2HPO4/NaH2PO4, pH 7, 30°C, cofactor NADH

data_origin: experimental

enzyme: 2-methylene-furan-3-one reductase


enzyme_display_name: UniProt Q16698

organism: Homo sapiens

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt Q16698

source: skid


organism: Vitis vinifera

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

source_db: uniprot

verification_status: verified

column_label: Abstract reports at pH 7.5 and 30 degrees C, K(M(cyan))=2.82+/-0.66 microM.

raw_value_unit_evidence: Km raw_value=2.82 microM raw_unit=microM

row_label: Vitis vinifera anthocyanidin reductase / cyanidin

table_label: PubMed XML abstract PMID 19772852

status: verified

source: uniprot


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase

substrate_name: crotonoyl-CoA

source_db: oed

verification_status: corrected

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Butenoyl-CoA (C4); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.0742 normalized_unit=mM; kcat normalized_value=1.5 normalized_unit=s^-1; kcat/Km normalized_value=20 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: (2E)-Butenoyl-CoA (C4): Km raw_value=74.2 raw_unit=uM; kcat raw_value=1.5 raw_unit=s^-1; kcat/Km raw_value=0.2 x 10^5 raw_unit=M^-1 s^-1

row_label: (2E)-Butenoyl-CoA (C4)

enzyme: enoyl-[acyl-carrier-protein] reductase

substrate: crotonoyl-CoA

status: corrected

source: oed


assay_conditions_summary: cofactor CoA

column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Butenoyl-CoA; Km column raw 74.2 uM normalized 0.0742 mM

raw_value_unit_evidence: Km 74.2 uM


column_label: Table 2 row (2E)-Hexenoyl-CoA (C6); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1). Explicit paper kcat/Km is 0.4 x 10^5, normalized to 40 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0635 normalized_unit=mM; kcat normalized_value=2.2 normalized_unit=s^-1; kcat/Km normalized_value=40 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: (2E)-Hexenoyl-CoA (C6): Km raw_value=63.5 raw_unit=uM; kcat raw_value=2.2 raw_unit=s^-1; kcat/Km raw_value=0.4 x 10^5 raw_unit=M^-1 s^-1

row_label: (2E)-Hexenoyl-CoA (C6)

table_label: ScienceDirect PMID 18479707 Table 2 | Kinetic parameters of the wild-type MECR/ETR1


column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Octenoyl-CoA; Km column raw 10.200000000000001 uM normalized 0.0102 mM


column_label: Table 2 row (2E)-Decenoyl-CoA (C10); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1). Explicit paper kcat/Km is 1.6 x 10^5, normalized to 160 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0104 normalized_unit=mM; kcat normalized_value=1.7 normalized_unit=s^-1; kcat/Km normalized_value=160 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: (2E)-Decenoyl-CoA (C10): Km raw_value=10.4 raw_unit=uM; kcat raw_value=1.7 raw_unit=s^-1; kcat/Km raw_value=1.6 x 10^5 raw_unit=M^-1 s^-1

row_label: (2E)-Decenoyl-CoA (C10)


column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Dodecenoyl-CoA; Km column raw 3.6 uM normalized 0.0036 mM

raw_value_unit_evidence: Km 3.6 uM


column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Tetradecenoyl-CoA; Km column raw 4.3 uM normalized 0.0043 mM

raw_value_unit_evidence: Km 4.3 uM


column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Hexadecenoyl-CoA; Km column raw 6.6 uM normalized 0.0066 mM

raw_value_unit_evidence: Km 6.6 uM


enzyme_display_name: 7-dehydrocholesterol reductase

organism: Mus musculus

enzyme: 7-dehydrocholesterol reductase


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


enzyme_display_name: 8-oxogeranial reductase

organism: Swertia mussotii

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines:
isoform IS2, at pH 7.0 and 25°C
isoform IS1, at pH 7.0 and 25°C

enzyme: 8-oxogeranial reductase


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


enzyme_display_name: (S)-8-oxocitronellyl enol synthase

organism: Antirrhinum majus

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 0.72 sec(-1) with (6E)-8-oxogeranial as substrate.

enzyme: (S)-8-oxocitronellyl enol synthase


sequence_source: multiple

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: with NADPH as cosubstrate, at pH 7.0 and 25°C

source_databases_merged: brenda uniprot


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E276A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines: recombinant His-tagged mutant E276A, pH 6.0, 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D300A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant D300A, pH 6.0, 22°C


enzyme_display_name: (S)-8-oxocitronellyl enol synthase ISY2

organism: Nepeta racemosa

proof_lines: kcat is 0.60 sec(-1) with (6E)-8-oxogeranial as substrate. kcat is 0.84 sec(-1) with NADPH as proton donor.

enzyme: (S)-8-oxocitronellyl enol synthase ISY2


organism: Catharanthus roseus

proof_lines: kcat is 1.6 sec(-1) with (6E)-8-oxogeranial. kcat is 2.2 sec(-1) with NADPH.


enzyme_display_name: acrylate reductase

organism: Vibrio harveyi

substrate_name: methacrylate

proof_lines: at pH 6.5, temperature not specified in the publication

proof_lines: kcat is 19 sec(-1) with acrylate as substrate. kcat is 2.5 sec(-1) with methacrylate as substrate.

enzyme: acrylate reductase

substrate: methacrylate


substrate_name: Acrylate

substrate: Acrylate


assay_conditions_summary: pH 6.5; cofactor NADH


organism: Plantago major

protein_accession_database: NCBI Protein

assay_conditions_summary: pH 7

proof_lines: at pH 7.0, temperature not specified in the publication


enzyme_display_name: aspartate-semialdehyde dehydrogenase

organism: Methanocaldococcus jannaschii

substrate_name: H+; 4-Phospho-L-aspartate; NADPH

km_display: Not reported

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

enzyme: aspartate-semialdehyde dehydrogenase

substrate: H+; 4-Phospho-L-aspartate; NADPH


substrate_name: NADP+; L-Aspartate 4-semialdehyde; Phosphate

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

assay_conditions_summary: cofactor NADP+


organism: Pseudomonas aeruginosa

substrate_name: NADP+; Phosphate; L-Aspartate 4-semialdehyde


organism: Vibrio cholerae

substrate_name: Phosphate; L-Aspartate 4-semialdehyde; NADP+


substrate: NADP+; L-Aspartate 4-semialdehyde; Phosphate


organism: Aspergillus nidulans

substrate_name: Phosphate; NAD+; D-Glyceraldehyde 3-phosphate

assay_conditions_summary: cofactor NAD+


organism: Oncorhynchus mykiss

substrate: Phosphate; NAD+; D-Glyceraldehyde 3-phosphate


organism: Oryctolagus cuniculus

substrate_name: NAD+; Phosphate; D-Glyceraldehyde 3-phosphate


organism: Oryza sativa

substrate_name: D-Glyceraldehyde 3-phosphate; NAD+; Phosphate


organism: Pinus sylvestris

substrate_name: NAD+; D-Glyceraldehyde 3-phosphate; Phosphate


organism: Pisum sativum

substrate_name: D-Glyceraldehyde 3-phosphate; Phosphate; NAD+


organism: Rattus norvegicus

substrate: D-Glyceraldehyde 3-phosphate; NAD+; Phosphate


organism: Amborella trichopoda


organism: Entamoeba histolytica

substrate_name: NADH; H+; 3-Phospho-D-glyceroyl phosphate


organism: Escherichia coli


organism: Geobacillus stearothermophilus

substrate: D-Glyceraldehyde 3-phosphate; Phosphate; NAD+


organism: Homo sapiens

substrate_name: Phosphate; D-Glyceraldehyde 3-phosphate; NAD+


organism: Jaculus orientalis


organism: Mus musculus


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

organism: Spinacia oleracea

substrate_name: H+; 3-Phospho-D-glyceroyl phosphate; NADPH


organism: Sulfolobus solfataricus

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

substrate: H+; 3-Phospho-D-glyceroyl phosphate; NADPH


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Acinetobacter baylyi

substrate_name: H2O; 2,5-Dioxopentanoate; NADP+

enzyme: 2,5-dioxovalerate dehydrogenase

substrate: H2O; 2,5-Dioxopentanoate; NADP+


organism: Halobacterium volcanii

substrate_name: NADP+; 2,5-Dioxopentanoate; H2O

substrate: NADP+; 2,5-Dioxopentanoate; H2O


organism: Pseudomonas putida

substrate_name: 2,5-Dioxopentanoate; NADP+; H2O

substrate: 2,5-Dioxopentanoate; NADP+; H2O


organism: Bacillus subtilis

substrate_name: NAD+; Coenzyme A; 2-Methyl-3-oxopropanoate


organism: Saccharomyces cerevisiae

ki_unit: mM


substrate: NAD+; Phosphate; D-Glyceraldehyde 3-phosphate


substrate_name: H+; NADH; 3-Phospho-D-glyceroyl phosphate


organism: Streptococcus mutans


organism: Streptomyces arenae

assay_conditions_summary: pH 8; cofactor NAD+


sequence: SVKVGINGFGRIGRLAFRRIQNVEGIEVVAINDL

wild_type_sequence: SVKVGINGFGRIGRLAFRRIQNVEGIEVVAINDL


organism: Clostridium beijerinckii

substrate_name: Acetyl-CoA; H+; NADH

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

substrate: Acetyl-CoA; H+; NADH


organism: Thermus thermophilus

substrate_name: Coenzyme A; NAD+; Acetaldehyde

smiles: CCC=O

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase - / substrate acetaldehyde; columns Km, kcat, kcat/Km; cells Km 5.5+/-0.5, kcat 7.4+/-0.04, kcat/Km 13.5+/-1.2 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=7.4 normalized_unit=s^-1; Km normalized_value=5.5 normalized_unit=mM; kcat/Km normalized_value=1.35 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase - / substrate acetaldehyde: Km 5.5+/-0.5; kcat 7.4+/-0.04 s^-1; kcat/Km 13.5+/-1.2 x10^2 M^-1 s^-1.

substrate: Coenzyme A; NAD+; Acetaldehyde


organism: Arabidopsis thaliana

substrate_name: NADPH; H+; 4-Phospho-L-aspartate

substrate: NADPH; H+; 4-Phospho-L-aspartate


substrate_name: 4-Phospho-L-malate; NADPH; H+

substrate: 4-Phospho-L-malate; NADPH; H+


organism: Escherichia coli

substrate_name: L-Aspartate 4-semialdehyde; Phosphate; NADP+


organism: Haemophilus influenzae

substrate_name: Phosphate; NADP+; L-Aspartate 4-semialdehyde

assay_conditions_summary: pH 9; cofactor NADP+

column_label: Table 2, Kinetic Parameters of Purified ASA Dehydrogenases; row Ha. influenzae; kcat column = 330 s^-1; NADP Km (mM) column = 0.15; NADP kcat/Km (M^-1 s^-1) column = 2.2 x 10^6 (normalized 2200 s^-1 mM^-1).

raw_value_unit_evidence: kcat 330 s^-1; NADP Km 0.15 mM; NADP kcat/Km 2.2 x 10^6 M^-1 s^-1

row_label: Ha. influenzae / NADP


enzyme_display_name: L-galactonolactone dehydrogenase

organism: Triticum aestivum

assay_conditions_summary: pH 8

proof_lines: recombinant wild-type TaGLDH-A1a variant, pH 8.0, temperature not specified in the publication

enzyme: L-galactonolactone dehydrogenase


proof_lines: recombinant mutant TaGLDH-A1b variant, pH 8.0, temperature not specified in the publication


organism: Ipomoea batatas

substrate_name: L-galactono-gamma-lactone

substrate: L-galactono-gamma-lactone


proof_lines:
isoform 2, pH 7, 22°C
isoform 1, pH 7, 22°C


organism: Solanum tuberosum


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R388A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E386D with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.


proof_lines: wild type enzyme, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R388K with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


substrate_name: G3P (at pH 8 and 26 degrees Celsius)

substrate: G3P (at pH 8 and 26 degrees Celsius)


organism: Thermotoga maritima

substrate_name: NAD+; D-Glyceraldehyde 3-phosphate; Arsenate


organism: Trichoderma koningii

substrate_name: NAD+; Phosphate; D-Glyceraldehyde 3-phosphate


substrate_name: D-Glyceraldehyde 3-phosphate; Phosphate; NAD+


organism: Trypanosoma brucei

substrate_name: Phosphate; D-Glyceraldehyde 3-phosphate; NAD+


substrate_name: NAD+; D-Glyceraldehyde 3-phosphate; Phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C340S 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 C340A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


enzyme_display_name: retinal dehydrogenase

organism: Mus musculus

substrate_name: all-trans-Retinal; H2O; NAD+

enzyme: retinal dehydrogenase

substrate: all-trans-Retinal; H2O; NAD+


enzyme_display_name: Retinal dehydrogenase 2

organism: Rattus norvegicus

substrate_name: free retinal

enzyme: Retinal dehydrogenase 2

substrate: free retinal


enzyme_display_name: glutamate-5-semialdehyde dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: L-Glutamate 5-semialdehyde; Phosphate; NAD+

enzyme: glutamate-5-semialdehyde dehydrogenase


enzyme_display_name: cinnamoyl-CoA reductase

substrate_name: H+; Feruloyl-CoA; NADPH

enzyme: cinnamoyl-CoA reductase

substrate: H+; Feruloyl-CoA; NADPH


substrate_name: Feruloyl-CoA; H+; NADPH

substrate: Feruloyl-CoA; H+; NADPH


organism: Homo sapiens

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


proof_lines: in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L56H with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L56H, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L56I with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L56IA in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C

proof_lines: mutant enzyme L56I, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C


substrate_name: phenazine methosulfate

proof_lines: in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C

substrate: phenazine methosulfate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L56C with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L56C, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L56F with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L56F in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C


proof_lines: wild type enzyme, in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C


enzyme_display_name: Fumarate reductase (cytochrome)

organism: Shewanella frigidimarina (strain NCIMB 400)

substrate_name: fumarate (in the presence of methyl viologen)

proof_lines: kcat is 250 sec(-1) with fumarate as substrate. kcat is 0.07 sec(-1) with succinate as substrate.

enzyme: Fumarate reductase (cytochrome)


substrate_name: succinate (in the presence of 2,6-dichlorophenol-indophenol)


enzyme_display_name: fumarate reductase (cytochrome)

organism: Shewanella frigidimarina

substrate_name: fumarate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R402A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9

proof_lines: mutant enzyme Q363/R402A, at pH 9.0 and 25°C

enzyme: fumarate reductase (cytochrome)

substrate: fumarate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R402K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H504A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6

proof_lines:
mutant enzyme H504A, at pH 6.0 and 25°C
mutant enzyme H504A, at pH 7.2 and 25°C
mutant enzyme H504A, at pH 7.5 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H365A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme H365A, at pH 6.0 and 25°C
mutant enzyme H365A, at pH 7.2 and 25°C
mutant enzyme H365A, at pH 9.0 and 25°C


substrate_name: fumarate (at pH 6.0 with methyl viologen as electron donor)

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

proof_lines: kcat is 658 sec(-1) at pH 6.0. kcat is 509 sec(-1) at pH 7.2. kcat is 370 sec(-1) at pH 7.5. kcat is 210 sec(-1) at pH 9.0.


substrate_name: Coenzyme A; NAD+; (S)-Methylmalonate semialdehyde

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


enzyme_display_name: carboxylate reductase (NADP+)

organism: Neurospora crassa

substrate_name: benzoyladenosine 5'-monophosphate

enzyme: carboxylate reductase (NADP+)

substrate: benzoyladenosine 5'-monophosphate


organism: Ctenopharyngodon idella

substrate_name: H2O; NAD+; Acetaldehyde

sequence: SALAINQPNYSVLKELGLNED

wild_type_sequence: SALAINQPNYSVLKELGLNED

smiles: CC=O

substrate: H2O; NAD+; Acetaldehyde


substrate_name: H2O; NAD+; L-2-Aminoadipate 6-semialdehyde

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


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

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

assay_conditions_summary: pH 5

proof_lines:
at pH 5.0
at pH 7.0


organism: Coccomyxa subellipsoidea


enzyme_display_name: UniProt P36551

substrate_name: Coproporphyrinogen-III

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

enzyme: UniProt P36551

substrate: Coproporphyrinogen-III


substrate_name: Harderoporphyrinogen

substrate: Harderoporphyrinogen


enzyme_display_name: UniProt P32397

organism: Bacillus subtilis

substrate_name: protoporphyrinogen-IX

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.4
Raw SKiD Env: Temp=22°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.5

enzyme: UniProt P32397

substrate: protoporphyrinogen-IX


enzyme_display_name: UniProt P50336

substrate_name: protoporphyrinogen IX

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=25°C, pH=7.4

enzyme: UniProt P50336

substrate: protoporphyrinogen IX


enzyme_display_name: UniProt O24164

organism: Nicotiana tabacum

enzyme: UniProt O24164


enzyme_display_name: bilirubin oxidase

organism: Thermosediminibacter oceani

substrate_name: syringaldazine

enzyme: bilirubin oxidase

substrate: syringaldazine


substrate_name: bilirubin

proof_lines:
at pH 8.0 and 70°C
at pH 8.0 and 70°C

substrate: bilirubin


organism: Thermobaculum terrenum


enzyme_display_name: UniProt P07872

substrate_name: octanoyl-CoA

enzyme: UniProt P07872

substrate: octanoyl-CoA


enzyme_display_name: Acyl-coenzyme A oxidase 3, peroxisomal

organism: Arabidopsis thaliana

substrate_name: lauroyl-CoA

enzyme: Acyl-coenzyme A oxidase 3, peroxisomal

substrate: lauroyl-CoA


organism: Arachis hypogaea

substrate_name: NADP+; D-Glyceraldehyde 3-phosphate; H2O


organism: Clostridium acetobutylicum

substrate: NADP+; D-Glyceraldehyde 3-phosphate; H2O


organism: Pisum sativum

substrate_name: D-Glyceraldehyde 3-phosphate; NAD+; Arsenate


organism: Streptococcus mutans


organism: Streptococcus pyogenes

substrate_name: D-Glyceraldehyde 3-phosphate; NADP+; H2O


enzyme_display_name: (S)-8-oxocitronellyl enol synthase

organism: Digitalis lanata

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

enzyme: (S)-8-oxocitronellyl enol synthase


enzyme_display_name: abscisic-aldehyde oxidase

substrate_name: H2O; Abscisic aldehyde; O2

enzyme: abscisic-aldehyde oxidase

substrate: H2O; Abscisic aldehyde; O2


enzyme_display_name: pyruvate oxidase

organism: Lactobacillus plantarum

substrate_name: Pyruvate; Phosphate; O2

enzyme: pyruvate oxidase

substrate: Pyruvate; Phosphate; O2


enzyme_display_name: oxalate oxidase

organism: Hordeum vulgare

substrate_name: O2; Oxalate

enzyme: oxalate oxidase

substrate: O2; Oxalate


enzyme_display_name: indole-3-acetaldehyde oxidase

substrate_name: Indole-3-acetaldehyde; H2O; O2

enzyme: indole-3-acetaldehyde oxidase

substrate: Indole-3-acetaldehyde; H2O; O2


organism: Corynebacterium glutamicum

substrate_name: Pyruvate; 2,6-Dichloroindophenol

substrate: Pyruvate; 2,6-Dichloroindophenol


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Enterococcus faecalis

substrate_name: NAD+; Coenzyme A; Pyruvate

enzyme: dihydrolipoyl dehydrogenase

substrate: NAD+; Coenzyme A; Pyruvate


organism: Homo sapiens

substrate_name: 4-Trimethylammoniobutanal; H2O; NAD+

substrate: 4-Trimethylammoniobutanal; H2O; NAD+


organism: Rattus norvegicus

substrate_name: 4-Trimethylammoniobutanal; NAD+; H2O

assay_conditions_summary: pH 9; buffer pH 9; cofactor NAD+

column_label: Table II, enzyme column Rat liver TMABA-DH, row gamma-trimethylaminobutyraldehyde, column Km (microM).

normalized_value_unit_evidence: Km normalized_value=0.0014 normalized_unit=mM converted from 1.4 microM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH / gamma-trimethylaminobutyraldehyde Km=1.4 microM.

table_label: Table II: Substrate specificity of purified TMABA-DH and heterologously expressed enzymes

substrate: 4-Trimethylammoniobutanal; NAD+; H2O


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

organism: Bacillus subtilis

substrate_name: NAD+; Phosphate; D-Glyceraldehyde 3-phosphate


organism: Methanothermus fervidus

substrate_name: Phosphate; NAD+; D-Glyceraldehyde 3-phosphate

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)


organism: Synechocystis sp.

substrate_name: NAD+; D-Glyceraldehyde 3-phosphate; Phosphate


enzyme_display_name: fluoroacetaldehyde dehydrogenase

organism: Streptomyces cattleya

substrate_name: Fluoroacetaldehyde; H2O; NAD+

enzyme: fluoroacetaldehyde dehydrogenase

substrate: Fluoroacetaldehyde; H2O; NAD+


enzyme_display_name: aldehyde oxidase

organism: Arabidopsis thaliana

substrate_name: H2O; Heptanal; 2,6-Dichloroindophenol

enzyme: aldehyde oxidase

substrate: H2O; Heptanal; 2,6-Dichloroindophenol


substrate_name: 2,6-Dichloroindophenol; Heptanal; H2O

substrate: 2,6-Dichloroindophenol; Heptanal; H2O


organism: Cavia porcellus

substrate_name: 6-Deoxypenciclovir; O2; H2O

substrate: 6-Deoxypenciclovir; O2; H2O


organism: Macaca fascicularis


organism: Oryctolagus cuniculus

substrate_name: H2O; O2; 6-Deoxypenciclovir

substrate: H2O; O2; 6-Deoxypenciclovir


enzyme_display_name: acyl-CoA oxidase

organism: Candida tropicalis

substrate_name: O2; Stearoyl-CoA

enzyme: acyl-CoA oxidase

substrate: O2; Stearoyl-CoA


substrate_name: Octanoyl-CoA; O2

substrate: Octanoyl-CoA; O2


substrate_name: Lauroyl-CoA; O2

substrate: Lauroyl-CoA; O2


substrate_name: O2; Palmitoyl-CoA

substrate: O2; Palmitoyl-CoA


organism: Synechococcus elongatus

substrate_name: H+; NADPH; Oleoyl-[acyl-carrier protein]


enzyme_display_name: Fatty acyl-CoA reductase 2, chloroplastic

substrate_name: hexadecanoyl-[ACP] (at pH 6 and 30 degrees Celsius)


enzyme_display_name: Fatty acyl-CoA reductase 6, chloroplastic

substrate_name: C16:0-ACP (at pH 7 and 30 degrees Celsius)

assay_conditions_summary: pH 7; cofactor CoA


organism: Thermus thermophilus

substrate_name: Propanal; NAD+; Coenzyme A

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase TTHB247 / aldolase - / substrate propionaldehyde; columns Km, kcat, kcat/Km; cells Km 6.4+/-0.6, kcat 8.4+/-0.04, kcat/Km 13.1+/-1.2 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=8.4 normalized_unit=s^-1; Km normalized_value=6.4 normalized_unit=mM; kcat/Km normalized_value=1.31 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase TTHB247 / aldolase - / substrate propionaldehyde: Km 6.4+/-0.6; kcat 8.4+/-0.04 s^-1; kcat/Km 13.1+/-1.2 x10^2 M^-1 s^-1.

substrate: Propanal; NAD+; Coenzyme A


organism: Bos taurus


substrate_name: m-Nitrobenzaldehyde; NAD+; H2O

substrate: m-Nitrobenzaldehyde; NAD+; H2O


organism: Sulfolobus solfataricus

substrate_name: Glyceraldehyde 3-phosphate; H2O; NADP+

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

substrate: Glyceraldehyde 3-phosphate; H2O; NADP+


organism: Thermoproteus tenax

substrate_name: H2O; NADP+; D-Glyceraldehyde 3-phosphate


organism: Zea mays

substrate_name: D-Glyceraldehyde 3-phosphate; NADP+; H2O


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

substrate_name: GAP (at 70 degrees Celsius)

substrate: GAP (at 70 degrees Celsius)


enzyme_display_name: L-2-aminoadipate reductase

organism: Saccharomyces cerevisiae

substrate_name: ATP; L-2-Aminoadipate

assay_conditions_summary: cofactor ATP

enzyme: L-2-aminoadipate reductase

substrate: ATP; L-2-Aminoadipate


organism: Pseudomonas putida

substrate_name: 4-Hydroxybenzaldehyde; NAD+; H2O

substrate: 4-Hydroxybenzaldehyde; NAD+; H2O


enzyme_display_name: dihydrouracil oxidase

organism: Rhodotorula glutinis

substrate_name: dihydrouracil

enzyme: dihydrouracil oxidase

substrate: dihydrouracil


substrate_name: Dihydrothymine

substrate: Dihydrothymine


substrate_name: Unknown

substrate: Unknown


organism: Glutamicibacter nicotianae

substrate_name: octanoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: octanoyl-CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


enzyme_display_name: bilirubin oxidase

organism: Bacillus pumilus

proof_lines: recombinant enzyme expressed in Escherichia coli strain BL21(DE3), pH 7.0, 37°C

proof_lines: recombinant enzyme expressed in Escherichia coli strain BL21(DE3), pH 6.8, 37°C

proof_lines: recombinant enzyme expressed in Escherichia coli strain Origami B(DE3), pH 7.0, 37°C


proof_lines: recombinant enzyme expressed in Escherichia coli strain BL21(DE3), pH 4.0, 37°C

proof_lines: recombinant enzyme expressed in Escherichia coli strain BL21(DE3), pH 3.2, 37°C

proof_lines: recombinant enzyme expressed in Escherichia coli strain Origami B(DE3), pH 4.0, 37°C


organism: Rattus norvegicus

substrate_name: Bilirubin; O2

substrate: Bilirubin; O2


substrate_name: bilirubin

substrate: bilirubin


organism: Aspergillus oryzae

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


organism: Arabidopsis thaliana

substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


enzyme_display_name: tryptophan alpha,beta-oxidase

organism: Chromobacterium violaceum

substrate_name: L-Tryptophan; O2

proof_lines: dehydrogenation of the tryptophanyl side chain

enzyme: tryptophan alpha,beta-oxidase

substrate: L-Tryptophan; O2


substrate_name: pentagastrin

substrate: pentagastrin


substrate_name: L-Tryptophanamide

substrate: L-Tryptophanamide


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: N-Acetyl-L-tryptophanamide

substrate: N-Acetyl-L-tryptophanamide


substrate_name: N-acetyl-L-tryptophan

substrate: N-acetyl-L-tryptophan


organism: Digitalis purpurea


enzyme_display_name: glutamyl-tRNA reductase

organism: Escherichia coli

substrate_name: H+; L-Glutamyl-tRNA(Glu); NADPH

assay_conditions_summary: cofactor NADPH

enzyme: glutamyl-tRNA reductase

substrate: H+; L-Glutamyl-tRNA(Glu); NADPH


enzyme_display_name: erythrose-4-phosphate dehydrogenase

substrate_name: H2O; D-Erythrose 4-phosphate; NAD+

enzyme: erythrose-4-phosphate dehydrogenase

substrate: H2O; D-Erythrose 4-phosphate; NAD+


organism: Geobacillus stearothermophilus

substrate_name: D-Erythrose 4-phosphate; NAD+; H2O

substrate: D-Erythrose 4-phosphate; NAD+; H2O


organism: Clostridium kluyveri

substrate_name: Succinate-semialdehyde

assay_conditions_summary: pH 8.5; cofactor NADPH

column_label: Table 3 Km mM column; direction Reverse; substrate succinate-semialdehyde; value 2.7 (+/- 0.2)

raw_value_unit_evidence: Table 3 reverse row succinate-semialdehyde Km = 2.7 (+/- 0.2) mM

row_label: Reverse row succinate-semialdehyde

table_label: Wiley PDF page 126 Table 3. Kinetic values for succinate-semialdehyde dehydrogenase

substrate: Succinate-semialdehyde


enzyme_display_name: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)

organism: Azoarcus evansii

substrate_name: H2O; NADP+; 3,4-Dehydroadipyl-CoA semialdehyde


organism: Mycobacterium tuberculosis

substrate_name: NADP+; H2O; Succinate semialdehyde

substrate: NADP+; H2O; Succinate semialdehyde


substrate_name: conjugated Bilirubin; O2

enzyme: bilirubin oxidase

substrate: conjugated Bilirubin; O2


proof_lines: conjugated bilirubin, pH 4.8, temperature not specified in the publication


organism: Pyricularia oryzae

proof_lines: conjugated bilirubin, pH 3.6, temperature not specified in the publication


organism: Zea mays

substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


enzyme_display_name: protoporphyrinogen oxidase

organism: Megalodesulfovibrio gigas

substrate_name: protoporphyrinogen-IX

enzyme: protoporphyrinogen oxidase

substrate: protoporphyrinogen-IX


enzyme_display_name: tetrahydroberberine oxidase

organism: Berberis stolonifera

substrate_name: (S)-tetrahydroberberine

enzyme: tetrahydroberberine oxidase

substrate: (S)-tetrahydroberberine


organism: Aquifex aeolicus


substrate_name: dodecanoyl-CoA

sequence_source: UniProt P0CZ23

column_label: Printed page 736/PDF page 4, Table I, AtACX3 row, Km cell 15.7 +/- 2.1; adjacent Results prose supplies uM and C12:0-CoA identity.

normalized_value_unit_evidence: Km normalized_value=0.0157 normalized_unit=mM; uncertainty 0.0021 mM.

raw_value_unit_evidence: Adjacent Results prose pairs AtACX3 with C12:0-CoA and reports Km raw_value=15.7 +/- 2.1 raw_unit=uM.

row_label: AtACX3 / C12:0-CoA

table_label: Table I. Kinetic parameters of ACX enzymes; unit resolved by adjacent Results prose

substrate: dodecanoyl-CoA


organism: Haemonchus contortus

substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 7.5; 315.15 K; cofactor CoA

proof_lines: isoform isoform ACOX-1.2, at pH 7.5 and 42°C

proof_lines: isoform isoform ACOX-1.3, at pH 7.5 and 42°C

proof_lines: isoform isoform ACOX-1.1, at pH 7.5 and 37°C

substrate: palmitoyl-CoA


organism: Coptis japonica


organism: Coscinium fenestratum


organism: Thalictrum minus var. hypoleucum

proof_lines:
isoenzyme I
isoenzyme II


enzyme_display_name: (S)-8-oxocitronellyl enol synthase

organism: Selaginella moellendorffii

proof_lines:
isoform 1, pH 7, 22°C
isoform 3, pH 7, 22°C

enzyme: (S)-8-oxocitronellyl enol synthase


organism: Albifimbria verrucaria

proof_lines: wild type recombinant enzyme, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M467Q with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 4


substrate_name: ferrocyanide

substrate: ferrocyanide


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature W396A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature W396F with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

substrate_name: protoporphyrinogen IX

substrate: protoporphyrinogen IX


proof_lines: pH 7.5, 22°C, recombinant wild-type enzyme

proof_lines: wild-type enzyme, pH 7.5, temperature not specified in the publication

proof_lines: recombinant wild-type enzyme, pH 7.4, 25°C


substrate_name: p-phenylenediamine

proof_lines: pH 6.5, recombinant enzyme from Pichia pastoris

substrate: p-phenylenediamine


substrate_name: ditaurobilirubin

proof_lines: pH 5.5, recombinant enzyme from Pichia pastoris

substrate: ditaurobilirubin


organism: Escherichia coli (strain K12)

substrate_name: coproporphyrinogen-III (at pH 6 at 37 degrees Celsius)

proof_lines: kcat is 0.17 min(-1) for decarboxylation of coproporphyrinogen-III (at pH 6 and at 37 degrees Celsius).


substrate_name: bilirubin

assay_conditions_summary: pH 7

proof_lines: unconjugated bilirubin, pH 7.0, temperature not specified in the publication

proof_lines: kcat is 16.8 sec(-1) with ABTS as substrate (PubMed:11884407). kcat is 322 sec(-1) with ABTS as substrate (PubMed:18307408). kcat is 144 sec(-1) with ABTS as substrate (PubMed:22481612). kcat is 3.7 sec(-1) with SGZ as substrate (PubMed:118

substrate: bilirubin


enzyme_display_name: coproporphyrinogen oxidase

organism: Homo sapiens

substrate_name: Coproporphyrinogen-III

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N272H with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

enzyme: coproporphyrinogen oxidase

substrate: Coproporphyrinogen-III


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V311M to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt P56601

organism: Myxococcus xanthus

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8.1
kcat is 5.2 min(-1).

source_databases_merged: skid uniprot

enzyme: UniProt P56601


organism: Catharanthus roseus

assay_conditions_summary: pH 7; 295.15 K; cofactor NADPH

proof_lines: kcat is 1.6 sec(-1) with (6E)-8-oxogeranial. kcat is 2.2 sec(-1) with NADPH.

source_databases_merged: brenda skid uniprot


enzyme_display_name: Acyl-coenzyme A oxidase acox-1.1

organism: Caenorhabditis elegans

assay_conditions_summary: pH 7.4; cofactor CoA

proof_lines: kcat is 252 sec(-1) with asc-C9-CoA (at 30 degrees Celsius and pH 7.4) (PubMed:25775534). kcat is 144 sec(-1) with asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.3) (PubMed:25775534). kcat is 478 sec(-1) with asc-omega

enzyme: Acyl-coenzyme A oxidase acox-1.1


substrate_name: asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.3)


enzyme_display_name: Laccase

organism: Bacillus subtilis (strain 168)

substrate_name: ABTS

enzyme: Laccase

substrate: ABTS


assay_conditions_summary: pH 7.5; buffer suspended in 50: 50 v/v chloroform-n-heptane mixture

proof_lines: preparations of enzyme lyophilized from N-(2-hydroxyethyl)-piperazine-N'-(3-propane-sulfonic acid) buffer suspended in 50 : 50 v/v chloroform-n-heptane mixture

proof_lines: unconjugated bilirubin, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R401A to reconstruct the assayed variant sequence.

proof_lines: mutant R401A, divinyl product, 37°C, pH not specified in the publication

proof_lines: mutant R401A, total product, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K71A to reconstruct the assayed variant sequence.

proof_lines: mutant K71A, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I176A to reconstruct the assayed variant sequence.

proof_lines: mutant I176A, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P64A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: mutant P64A, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F227R to reconstruct the assayed variant sequence.

proof_lines: mutant F227R, pH 7.5, temperature not specified in the publication


substrate_name: syringaldazine

proof_lines: at pH 8.2, lower Km at pH 7.0 and pH 9.0

substrate: syringaldazine


organism: Escherichia coli

substrate_name: NAD+; Coenzyme A; Pyruvate

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Coenzyme A; Pyruvate


organism: Sus scrofa

substrate_name: Hexacyanoferrate(III); Pyruvate; H2O

substrate: Hexacyanoferrate(III); Pyruvate; H2O


organism: Corynebacterium glutamicum

substrate_name: 2,6-Dichloroindophenol; 2-Oxoglutarate

substrate: 2,6-Dichloroindophenol; 2-Oxoglutarate


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Fasciola hepatica

substrate_name: Coenzyme A; NAD+; 2-Oxoglutarate

enzyme: dihydrolipoyl dehydrogenase

substrate: Coenzyme A; NAD+; 2-Oxoglutarate


substrate_name: Thiamine diphosphate; 2-Oxoglutarate

substrate: Thiamine diphosphate; 2-Oxoglutarate


organism: Rattus norvegicus

substrate_name: 2-Oxoglutarate; Coenzyme A; NAD+

substrate: 2-Oxoglutarate; Coenzyme A; NAD+


organism: Solanum tuberosum

substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

sequence: AQAAPVPRPVXLSKKTDSF

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


organism: Teladorsagia circumcincta


organism: Xenopus laevis

substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


substrate_name: Acceptor; alpha-Ketovaline; H2O

substrate: Acceptor; alpha-Ketovaline; H2O


smiles: O=O


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

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

source_databases_merged: sabio_rk skid uniprot


enzyme_display_name: Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]

organism: Mus musculus


enzyme_display_name: dihydropyrimidine dehydrogenase (NADP+)

substrate_name: H+; NADPH; Uracil

enzyme: dihydropyrimidine dehydrogenase (NADP+)

substrate: H+; NADPH; Uracil


organism: Canis familiaris

assay_conditions_summary: cofactor NADP+


organism: Macaca fuscata


organism: Oryctolagus cuniculus

substrate_name: 1,2-Dihydronaphthalene-1,2-diol; NADP+

substrate: 1,2-Dihydronaphthalene-1,2-diol; NADP+


enzyme_display_name: 2-methylene-furan-3-one reductase

organism: Fragaria ananassa

enzyme: 2-methylene-furan-3-one reductase


enzyme_display_name: UniProt P9WGR1

organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=6.8

enzyme: UniProt P9WGR1


enzyme_display_name: prephenate dehydrogenase

substrate_name: Prephenate; NAD+

assay_conditions_summary: pH 7.5; cofactor NAD+

enzyme: prephenate dehydrogenase

substrate: Prephenate; NAD+


enzyme_display_name: 1-cyclohexenylcarbonyl-CoA reductase

organism: Streptomyces collinus

enzyme: 1-cyclohexenylcarbonyl-CoA reductase


enzyme_display_name: 8-oxogeranial reductase

organism: Antirrhinum majus

substrate_name: H+; NADPH; 8-Oxogeranial

enzyme: 8-oxogeranial reductase

substrate: H+; NADPH; 8-Oxogeranial


enzyme_display_name: UniProt Q16698

organism: Homo sapiens

assay_conditions_summary: pH 6; 296.15 K; cofactor CoA

enzyme: UniProt Q16698


enzyme_display_name: 7-dehydrocholesterol reductase

substrate_name: NADPH; H+; Cholesta-5,7-dien-3beta-ol

enzyme: 7-dehydrocholesterol reductase

substrate: NADPH; H+; Cholesta-5,7-dien-3beta-ol


enzyme_display_name: cholestenone 5alpha-reductase

organism: Arabidopsis thaliana

substrate_name: Progesterone; NADPH; H+

enzyme: cholestenone 5alpha-reductase

substrate: Progesterone; NADPH; H+


substrate_name: Testosterone; H+; NADPH

substrate: Testosterone; H+; NADPH


substrate_name: H+; Testosterone; NADPH

substrate: H+; Testosterone; NADPH


organism: Solanum lycopersicum

substrate_name: H+; Progesterone; NADPH

substrate: H+; Progesterone; NADPH


enzyme_display_name: 2,4-dienoyl-CoA reductase (NADPH)

enzyme: 2,4-dienoyl-CoA reductase (NADPH)


enzyme_display_name: Trans-2-enoyl-CoA reductase

organism: Euglena gracilis

substrate_name: (2E)-butenoyl-CoA (crotonyl-CoA) (in the presence of NADH)

enzyme: Trans-2-enoyl-CoA reductase


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific)

organism: Bacillus subtilis

smiles: CCCCC/C=C/C(=O)SCCNC(C)=O


organism: Staphylococcus aureus

enzyme: enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific)


substrate_name: NADPH; But-2-enoyl-[acyl-carrier protein]; H+


enzyme_display_name: trans-2-enoyl-CoA reductase (NAD+)

substrate_name: H+; Crotonoyl-CoA; NADH

enzyme: trans-2-enoyl-CoA reductase (NAD+)

substrate: H+; Crotonoyl-CoA; NADH


enzyme_display_name: pyruvate synthase

organism: Acetogenium kivui

substrate_name: Oxidized ferredoxin; Pyruvate; Coenzyme A

enzyme: pyruvate synthase


enzyme_display_name: aldehyde ferredoxin oxidoreductase

organism: Caldicellulosiruptor bescii

substrate_name: oxidized ferredoxin

enzyme: aldehyde ferredoxin oxidoreductase

substrate: oxidized ferredoxin


organism: Pyrococcus furiosus

substrate_name: D-Glyceraldehyde 3-phosphate; H2O; Oxidized benzyl viologen

source_databases_merged: sabio_rk brenda uniprot


organism: Desulfovibrio gigas


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)

substrate_name: NADPH; Crotonoyl-CoA

substrate: NADPH; Crotonoyl-CoA


substrate_name: NADPH; Crotonoyl-CoA; H+

substrate: NADPH; Crotonoyl-CoA; H+


enzyme_display_name: L-galactonolactone dehydrogenase

organism: Brassica oleracea

substrate_name: Cytochrome c; L-Galactono-1,4-lactone

enzyme: L-galactonolactone dehydrogenase

substrate: Cytochrome c; L-Galactono-1,4-lactone


enzyme_display_name: coproporphyrinogen oxidase

organism: Gallus gallus

enzyme: coproporphyrinogen oxidase


enzyme_display_name: protoporphyrinogen oxidase

organism: Aquifex aeolicus

substrate_name: Protoporphyrinogen IX; O2

enzyme: protoporphyrinogen oxidase

substrate: Protoporphyrinogen IX; O2


substrate_name: Mesoporphyrinogen-IX

substrate: Mesoporphyrinogen-IX


substrate_name: O2; Protoporphyrinogen IX

substrate: O2; Protoporphyrinogen IX


organism: Pseudomonas aeruginosa


substrate_name: NADH; trans-Dodec-2-enoyl-[acp]; H+

substrate: NADH; trans-Dodec-2-enoyl-[acp]; H+


organism: Streptococcus pneumoniae

substrate_name: Crotonoyl-CoA; NADH; H+

substrate: Crotonoyl-CoA; NADH; H+


organism: Vibrio cholerae

substrate_name: NADH; But-2-enoyl-[acyl-carrier protein]; H+


enzyme_display_name: UniProt Q8Z9U1

organism: Yersinia pestis

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

enzyme: UniProt Q8Z9U1


enzyme_display_name: UDP-N-acetylmuramate dehydrogenase

organism: Escherichia coli

enzyme: UDP-N-acetylmuramate dehydrogenase


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


assay_conditions_summary: cofactor NADH


enzyme_display_name: 15-oxoprostaglandin 13-oxidase

organism: Homo sapiens

enzyme: 15-oxoprostaglandin 13-oxidase


organism: Mus musculus


organism: Alcaligenes faecalis

substrate_name: PDD (at pH 9 and 30 degrees Celsius)

assay_conditions_summary: pH 9

substrate: PDD (at pH 9 and 30 degrees Celsius)


organism: Comamonas testosteroni


organism: Myxococcus xanthus


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


enzyme_display_name: bilirubin oxidase

organism: Bacillus pumilus

enzyme: bilirubin oxidase


organism: Bacillus sp. HR03

substrate_name: Bilirubin; O2

substrate: Bilirubin; O2


organism: Halobacterium volcanii


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: butyrlaldehyde (in the presence of HsaF)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 9.4 sec(-1) with acetaldehyde as substrate (in the presence of HsaF). kcat is 19.0 sec(-1) with acetaldehyde as substrate (in the absence of HsaF). kcat is 11.1 sec(-1) with propanal as substrate (in the presence of HsaF). kcat is 2


organism: Paraburkholderia xenovorans

substrate_name: pentaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I171A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES

proof_lines: mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0)

substrate: pentaldehyde


enzyme_display_name: Acetaldehyde dehydrogenase (acetylating) EutE

organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: Unknown

substrate: Unknown


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: [LysW]-aminoadipate 6-semialdehyde

substrate: [LysW]-aminoadipate 6-semialdehyde


enzyme_display_name: Aspartate-semialdehyde dehydrogenase

organism: Blastomyces gilchristii (strain SLH14081)

proof_lines: kcat is 13.8 sec(-1) with L-aspartate 4-semialdehyde as substrate in the reverse direction (at 25 degrees Celsius and at pH 8.6).

enzyme: Aspartate-semialdehyde dehydrogenase


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


enzyme_display_name: UniProt Q46381

enzyme: UniProt Q46381


enzyme_display_name: fumarate reductase (NADH)

organism: Enterococcus faecalis

substrate_name: Fumarate; Reduced FMN

assay_conditions_summary: cofactor FMN

enzyme: fumarate reductase (NADH)

substrate: Fumarate; Reduced FMN


organism: Klebsiella pneumoniae

substrate_name: Fumarate; H+; NADH

substrate: Fumarate; H+; NADH


enzyme_display_name: anthocyanidin reductase

organism: Medicago truncatula

substrate_name: Cyanidin; NADP+

enzyme: anthocyanidin reductase

substrate: Cyanidin; NADP+


substrate_name: Delphinidin; NADP+

substrate: Delphinidin; NADP+


organism: Vitis vinifera


enzyme_display_name: acrylyl-CoA reductase (NADPH)

organism: Sulfolobus tokodaii

substrate_name: NADPH; Acryloyl-CoA; H+

assay_conditions_summary: cofactor NADPH

enzyme: acrylyl-CoA reductase (NADPH)

substrate: NADPH; Acryloyl-CoA; H+


organism: Cryptococcus deneoformans (strain JEC21 / ATCC MYA-565)

substrate_name: L-aspartate 4-semialdehyde in the reverse direction (at 25 degrees Celsius and at pH 8.6)

proof_lines: kcat is 10.2 sec(-1) with L-aspartate 4-semialdehyde as substrate (at 25 degrees Celsius and at pH 8.6).


enzyme_display_name: aspartate-semialdehyde dehydrogenase

enzyme: aspartate-semialdehyde dehydrogenase


organism: Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892)

proof_lines: kcat is 16.5 sec(-1) with L-aspartate 4-semialdehyde as substrate in the reverse direction (at 25 degrees Celsius and at pH 8.6).


organism: Escherichia coli

substrate_name: NAD+; Phosphate; D-Glyceraldehyde 3-phosphate

proof_lines: kcat is 1056 sec(-1) for dehydrogenase activity.


organism: Glycine max

substrate_name: Phosphate; D-Glyceraldehyde 3-phosphate; NAD+


organism: Lactococcus lactis subsp. lactis

substrate_name: D-Glyceraldehyde 3-phosphate; NAD+; Phosphate

assay_conditions_summary: pH 7.2; 303.15 K; cofactor NAD+

proof_lines: 30°C, pH 7.2, competitive inhibitor, no effect on the maximum velocity


enzyme_display_name: Trans-2-enoyl-CoA reductase

organism: Euglena gracilis

substrate_name: (2E)-butenoyl-CoA (crotonyl-CoA) (in the presence of NADH)

enzyme: Trans-2-enoyl-CoA reductase


organism: Arabidopsis thaliana

substrate_name: Crotonoyl-CoA; NADH; H+


organism: Bacillus subtilis

smiles: C(\C=C\CCCCC)(=O)SCCNC(C)=O

column_label: Page 3 Characterization prose, bsFabI NADH segment, Km 7 uM; Figure 2 gives the fixed 100 uM 8:1-NAC condition.

normalized_value_unit_evidence: Measured NADH Km=0.007 mM; 8:1-NAC is the fixed participant.

raw_value_unit_evidence: Page 3 states bsFabI has an apparent Km of 7 uM for NADH.

row_label: bsFabI, NADH

table_label: Characterization of the Reductases, page 3; Figure 2 assay context


enzyme_display_name: UniProt Q3JQY0

organism: Burkholderia pseudomallei

assay_conditions_summary: pH 6.8; 298.15 K; cofactor CoA

enzyme: UniProt Q3JQY0


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----


organism: Plasmodium falciparum

substrate_name: Crotonoyl-CoA; H+; NADH

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row Wild-type; substrate axis NADH; exact required metric cells preserved in paper_metric_evidence.

raw_value_unit_evidence: Wild-type | kcat 1.62 (+/-0.06) s^-1 | Km Crotonoyl-CoA 160+/-5 uM | Km NADH 33+/-3 uM

row_label: Wild-type

substrate: Crotonoyl-CoA; H+; NADH


substrate_name: H+; NADH; Crotonoyl-CoA

substrate: H+; NADH; Crotonoyl-CoA


column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row Wild-type; substrate axis crotonoyl-CoA; exact required metric cells preserved in paper_metric_evidence.


table_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR.


substrate_name: H+; Crotonoyl-CoA; NADH

substrate: H+; Crotonoyl-CoA; NADH


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

sequence_variant_note: Mutation signature G3P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: kcat is 1670 min(-1) for dehydrogenase activity with G3P.


organism: Palinurus versicolor

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

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Phosphate; D-Glyceraldehyde 3-phosphate


organism: Staphylococcus aureus (strain MRSA252)

proof_lines: kcat is 70 sec(-1) for dehydrogenase activity.


organism: Ustilago maydis

substrate_name: Phosphate; NAD+; D-Glyceraldehyde 3-phosphate


organism: Zymomonas mobilis

substrate_name: 3-Phospho-D-glyceroyl phosphate; NADH; H+


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)

organism: Spinacia oleracea

substrate_name: Glycerate 1,3-bisphosphate; H+; NADPH

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

substrate: Glycerate 1,3-bisphosphate; H+; NADPH


organism: Blastobotrys adeninivorans

substrate_name: Unknown

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

assay_conditions_summary: cofactor ATP


organism: Candida maltosa


organism: Burkholderia cepacia

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


organism: Mus musculus

proof_lines: Activity was measured with total soluble protein.


organism: Pseudomonas putida


enzyme_display_name: biliverdin reductase

organism: Cavia porcellus

substrate_name: biliverdin IX alpha

enzyme: biliverdin reductase

substrate: biliverdin IX alpha


organism: Homo sapiens

substrate_name: biliverdin IX beta

substrate: biliverdin IX beta


organism: Rattus norvegicus


enzyme_display_name: Delta4-3-oxosteroid 5beta-reductase

substrate_name: H+; Testosterone; NADPH

enzyme: Delta4-3-oxosteroid 5beta-reductase

substrate: H+; Testosterone; NADPH


enzyme_display_name: 2,4-dienoyl-CoA reductase (NADPH)

enzyme: 2,4-dienoyl-CoA reductase (NADPH)


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Azospirillum brasilense

substrate_name: H2O; NAD+; 2,5-Dioxopentanoate

proof_lines: kcat is 21.3 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NAD(+)). kcat is 23.0 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NADP(+)).

enzyme: 2,5-dioxovalerate dehydrogenase

substrate: H2O; NAD+; 2,5-Dioxopentanoate


substrate_name: 2,5-Dioxopentanoate; NAD+; H2O

proof_lines: kcat is 53.9 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NAD(+)). kcat is 15.4 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NADP(+)).

substrate: 2,5-Dioxopentanoate; NAD+; H2O


assay_conditions_summary: cofactor NADP+

proof_lines: The catalytic efficiency with alphaKGSA in the presence of NAD(+) is 5.2- and 6.2-fold higher than with succinic semialdehyde and glutaraldehyde, respectively. When NADP(+) is used as a cosubstrate, the catalytic efficiency with alphaKGSA d


organism: Bacillus subtilis (strain 168)

substrate_name: alpha-ketoglutaric semialdehyde (in the presence of NAD(+), at 25 degrees Celsius and pH 7.2)

proof_lines: kcat is 2.75 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NAD(+)). kcat is 1.12 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NADP(+)). kcat is 1.29 sec(-1) with propionaldehy


organism: Antirrhinum majus

proof_lines: kcat is 0.31 sec(-1) with benzaldehyde as substrate (PubMed:19292760). kcat is 2.08 sec(-1) with acetaldehyde as substrate (PubMed:19292760). kcat is 0.23 sec(-1) with phenylacetaldehyde as substrate (PubMed:19292760).

substrate: Unknown


enzyme_display_name: Aldehyde dehydrogenase 1A1

organism: Bos taurus

proof_lines: Has a much higher catalytic efficiency toward all-trans retinal.

enzyme: Aldehyde dehydrogenase 1A1


organism: Macaca fascicularis

proof_lines: Has a nearly 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans and 13-cis retinal.


enzyme_display_name: Retinaldehyde dehydrogenase 3

enzyme: Retinaldehyde dehydrogenase 3


enzyme_display_name: retinal dehydrogenase

organism: Oryctolagus cuniculus

substrate_name: NAD+; H2O; Hexanal

enzyme: retinal dehydrogenase

substrate: NAD+; H2O; Hexanal


enzyme_display_name: phenylacetaldehyde dehydrogenase

organism: Aromatoleum aromaticum

substrate_name: Phenylacetaldehyde; H2O; NADP+

enzyme: phenylacetaldehyde dehydrogenase

substrate: Phenylacetaldehyde; H2O; NADP+


substrate_name: NAD+; H2O; Phenylacetaldehyde

substrate: NAD+; H2O; Phenylacetaldehyde


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic

organism: Arabidopsis thaliana


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


enzyme_display_name: Aminoaldehyde dehydrogenase BADH

organism: Spinacia oleracea

enzyme: Aminoaldehyde dehydrogenase BADH


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

enzyme: Aminoaldehyde dehydrogenase 1a


enzyme_display_name: Aldehyde dehydrogenase family 3 member B1


enzyme_display_name: 2-oxoaldehyde dehydrogenase (NADP+)

substrate_name: Pyruvate; NADPH; H+

enzyme: 2-oxoaldehyde dehydrogenase (NADP+)

substrate: Pyruvate; NADPH; H+


enzyme_display_name: bilirubin oxidase

organism: Thermobaculum terrenum

substrate_name: Bilirubin; O2

enzyme: bilirubin oxidase

substrate: Bilirubin; O2


enzyme_display_name: Acyl-coenzyme A oxidase 2, peroxisomal

enzyme: Acyl-coenzyme A oxidase 2, peroxisomal


enzyme_display_name: Peroxisomal acyl-coenzyme A oxidase 1

enzyme: Peroxisomal acyl-coenzyme A oxidase 1


enzyme_display_name: acyl-CoA oxidase

substrate_name: O2; Palmitoyl-CoA

enzyme: acyl-CoA oxidase

substrate: O2; Palmitoyl-CoA


substrate_name: Palmitoyl-CoA; O2

substrate: Palmitoyl-CoA; O2


substrate_name: O2; Octanoyl-CoA

substrate: O2; Octanoyl-CoA


enzyme: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic


enzyme: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


enzyme_display_name: Aminoaldehyde dehydrogenase 1, peroxisomal

organism: Pisum sativum


enzyme_display_name: Aminoaldehyde dehydrogenase 2, peroxisomal


organism: Escherichia coli (strain K12)


enzyme: Aldehyde dehydrogenase family 3 member B1


enzyme_display_name: carboxylate reductase (NADP+)

organism: Nocardia iowensis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: Vmax is 3 times higher than that of the natural enzyme when recombinant apo-Car is incubated with the purified PPTase Npt and CoA.

enzyme: carboxylate reductase (NADP+)


organism: Acanthopagrus schlegelii

sequence: SGLLINQPKYSWLKELGL

wild_type_sequence: SGLLINQPKYSWLKELGL


enzyme_display_name: cinnamoyl-CoA reductase

organism: Fragaria x ananassa

substrate_name: caffeoyl-CoA

assay_conditions_summary: pH 6; 298.15 K; cofactor CoA

enzyme: cinnamoyl-CoA reductase

substrate: caffeoyl-CoA


enzyme_display_name: Cinnamoyl-CoA reductase 1

organism: Medicago truncatula

assay_conditions_summary: pH 6.25; cofactor CoA

proof_lines: kcat is 60.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 5.5 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 3.1 min(-1) with ca

enzyme: Cinnamoyl-CoA reductase 1


enzyme_display_name: Cinnamoyl-CoA reductase 2

proof_lines: kcat is 18.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 12.0 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 9.0 min(-1) with c

enzyme: Cinnamoyl-CoA reductase 2


enzyme_display_name: Cinnamoyl-CoA reductase CAD2

proof_lines: kcat is 0.46 sec(-1) with coumaraldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 0.10 sec(-1) with coniferaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 0.24 sec(-1)

enzyme: Cinnamoyl-CoA reductase CAD2


organism: Petunia hybrida

proof_lines: kcat is 1.2 sec(-1) with p-coumaroyl-CoA as substrate (PubMed:25217505). kcat is 5.8 sec(-1) with feruloyl-CoA as substrate (PubMed:25217505). kcat is 3.4 sec(-1) with sinapoyl-CoA as substrate (PubMed:25217505).


organism: Mycobacterium smegmatis

substrate_name: H2O; Succinate semialdehyde; NADP+

substrate: H2O; Succinate semialdehyde; NADP+


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: butyrlaldehyde (in the presence of HsaF)

proof_lines: kcat is 9.4 sec(-1) with acetaldehyde as substrate (in the presence of HsaF). kcat is 19.0 sec(-1) with acetaldehyde as substrate (in the absence of HsaF). kcat is 11.1 sec(-1) with propanal as substrate (in the presence of HsaF). kcat is 2


organism: Paraburkholderia xenovorans

substrate_name: pentaldehyde

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

substrate: pentaldehyde


organism: Mus musculus

substrate_name: Unknown


organism: Streptomyces coelicolor

proof_lines: product inhibition, with 1-pyrroline-5-carboxylate


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

proof_lines: kcat is 26 sec(-1) with glyceraldehyde as substrate, 20 sec(-1) with glyceraldehyde-3-phosphate as substrate, 37 sec(-1) with glycolaldehyde as substrate and 25 sec(-1) with NADP as substrate (at pH 7.9 and 58 degrees Celsius).


enzyme_display_name: UniProt G3X982

proof_lines: kcat is 4 sec(-1) for phthalazine oxidation (PubMed:11562361). kcat is 130 min(-1) for benzaldehyde oxidation, 384 min(-1) for butyraldehyde oxidation and 1279 min(-1) for 2-OH-pyrimidine oxidation (PubMed:21705476). kcat is 41.1 min(-1) fo

enzyme: UniProt G3X982


enzyme_display_name: Aldehyde oxidase 4

enzyme: Aldehyde oxidase 4


enzyme_display_name: aldehyde oxidase

organism: Oryctolagus cuniculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A1081V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; buffer 80 mM phosphate

proof_lines: mutant enzyme A1081V, in 80 mM phosphate buffer, pH 7.4, at 37°C

enzyme: aldehyde oxidase


enzyme_display_name: (methyl)glyoxal oxidase

organism: Phanerodontia chrysosporium

assay_conditions_summary: pH 6

proof_lines: at pH 6.0, temperature not specified in the publication

proof_lines: at pH 4.5, temperature not specified in the publication

enzyme: (methyl)glyoxal oxidase


enzyme_display_name: 2-Hydroxyacid oxidase 1

organism: Homo sapiens

substrate_name: 2-hydroxy octanoate (at pH 7.5 and 37 degrees Celsius, with DCIP as electron acceptor)

assay_conditions_summary: pH 7

proof_lines: kcat is 3.6 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 4.1 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.5 and 37 degr

enzyme: 2-Hydroxyacid oxidase 1


enzyme_display_name: L-lactate oxidase

organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)

enzyme: L-lactate oxidase


enzyme_display_name: Pyruvate:ferredoxin oxidoreductase

organism: Moorella thermoacetica (strain ATCC 39073 / JCM 9320)

substrate_name: oxidized ferredoxin

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 3.2 sec(-1) for the synthesis of pyruvate from acetyl-CoA and CO2 with methyl viologen as electron donor (PubMed:10878009). kcat is 2.0 sec(-1) for the synthesis of pyruvate from acetyl-CoA and CO2 with reduced ferredoxin as electro

enzyme: Pyruvate:ferredoxin oxidoreductase

substrate: oxidized ferredoxin


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta

organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta


enzyme_display_name: 2-oxoacid oxidoreductase (ferredoxin)

organism: Halobacterium salinarum

proof_lines: cosubstrates: 1 mM pyruvate, 0.05 mM CoA, pH and temperature not specified in the publication

proof_lines: cosubstrates: 1 mM 2-oxoxbutyrate, 0.05 mM CoA, pH and temperature not specified in the publication

enzyme: 2-oxoacid oxidoreductase (ferredoxin)


enzyme_display_name: Indole-3-acetaldehyde oxidase

organism: Arabidopsis thaliana

proof_lines: Kinetic values were obtained with the AO-alpha dimer.

enzyme: Indole-3-acetaldehyde oxidase


proof_lines: Kinetic values were obtained with the AO-gamma dimer.


proof_lines: kcat is 95.2 sec(-1) with benzoic acid (BA) as substrate, 1.904 sec(-1) with indole-3-acetaldehyde as substrate, and 436.5 sec(-1) with cinnamylaldehyde as substrate (at pH 7, PubMed:19297586).


organism: Zea mays


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Bos taurus

substrate_name: Pyruvate; NAD+; Coenzyme A

enzyme: dihydrolipoyl dehydrogenase

substrate: Pyruvate; NAD+; Coenzyme A


enzyme_display_name: Pyruvate dehydrogenase [ubiquinone]

organism: Escherichia coli (strain K12)

substrate_name: pyruvate, non-activated form

proof_lines: kcat is 7 sec(-1) for non-activated, 200 sec(-1) for activated form.

enzyme: Pyruvate dehydrogenase [ubiquinone]

substrate: pyruvate, non-activated form


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase subunit alpha

organism: Sulfolobus sp

proof_lines: kcat is 51 sec(-1) for pyruvate as substrate (PubMed:11683888). kcat is 19 sec(-1) for 2-oxoglutarate as substrate (PubMed:11683888).


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase subunit beta


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

enzyme: 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta


enzyme: 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha


enzyme: 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta


enzyme: 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha


enzyme_display_name: PE-PGRS family protein PE_PGRS45

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

enzyme: PE-PGRS family protein PE_PGRS45


enzyme_display_name: Aldehyde oxidase 4


enzyme_display_name: aldehyde oxidase

proof_lines: kcat is 6.4 min(-1) for benzaldehyde oxidation, 5.6 min(-1) for phthalazine oxidation, 12.2 min(-1) for phenanthridine oxidation and 5.6 min(-1) for chloroquinazolinone oxidation.


organism: Macaca fascicularis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V1085A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V1085A, in 80 mM phosphate buffer, pH 7.4, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M1009I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M1009I, in 80 mM phosphate buffer, pH 7.4, at 37°C


enzyme_display_name: Aldehyde oxidase 1

organism: Mus musculus

proof_lines: kcat is 317.6 min(-1) for benzaldehyde oxidation, 128.1 min(-1) for phthalazine oxidation, 49.5 min(-1) for retinal oxidation, and 519.9 min(-1) for acetaldehyde oxidation (at 30 degrees Celsius and pH 7.5) (PubMed:19401776). However in thi

enzyme: Aldehyde oxidase 1


enzyme_display_name: coproporphyrinogen III oxidase (coproporphyrin-forming)

organism: Halothece sp. PCC 7418

substrate_name: protoporphyrinogen IX

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

proof_lines: pH and temperature not specified in the publication

substrate: protoporphyrinogen IX


organism: Apium graveolens

substrate_name: NADP+; H2O; D-Glyceraldehyde 3-phosphate

assay_conditions_summary: pH 7.7; cofactor NADP+

proof_lines:
competitive below 0.04 mM
noncompetitive above 0.075 mM


organism: Spinacia oleracea

substrate_name: H2O; D-Glyceraldehyde 3-phosphate; NADP+


organism: Triticum aestivum

substrate_name: H2O; NADP+; D-Glyceraldehyde 3-phosphate


organism: Thermoproteus tenax

sequence_variant_note: Mutation signature G1P/F6P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: cofactor ADP

proof_lines: Km applies to a data set exhibiting Michaelis-Menten kinetics. When an enzyme does not exhibit Michaelis-Menten kinetics the binding affinity is simply expressed as S0.5 which corresponds to the observed substrate concentration for 0.5 x Vm


enzyme_display_name: Aldehyde dehydrogenase family 3 member A2

organism: Homo sapiens

proof_lines: kcat is 2.18 sec(-1) for decanal as substrate. kcat is 2.23 sec(-1) for dodecanal as substrate. kcat is 0.86 sec(-1) for tetradecanal as substrate. kcat is 0.95 sec(-1) for hexadecanal as substrate. kcat is 1.52 sec(-1) for octadecanal as s


enzyme_display_name: 3-sulfolactaldehyde dehydrogenase

organism: Pseudomonas putida

proof_lines: kcat is 11.8 sec(-1) for 4-oxobutanoate oxidation with NAD(+). kcat is 11.4 sec(-1) for 4-oxobutanoate oxidation with NADP(+).

enzyme: 3-sulfolactaldehyde dehydrogenase


enzyme_display_name: Coproporphyrinogen III oxidase

organism: Bacillus subtilis (strain 168)

substrate_name: coproporphyrinogen III

proof_lines: kcat is 0.05 min(-1) with coproporphyrinogen III as substrate (PubMed:9784236). kcat is 0.19 min(-1) with protoporphyrinogen IX as substrate (PubMed:9784236). kcat is 2.69 min(-1) with mesoporphyrinogen IX as substrate (PubMed:9784236).

enzyme: Coproporphyrinogen III oxidase

substrate: coproporphyrinogen III


enzyme_display_name: L-galactonolactone oxidase

organism: Trypanosoma cruzi

assay_conditions_summary: pH 8; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA

enzyme: L-galactonolactone oxidase


enzyme_display_name: albonoursin synthase

organism: Streptomyces noursei

substrate_name: cyclo(L-Leu-L-Phe)

assay_conditions_summary: pH 8; buffer 100 mM Tris/HCl

proof_lines: in 100 mM Tris/HCl buffer, pH 8.0, at 30°C

proof_lines: kcat is 0.453 and 0.69 sec(-1) for cyclo(L-Phe-L-His) and cyclo(L-Phe-L-Leu), respectively.

enzyme: albonoursin synthase

substrate: cyclo(L-Leu-L-Phe)


enzyme_display_name: UniProt Q02127

substrate_name: dihydroorotate

enzyme: UniProt Q02127

substrate: dihydroorotate


substrate_name: coenzyme Q0

substrate: coenzyme Q0


enzyme_display_name: UniProt Q63707

organism: Rattus norvegicus

enzyme: UniProt Q63707


enzyme_display_name: benzylmalonyl-CoA dehydrogenase

organism: Aromatoleum aromaticum

substrate_name: benzylmalonyl-CoA

assay_conditions_summary: pH 7.8; cofactor CoA

proof_lines: at pH 7.8, temperature not specified in the publication

proof_lines: kcat is 3.5 sec(-1) with benzylmalonyl-CoA as substrate.

enzyme: benzylmalonyl-CoA dehydrogenase

substrate: benzylmalonyl-CoA


enzyme_display_name: fumarate reductase (CoM/CoB)

organism: Methanothermobacter thermautotrophicus

substrate_name: fumarate

enzyme: fumarate reductase (CoM/CoB)

substrate: fumarate


organism: Saccharomyces cerevisiae


substrate_name: oxygen

substrate: oxygen


substrate: Unknown


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

proof_lines: kcat is 1.33 min(-1) with coproporphyrinogen III as substrate (PubMed:25908396). kcat is 0.46 min(-1) with coproporphyrinogen III as substrate (PubMed:27597779). kcat is 0.44 min(-1) with protoporphyrinogen IX as substrate (PubMed:27597779)


enzyme_display_name: 9,9'-dicis-zeta-carotene desaturase

organism: Rubrivivax gelatinosus

substrate_name: phytoene

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

enzyme: 9,9'-dicis-zeta-carotene desaturase

substrate: phytoene


proof_lines: pH 8.0, 28°C, recombinant wild-type enzyme


enzyme_display_name: succinate dehydrogenase (ubiquinone)

organism: Ascaris suum

substrate_name: Reduced acceptor; Fumarate

enzyme: succinate dehydrogenase (ubiquinone)

substrate: Reduced acceptor; Fumarate


enzyme_display_name: succinate dehydrogenase

substrate_name: Fumarate

enzyme: succinate dehydrogenase

substrate: Fumarate


substrate_name: Succinate; Ubiquinone-2

substrate: Succinate; Ubiquinone-2


substrate_name: Acceptor; Succinate

substrate: Acceptor; Succinate


substrate_name: FAD; Succinate

assay_conditions_summary: cofactor FAD

substrate: FAD; Succinate


organism: Shewanella frigidimarina


substrate_name: succinate

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

substrate: succinate


organism: Desulfobulbus elongatus


enzyme_display_name: dihydroorotate dehydrogenase (quinone)

organism: Lactococcus lactis

enzyme: dihydroorotate dehydrogenase (quinone)


organism: Enterococcus faecalis

substrate_name: S-dihydroorotate

substrate: S-dihydroorotate


organism: Bacillus subtilis

substrate_name: Menadione; L-Dihydroorotate

substrate: Menadione; L-Dihydroorotate


enzyme_display_name: Acetyl-CoA decarbonylase/synthase complex subunit alpha 1

organism: Methanosarcina barkeri (strain Fusaro / DSM 804)

substrate_name: Unknown


enzyme_display_name: anaerobic carbon monoxide dehydrogenase

organism: Rhodospirillum rubrum

proof_lines: noncompetitive inhibition vs. methyl viologen

enzyme: anaerobic carbon monoxide dehydrogenase


enzyme_display_name: aldehyde ferredoxin oxidoreductase

organism: Pyrococcus furiosus

substrate_name: Formaldehyde; Methyl viologen; H2O

proof_lines: Significant activity only with aliphatic and aromatic aldehydes and only at low concentration (0.5 mM).

enzyme: aldehyde ferredoxin oxidoreductase

substrate: Formaldehyde; Methyl viologen; H2O


organism: Thermococcus litoralis

proof_lines: Significant activity only with aliphatic aldehydes up to C3 and only at high concentration (15 mM).


enzyme_display_name: NAD-dependent dihydropyrimidine dehydrogenase subunit PreA

organism: Escherichia coli (strain K12)


enzyme_display_name: NAD-dependent dihydropyrimidine dehydrogenase subunit PreT


organism: Ipomoea batatas


enzyme_display_name: fumarate reductase (menaquinone)

organism: Mycobacterium bovis

enzyme: fumarate reductase (menaquinone)


organism: Drosophila melanogaster

substrate_name: (S)-dihydroorotate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Δ22 to reconstruct the assayed variant sequence.

mutation_type: deletion

substrate: (S)-dihydroorotate


mutation_signature: Δ2

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Δ2 to reconstruct the assayed variant sequence.

proof_lines:
DELTA2-21 mutant enzyme
DELTA2-37 mutant enzyme


substrate_name: decylubiquinone

substrate: decylubiquinone


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E101L with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: pH 8.0, 25°C, recombinant subunit SDHC mutant E101L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G227L with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant subunit SDHB mutant G227L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E101D with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant subunit SDHC mutant E101D


organism: Candida albicans

substrate_name: dihydroorotate

proof_lines: full-length DHODH, fixed concentration of dihydroorotate of 1.0 mM and varied concentrations of decylubiquinone from 0-0.2 mM

proof_lines: full-length DHODH, concentration of dihydroorotate varied from 0-1.0 mM at fixed concentrations of 0.1 mM decylubiquinone and 0.06 mM 2,6-dichloroindophenol

substrate: dihydroorotate


mutation_signature: N-terminally truncated DHODH N-terminally truncated DHODH

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

mutation_type: truncation


mutation_signature: N-terminally truncated DHODH / 6-dichloroindophenol from 0-0.2 mM N-terminally truncated DHODH

proof_lines: N-terminally truncated DHODH, fixed concentration of dihydroorotate and varied concentrations of 2,6-dichloroindophenol from 0-0.2 mM


mutation_signature: N-terminally truncated DHODH / fixed concentration of dihydroorotate of 1.0 mM and varied concentrations of decylubiquinone from 0-0.2 mM N-terminally truncated

proof_lines: N-terminally truncated DHODH, fixed concentration of dihydroorotate of 1.0 mM and varied concentrations of decylubiquinone from 0-0.2 mM


mutation_signature: N-terminally truncated DHODH / 6-dichloroindophenol N-terminally truncated DHODH

proof_lines: N-terminally truncated DHODH, concentration of dihydroorotate varied from 0-1.0 mM at fixed concentrations of 0.1 mM decylubiquinone and 0.06 mM 2,6-dichloroindophenol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S33C with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S33T with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S33A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

substrate_name: fumarate (adult complex II, at 25 degrees Celsius and in anaerobic conditions)

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

proof_lines: kcat is 6000 min(-1) with fumarate as substrate (adult complex II, at 25 degrees Celsius and in anaerobic conditions).


enzyme_display_name: Succinate dehydrogenase [rhodoquinone] flavoprotein subunit 1, mitochondrial

substrate: fumarate (adult complex II, at 25 degrees Celsius and in anaerobic conditions)


substrate_name: fumarate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E49A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

substrate: fumarate


substrate_name: succinate (at 37 degrees Celsius)

enzyme: Succinate dehydrogenase [rhodoquinone] flavoprotein subunit 1, mitochondrial

substrate: succinate (at 37 degrees Celsius)


enzyme_display_name: Protoporphyrinogen IX dehydrogenase [quinone]

substrate_name: protoporphyrinogen IX

proof_lines: kcat for protoporphyrinogen IX is 17.52 min(-1) and for menadione is 16.86 min(-1).

substrate: protoporphyrinogen IX


substrate_name: menadione (a soluble menaquinone analog)

enzyme: Protoporphyrinogen IX dehydrogenase [quinone]


enzyme_display_name: coproporphyrinogen III oxidase (coproporphyrin-forming)

organism: Phormidium nigroviride

proof_lines: pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E49L with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: mutant E49L, cosubstrate menaquinone, pH 7.9, 30°C

proof_lines: mutant E49L, cosubstrate ubiquinone, pH 7.9, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E49F with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: mutant E49F, cosubstrate menaquinone, pH 7.9, 30°C

proof_lines: mutant E49F, cosubstrate ubiquinone, pH 7.9, 30°C


proof_lines: mutant E49F, cosubstrate menaquinone, pH 7.0, 30°C


proof_lines: mutant E49L, cosubstrate menaquinone, pH 7.0, 30°C


substrate_name: menaquinone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E29L to reconstruct the assayed variant sequence.

substrate: menaquinone


organism: Mycobacterium smegmatis

substrate_name: Reduced acceptor; Fumarate

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

substrate: Reduced acceptor; Fumarate


organism: Ascaris suum

substrate_name: succinate (free larvae complex II, at 25 degrees Celsius)

enzyme: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial


organism: Mammalia


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate: Unknown


organism: Bos taurus

substrate_name: Ubiquinone; L-Dihydroorotate

substrate: Ubiquinone; L-Dihydroorotate


organism: Homo sapiens

substrate_name: L-Dihydroorotate; Ubiquinone

substrate: L-Dihydroorotate; Ubiquinone


enzyme_display_name: Dihydroorotate dehydrogenase (quinone), mitochondrial

organism: Plasmodium falciparum (isolate 3D7)


organism: Rattus norvegicus

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


organism: Saccharomyces kluyveri

substrate_name: L-Dihydroorotate; Decylubiquinone

substrate: L-Dihydroorotate; Decylubiquinone


organism: Schizosaccharomyces pombe

substrate_name: Decylubiquinone; L-Dihydroorotate

substrate: Decylubiquinone; L-Dihydroorotate


organism: Helicobacter pylori

substrate_name: Fumarate; Reduced acceptor

substrate: Fumarate; Reduced acceptor


organism: Capsicum annuum

substrate_name: Neurosporene; Decylplastoquinone

substrate: Neurosporene; Decylplastoquinone


enzyme_display_name: 6-hydroxynicotinate reductase

organism: Eubacterium barkeri

substrate_name: reduced ferrodoxin

enzyme: 6-hydroxynicotinate reductase

substrate: reduced ferrodoxin


organism: Escherichia coli (strain K12)


enzyme_display_name: 15-cis-phytoene desaturase

organism: Narcissus pseudonarcissus

enzyme: 15-cis-phytoene desaturase


enzyme_display_name: Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial

substrate_name: ubquinone-1 (free larvae complex II, succinate as cosubstrate and at 25 degrees Celsius)


enzyme_display_name: succinate dehydrogenase (ubiquinone)

organism: Escherichia coli

substrate_name: Menaquinone; Succinate

substrate: Menaquinone; Succinate


substrate_name: Ubiquinone; Succinate

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

substrate: Ubiquinone; Succinate


organism: Shewanella frigidimarina


substrate_name: FADH2; Fumarate

substrate: FADH2; Fumarate


organism: Bacillus subtilis


enzyme_display_name: 2-methylene-furan-3-one reductase

organism: Solanum lycopersicum

proof_lines: kcat is 0.39 sec(-1) with EDHMF as substrate. kcat is 0.34 sec(-1) with HMPDF as substrate. kcat is 0.15 sec(-1) with BDHMF as substrate.

enzyme: 2-methylene-furan-3-one reductase


enzyme_display_name: prephenate dehydrogenase

organism: Aquifex aeolicus

substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S126A to reconstruct the assayed variant sequence.

enzyme: prephenate dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R250Q with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


substrate_name: prephenate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H197N with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

substrate: prephenate


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D300A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 295.15 K; cofactor CoA

proof_lines: recombinant His-tagged mutant D300A, pH 6.0, 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E276A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant E276A, pH 6.0, 22°C


enzyme_display_name: Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit

organism: Bacillus subtilis (strain 168)


substrate_name: NADP+; Acenaphthen-1-ol

assay_conditions_summary: cofactor NADP+

proof_lines: kcat is 0.29 min(-1) for the reduction of progesterone (PubMed:10998348). kcat is 1.1 min(-1) for the reduction of 3beta-hydroxy-5beta-pregnane-20-one (PubMed:10998348). kcat is 1.2 min(-1) for the oxidation of (20S)-hydroxypregn-4-en-3-one

substrate: NADP+; Acenaphthen-1-ol


proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of


enzyme_display_name: 3-oxo-5-alpha-steroid 4-dehydrogenase 2

enzyme: 3-oxo-5-alpha-steroid 4-dehydrogenase 2


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

organism: Staphylococcus aureus

substrate_name: dodecenoyl-[Staphylococcus aureus acyl carrier protein]

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A95V with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 298.15 K; buffer 100 mM Na2HPO4

proof_lines: mutant enzyme A95V, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)


substrate_name: crotonyl-[acyl-carrier protein]

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y147H with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y147H, pH and temperature not specified in the publication

enzyme: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

substrate: crotonyl-[acyl-carrier protein]


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M99T with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M99T, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y147F with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y147F, pH and temperature not specified in the publication


enzyme_display_name: 2-alkenal reductase (NADP(+)-dependent)

organism: Nicotiana tabacum

substrate_name: methyl-trans-2-methylcinnamaldehyde (at pH 7.3)

assay_conditions_summary: pH 7.3; cofactor NADPH

proof_lines: kcat is 3.3 sec(-1) for (R)-pulegone at pH 7.0. kcat is 2.8 sec(-1) for (S)-pulegone at pH 7.0. kcat is 1.3 sec(-1) for NADPH at pH 7.3. kcat is 1.46 sec(-1) for 1-nitrocyclohexene at pH 7.3. kcat is 9.2 sec(-1) for 2-methylpentenal at pH 5

enzyme: 2-alkenal reductase (NADP(+)-dependent)


organism: Fragaria ananassa

proof_lines: kcat is 1.94 sec(-1) with EDHMF as substrate. kcat is 2.69 sec(-1) with HMPDF as substrate. kcat is 1.43 sec(-1) with BDHMF as substrate.


enzyme_display_name: 3-oxo-5-alpha-steroid 4-dehydrogenase 1

organism: Homo sapiens

enzyme: 3-oxo-5-alpha-steroid 4-dehydrogenase 1


enzyme_display_name: biliverdin reductase

substrate_name: NADP+

assay_conditions_summary: pH 7.2; cofactor NADP+

proof_lines: in the presence of 3 M urea, at pH 7.2 and 25°C

proof_lines: in the absence of urea, at pH 7.2 and 25°C

enzyme: biliverdin reductase

substrate: NADP+


substrate_name: biliverdin

substrate: biliverdin


assay_conditions_summary: pH 7.2; cofactor NAD+


substrate_name: methyl 2,3-dihydro-2,3-dihydroxybenzoate (at pH 7.4 and 37 degrees Celsius)

proof_lines: kcat is 5550 min(-1) for dehydrogenase activity with 2,3-dihydro-2,3-dihydroxybenzoate as substrate (at pH 7.4 and 37 degrees Celsius). kcat is 1380 min(-1) for dehydrogenase activity with cis-3-hydroxy-4-cyclohexene-1-carboxylate as substr


organism: Pseudomonas putida


organism: Yersinia pestis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T267Y with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T267V with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T267S with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T267G with inferred residue-numbering offset +9 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.

proof_lines: IC50 above 0.05 mM, wild type enzyme, at pH 8.0 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T267W with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


enzyme_display_name: arogenate dehydrogenase (NADP+)

organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1

proof_lines: pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1

enzyme: arogenate dehydrogenase (NADP+)


enzyme_display_name: acrylyl-CoA reductase (NADPH)

organism: Cereibacter sphaeroides

substrate_name: NADH

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: pH 7.0, 30°C, recombinant His-tagged enzyme

enzyme: acrylyl-CoA reductase (NADPH)

substrate: NADH


organism: Ruegeria pomeroyi


enzyme_display_name: Crotonyl-CoA carboxylase/reductase

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

substrate_name: (2E)-butenoyl-CoA (in the reductive carboxylation assay)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 104 sec(-1) for the reductive carboxylation of (2E)-butenoyl-CoA (PubMed:17548827). Acryloyl-CoA is accepted as an alternative substrate analog by the enzyme with 40% relative activity (compared with Vmax of crotonyl-CoA carboxylati

enzyme: Crotonyl-CoA carboxylase/reductase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G95S with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


organism: Haemophilus influenzae

substrate_name: NADH; H+; But-2-enoyl-[acyl-carrier protein]

assay_conditions_summary: cofactor NADH


enzyme_display_name: Fatty acid synthase

enzyme: Fatty acid synthase

substrate: Unknown


organism: Rattus norvegicus


enzyme_display_name: 12-oxophytodienoate reductase 3

enzyme: 12-oxophytodienoate reductase 3


enzyme_display_name: Prostaglandin reductase 1

organism: Cavia porcellus

enzyme: Prostaglandin reductase 1


enzyme_display_name: Prostaglandin reductase-3

organism: Mus musculus

proof_lines: kcat is 8.6 min(-1) for 15-keto-PGE2, 4.37 min(-1) for 15-keto-PGE1, 11.55 for min(-1) for 15-keto-PGF2-alpha, 11.45 min(-1) for 15-keto-PGF1-alpha.

enzyme: Prostaglandin reductase-3


organism: Sus scrofa

column_label: Table 2 is labelled Apparent Km and Vmax values for pig lung PGR; the 15-oxo-PGE1 row reports Native Vmax 2470 in the Vmax (m-units/mg) column.

normalized_value_unit_evidence: Vmax central normalized_value=2470 normalized_unit=nmol/min/mg.

raw_value_unit_evidence: Table 2 reports the 15-oxo-PGE1 row under Vmax (m-units/mg), Native as raw_value=2470 raw_unit=m-units/mg.

row_label: Native pig lung PGR / 15-oxo-PGE1

table_label: Biochem. J. 1998 Table 2


organism: Digitalis lanata

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


enzyme_display_name: Delta4-3-oxosteroid 5beta-reductase

assay_conditions_summary: cofactor NADPH

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

enzyme: Delta4-3-oxosteroid 5beta-reductase


enzyme_display_name: protochlorophyllide reductase

organism: Thermosynechococcus elongatus

substrate_name: Protochlorophyllide; H+; NADPH

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: AbstractText; thermophilic POR reaction prose; K(m) NADPH raw value 0.013 uM; V(max) metric raw value 0.53 uM min^-1.

raw_value_unit_evidence: Abstract reports K(m) for NADPH = 0.013 uM and V(max) = 0.53 uM min^-1.

row_label: Thermophilic POR steady-state reaction; V(max) prose

table_label: PMID 16307122 PubMed abstract / RSC article abstract

enzyme: protochlorophyllide reductase

substrate: Protochlorophyllide; H+; NADPH


enzyme_display_name: trans-2-enoyl-CoA reductase (NADPH)

organism: Bos taurus

substrate_name: H+; NADPH; trans-Dec-2-enoyl-CoA

enzyme: trans-2-enoyl-CoA reductase (NADPH)

substrate: H+; NADPH; trans-Dec-2-enoyl-CoA


substrate_name: H+; trans-Hex-2-enoyl-CoA; NADPH

substrate: H+; trans-Hex-2-enoyl-CoA; NADPH


enzyme_display_name: albonoursin synthase

organism: Streptomyces noursei

substrate_name: cyclo(L-Phe-L-His)

assay_conditions_summary: pH 8; 303.15 K; buffer 100 mM Tris/HCl

proof_lines: in 100 mM Tris/HCl buffer, pH 8.0, at 30°C

proof_lines: kcat is 0.453 and 0.69 sec(-1) for cyclo(L-Phe-L-His) and cyclo(L-Phe-L-Leu), respectively.

enzyme: albonoursin synthase

substrate: cyclo(L-Phe-L-His)


enzyme_display_name: Aclacinomycin-N/aclacinomycin-A oxidase

organism: Streptomyces galilaeus

substrate_name: AclA

proof_lines: kcat is 0.17 sec(-1) for oxidase activity with AclA.

enzyme: Aclacinomycin-N/aclacinomycin-A oxidase

substrate: AclA


enzyme_display_name: Coproporphyrinogen III oxidase

organism: Bacillus subtilis (strain 168)

substrate_name: mesoporphyrinogen IX

proof_lines: kcat is 0.05 min(-1) with coproporphyrinogen III as substrate (PubMed:9784236). kcat is 0.19 min(-1) with protoporphyrinogen IX as substrate (PubMed:9784236). kcat is 2.69 min(-1) with mesoporphyrinogen IX as substrate (PubMed:9784236).

enzyme: Coproporphyrinogen III oxidase

substrate: mesoporphyrinogen IX


enzyme_display_name: Benzylmalonyl-CoA dehydrogenase

organism: Aromatoleum aromaticum (strain DSM 19018 / LMG 30748 / EbN1)

substrate_name: Unknown

proof_lines: kcat is 3.5 sec(-1) with benzylmalonyl-CoA as substrate.

enzyme: Benzylmalonyl-CoA dehydrogenase


organism: Escherichia coli (strain K12)

assay_conditions_summary: pH 6

proof_lines: kcat is 0.17 min(-1) for decarboxylation of coproporphyrinogen-III (at pH 6 and at 37 degrees Celsius).


enzyme_display_name: coproporphyrinogen oxidase

organism: Homo sapiens

substrate_name: Coproporphyrinogen-III

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R262A to reconstruct the assayed variant sequence.

proof_lines: mutant R262A, divinyl product, 37°C, pH not specified in the publication

proof_lines: mutant R262A, total product, 37°C, pH not specified in the publication

enzyme: coproporphyrinogen oxidase

substrate: Coproporphyrinogen-III


organism: Mycobacterium tuberculosis

substrate_name: 2-trans-Dodecenoyl-CoA; H+; NADH

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: kcat is 320.4 min(-1) for the reduction of 2-trans-dodecenoyl-CoA (at pH 7.5 and 25 degrees Celsius) (PubMed:21143326). kcat is 278 min(-1) for the reduction of 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius) (PubMed:10521269).

substrate: 2-trans-Dodecenoyl-CoA; H+; NADH