substrate_name: tyramine

column_label: table label: Table 1 (Comparison of steady-state kinetic values for zMAO-catalyzed oxidation of amine substrate analogues with those published for hMAO A and hMAO B.); row label: Tyramine; column label: kcat (min^-1); Km (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 1 Tyramine; kcat 7.78 s^-1, kcat_over_km 432.2222222222223 s^-1 mM^-1, km 0.018 mM.

normalized_value_unit_evidence: kcat normalized value: 7.78; normalized unit: s^-1; kcat_over_km normalized value: 432.2222222222223; normalized unit: s^-1 mM^-1; km normalized value: 0.018; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 467 +/- 20; raw unit: min^-1; km raw value: 18 +/- 3; raw unit: uM; kcat_over_km raw value: 7.78 / 0.018; raw unit: s^-1 per mM

row_label: Tyramine

substrate: tyramine


enzyme_display_name: monoamine oxidase

organism: Danio rerio

substrate_name: Unknown

source_db: brenda

verification_status: unverified

kcat_display: Not reported

km_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

ki_unit: mM

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

proof_lines: at 25°C in 50 mM potassium phosphate, pH 7.4

enzyme: monoamine oxidase

substrate: Unknown

status: unverified

source: brenda


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Streptomyces clavuligerus

substrate_name: penicillin G

ki_display: Not reported

kcat_over_km_origin: calculated

km_unit: mM

sequence_source: UniProt P18548 canonical cefE sequence

sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature V275I to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines:
pH 6.5, 30°C, recombinant mutant V275I
mutant enzyme V275I

data_origin: experimental

enzyme: deacetoxycephalosporin-C synthase

substrate: penicillin G


sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature N304K to reconstruct the assayed variant sequence.

proof_lines:
pH 6.5, 30°C, recombinant mutant N304K
mutant enzyme N304K


sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature C281Y to reconstruct the assayed variant sequence.

proof_lines:
pH 6.5, 30°C, recombinant mutant C281Y
mutant enzyme C281Y


sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature I305M to reconstruct the assayed variant sequence.

proof_lines: mutant I305M, pH and temperature not specified in the publication


substrate_name: Penicillin N

sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature G79E to reconstruct the assayed variant sequence.

substrate: Penicillin N


sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature I305L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature V275I/I305M to reconstruct the assayed variant sequence.

proof_lines: pH 6.5, 30°C, recombinant mutant V275I/I305M

proof_lines: pH 6.5, 30°C, recombinant mutants V275I and I305M


sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature C281Y/I305L to reconstruct the assayed variant sequence.

proof_lines: pH 6.5, 30°C, recombinant mutants C281Y and I305L


sequence_variant_note: Resolved canonical sequence from UniProt P18548 canonical cefE sequence and applied mutation signature G79E/I305M to reconstruct the assayed variant sequence.

proof_lines: pH 6.5, 30°C, recombinant mutants G79E and I305M


enzyme_display_name: ADP-ribose diphosphatase

substrate_name: cADP-ribose

assay_conditions_summary: pH 7.5; cofactor ADP

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

enzyme: ADP-ribose diphosphatase

substrate: cADP-ribose


substrate_name: ADP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H97A to reconstruct the assayed variant sequence.

proof_lines: mutant H97A, pH 7.5, temperature not specified in the publication

substrate: ADP


substrate_name: ADP-ribose

substrate: ADP-ribose


substrate_name: CDP-glycerol

substrate: CDP-glycerol


substrate_name: CDP-choline

substrate: CDP-choline


substrate_name: CDP-ethanolamine

substrate: CDP-ethanolamine


enzyme_display_name: xanthine oxidase

organism: Homo sapiens

substrate_name: hypoxanthine

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

proof_lines:
membrane-bound enzyme
free enzyme

enzyme: xanthine oxidase

substrate: hypoxanthine


enzyme_display_name: leukotriene-B4 20-monooxygenase

substrate_name: 20-hydroxy-leukotriene B4

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

enzyme: leukotriene-B4 20-monooxygenase

substrate: 20-hydroxy-leukotriene B4


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


substrate_name: lipoxin B4

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

substrate: lipoxin B4


smiles: CCCCCCC(CCCCCCCCCCC(=O)[O-])O


substrate_name: lipoxin A4

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

substrate: lipoxin A4


enzyme_display_name: diamine oxidase

smiles: CC(=O)NCCCNCCCCN

enzyme: diamine oxidase


substrate_name: N-acetylcadaverine

smiles: CC(=O)NCCCCCN

substrate: N-acetylcadaverine


substrate_name: acetylputrescine

smiles: CC(=O)NCCCCN

substrate: acetylputrescine


enzyme_display_name: retinal dehydrogenase

sequence_variant_note: Mutation signature H1A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 8

enzyme: retinal dehydrogenase


proof_lines:
isoform ALDH1A1, at pH 8.0 and 37°C
isoform ALDH1A3, at pH 8.0 and 37°C


enzyme_display_name: (S)-malate dehydrogenase (NAD(+), oxaloacetate-forming)

substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: enzyme from normal breast tissue, at pH 8.0, temperature not specified in the publication

proof_lines: enzyme from cancerous breast tissue, at pH 8.0, temperature not specified in the publication

substrate: NAD+


substrate_name: (S)-malate

enzyme: (S)-malate dehydrogenase (NAD(+), oxaloacetate-forming)

substrate: (S)-malate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M73T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T91A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H244Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M188I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L277Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A106T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C155Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M188V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C155Y/Y184H/V275I/C281Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y184H to reconstruct the assayed variant sequence.


substrate_name: ampicillin

sequence_variant_note: Mutation signature C281Y/R306L references residue 281, which is outside the resolved sequence length.

substrate: ampicillin


sequence_variant_note: Mutation signature N304K references residue 304, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature V275I/N304R references residue 275, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature N304A references residue 304, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature V275I/N304K references residue 275, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature N304L references residue 304, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature C281F references residue 281, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature V275I/N304A references residue 275, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature V275I/N304L references residue 275, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature C281Y/N304L references residue 281, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature C281Y/N304R references residue 281, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature V275I references residue 275, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature C281Y references residue 281, which is outside the resolved sequence length.


enzyme_display_name: glutaconate CoA-transferase

organism: Acidaminococcus fermentans

substrate_name: glutaconyl-CoA

verification_status: verified

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

assay_conditions_summary: cofactor CoA

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Glutaconyl-CoA; cosubstrate glutarate; column Apparent Km (mM) = 0.017; V relative = 100; normalized Km 0.017 mM

raw_value_unit_evidence: row Glutaconyl-CoA; cosubstrate glutarate; apparent Km 0.017 mM; V relative 100

row_label: Glutaconyl-CoA

enzyme: glutaconate CoA-transferase

substrate: glutaconyl-CoA

status: verified


substrate_name: acetyl-CoA

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Acetyl-CoA; cosubstrate glutaconate; column Apparent Km (mM) = 0.17; V relative = 12; normalized Km 0.17 mM

normalized_value_unit_evidence: Km 0.17 mM

raw_value_unit_evidence: row Acetyl-CoA; cosubstrate glutaconate; apparent Km 0.17 mM; V relative 12

row_label: Acetyl-CoA

substrate: acetyl-CoA


substrate_name: glutaconate

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

assay_conditions_summary: pH 7; cofactor CoA

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Glutaconate; cosubstrate acetyl-CoA; column Apparent Km (mM) = 0.2; V relative = 12; normalized Km 0.2 mM

normalized_value_unit_evidence: Km 0.2 mM

raw_value_unit_evidence: row Glutaconate; cosubstrate acetyl-CoA; apparent Km 0.2 mM; V relative 12

row_label: Glutaconate

substrate: glutaconate


substrate_name: Glutarate

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

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Glutarate; cosubstrate glutaconyl-CoA; column Apparent Km (mM) = 0.7; V relative = 100; normalized Km 0.7 mM

normalized_value_unit_evidence: Km 0.7 mM

raw_value_unit_evidence: row Glutarate; cosubstrate glutaconyl-CoA; apparent Km 0.7 mM; V relative 100

row_label: Glutarate

substrate: Glutarate


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

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row (R)-2-Hydroxyglutarate; cosubstrate glutaconyl-CoA; column Apparent Km (mM) = 1.5; V relative = 100; normalized Km 1.5 mM

normalized_value_unit_evidence: Km 1.5 mM

raw_value_unit_evidence: row (R)-2-Hydroxyglutarate; cosubstrate glutaconyl-CoA; apparent Km 1.5 mM; V relative 100


substrate_name: adipate

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Adipate; cosubstrate glutaconyl-CoA; column Apparent Km (mM) = 8; V relative = 60; normalized Km 8 mM

normalized_value_unit_evidence: Km 8 mM

raw_value_unit_evidence: row Adipate; cosubstrate glutaconyl-CoA; apparent Km 8 mM; V relative 60

row_label: Adipate

substrate: adipate


substrate_name: Acrylate

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Acrylate; cosubstrate acetyl-CoA; column Apparent Km (mM) = 10; V relative = 5; normalized Km 10 mM

normalized_value_unit_evidence: Km 10 mM

raw_value_unit_evidence: row Acrylate; cosubstrate acetyl-CoA; apparent Km 10 mM; V relative 5

row_label: Acrylate

substrate: Acrylate


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

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row 3-Hydroxyglutarate; cosubstrate glutaconyl-CoA; column Apparent Km (mM) = 13; V relative = 20; normalized Km 13 mM

normalized_value_unit_evidence: Km 13 mM

raw_value_unit_evidence: row 3-Hydroxyglutarate; cosubstrate glutaconyl-CoA; apparent Km 13 mM; V relative 20


substrate_name: propionate

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Propionate; cosubstrate glutaconyl-CoA; column Apparent Km (mM) = 16; V relative = 150; normalized Km 16 mM

normalized_value_unit_evidence: Km 16 mM

raw_value_unit_evidence: row Propionate; cosubstrate glutaconyl-CoA; apparent Km 16 mM; V relative 150

row_label: Propionate

substrate: propionate


substrate_name: acetate

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Acetate; cosubstrate glutaconyl-CoA; column Apparent Km (mM) = 26; V relative = 100; normalized Km 26 mM

normalized_value_unit_evidence: Km 26 mM

raw_value_unit_evidence: row Acetate; cosubstrate glutaconyl-CoA; apparent Km 26 mM; V relative 100

row_label: Acetate

substrate: acetate


substrate_name: isocrotonate

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Isocrotonate; cosubstrate acetyl-CoA; column Apparent Km (mM) = 100; V relative = 5; normalized Km 100 mM

normalized_value_unit_evidence: Km 100 mM

raw_value_unit_evidence: row Isocrotonate; cosubstrate acetyl-CoA; apparent Km 100 mM; V relative 5

row_label: Isocrotonate

substrate: isocrotonate


substrate_name: Butyrate

smiles: CCCC(=O)[O-]

column_label: Table 2. Substrate specificity of glutaconate CoA-transferase; row Butyrate; cosubstrate glutaconyl-CoA; column Apparent Km (mM) = 150; V relative = 70; normalized Km 150 mM

normalized_value_unit_evidence: Km 150 mM

raw_value_unit_evidence: row Butyrate; cosubstrate glutaconyl-CoA; apparent Km 150 mM; V relative 70

row_label: Butyrate

substrate: Butyrate


enzyme_display_name: gentisate 1,2-dioxygenase

organism: Aquipseudomonas alcaligenes

column_label: Table 2 WT GST-GDO row 4-Chlorogentisate prints Km=23.26 +/- 2.45 microM in the WTGST-GDO Km column.

raw_value_unit_evidence: Km raw_value=23.26 +/- 2.45 raw_unit=microM

row_label: WTGST-GDO; substrate 4-Chlorogentisate

table_label: PMC full-text HTML Table 2, specific activities and catalytic efficiencies of recombinant P25X GST-GDO and Y181F mutant

enzyme: gentisate 1,2-dioxygenase


assay_conditions_summary: pH 7.4; buffer 0.1 M KH2PO4

column_label: Table 2 WT GST-GDO row 3-Bromogentisate prints Km=45.91 +/- 3.05 microM in the WTGST-GDO Km column.

raw_value_unit_evidence: Km raw_value=45.91 +/- 3.05 raw_unit=microM

row_label: WTGST-GDO; substrate 3-Bromogentisate


sequence_variant_note: Mutation signature Y181F/H2P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme Y181F, in 0.1 M KH2PO4 buffer (pH 7.4) at 23°C


column_label: Table 2 WT GST-GDO row 3-Methylgentisate prints Km=62.34 +/- 3.23 microM in the WTGST-GDO Km column.

raw_value_unit_evidence: Km raw_value=62.34 +/- 3.23 raw_unit=microM

row_label: WTGST-GDO; substrate 3-Methylgentisate


column_label: Table 2 WT GST-GDO row 4-Methylgentisate prints Km=74.26 +/- 4.39 microM in the WTGST-GDO Km column.

raw_value_unit_evidence: Km raw_value=74.26 +/- 4.39 raw_unit=microM

row_label: WTGST-GDO; substrate 4-Methylgentisate


column_label: Table 2 WT GST-GDO row 3-Isopropylgentisate prints Km=79.37 +/- 1.5 microM in the WTGST-GDO Km column.

raw_value_unit_evidence: Km raw_value=79.37 +/- 1.5 raw_unit=microM


verification_status: corrected

column_label: Table 2 WT GST-GDO row Gentisate (2,5-dihydroxybenzoate synonym) prints Km=86.02 +/- 5.73 microM in the WTGST-GDO Km column; expected row reports 0.0862 mM.

raw_value_unit_evidence: Km raw_value=86.02 +/- 5.73 raw_unit=microM

row_label: WTGST-GDO; substrate Gentisate (2,5-dihydroxybenzoate synonym)

status: corrected


enzyme_display_name: diaminopimelate dehydrogenase

organism: Corynebacterium glutamicum

substrate_name: oxaloacetate

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

enzyme: diaminopimelate dehydrogenase

substrate: oxaloacetate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A69R to reconstruct the assayed variant sequence.

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

proof_lines: mutant A69R, pH not specified in the publication, temperature not specified in the publication


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


substrate_name: pyruvate

substrate: pyruvate


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


substrate_name: penicillin G

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

proof_lines: recombinant FF2 derived from gene shuffling

proof_lines: recombinant His-tagged enzyme, pH 7.5, 30°C

proof_lines: recombinant clone FF8 derived from gene shuffling

substrate: penicillin G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature G79E to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme G79E
pH 6.5, 30°C, recombinant mutant G79E


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature M188V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for PenN or PenG expansion; row M188V; PenG column kcat (s^-1); metric kcat; normalized value 0.0456 s^-1 | Table 1. Kinetic parameters for PenN or PenG expansion; row M188V; PenG column Km (mM); metric km; normalized value 0.76 mM | Table 1. Kinetic parameters for PenN or PenG expansion; row M188V; PenG column computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.06 s^-1*mM^-1; printed rounded column 60 M^-1*s^-1

normalized_value_unit_evidence: kcat normalized_value=0.0456 normalized_unit=s^-1; km normalized_value=0.76 normalized_unit=mM; kcat_over_km normalized_value=0.06 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: PenG kcat raw_value=0.0456 +/- 0.0016 raw_unit=s^-1; Km raw_value=0.76 +/- 0.170 raw_unit=mM; printed kcat/Km raw_value=60 raw_unit=M^-1*s^-1; quotient raw_value=0.0456/0.76 raw_unit=s^-1*mM^-1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature C155Y to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for PenN or PenG expansion; row C155Y; PenG column kcat (s^-1); metric kcat; normalized value 0.0476 s^-1 | Table 1. Kinetic parameters for PenN or PenG expansion; row C155Y; PenG column Km (mM); metric km; normalized value 1.76 mM | Table 1. Kinetic parameters for PenN or PenG expansion; row C155Y; PenG column computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.027045454545454546 s^-1*mM^-1; printed rounded column 27 M^-1*s^-1

normalized_value_unit_evidence: kcat normalized_value=0.0476 normalized_unit=s^-1; km normalized_value=1.76 normalized_unit=mM; kcat_over_km normalized_value=0.027045454545454546 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: PenG kcat raw_value=0.0476 +/- 0.0012 raw_unit=s^-1; Km raw_value=1.76 +/- 0.050 raw_unit=mM; printed kcat/Km raw_value=27 raw_unit=M^-1*s^-1; quotient raw_value=0.0476/1.76 raw_unit=s^-1*mM^-1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature T91A to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for PenN or PenG expansion; row T91A; PenG column kcat (s^-1); metric kcat; normalized value 0.0522 s^-1 | Table 1. Kinetic parameters for PenN or PenG expansion; row T91A; PenG column Km (mM); metric km; normalized value 1.36 mM | Table 1. Kinetic parameters for PenN or PenG expansion; row T91A; PenG column computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.03838235294117647 s^-1*mM^-1; printed rounded column 38 M^-1*s^-1

normalized_value_unit_evidence: kcat normalized_value=0.0522 normalized_unit=s^-1; km normalized_value=1.36 normalized_unit=mM; kcat_over_km normalized_value=0.03838235294117647 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: PenG kcat raw_value=0.0522 +/- 0.0004 raw_unit=s^-1; Km raw_value=1.36 +/- 0.090 raw_unit=mM; printed kcat/Km raw_value=38 raw_unit=M^-1*s^-1; quotient raw_value=0.0522/1.36 raw_unit=s^-1*mM^-1


substrate_name: acetyl-6-aminopenicillanic acid

substrate: acetyl-6-aminopenicillanic acid


sequence_variant_note: Mutation signature M737T references residue 737, which is outside the resolved sequence length.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature H244Q to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for PenN or PenG expansion; row H244Q; PenG column kcat (s^-1); metric kcat; normalized value 0.0698 s^-1 | Table 1. Kinetic parameters for PenN or PenG expansion; row H244Q; PenG column Km (mM); metric km; normalized value 1.39 mM | Table 1. Kinetic parameters for PenN or PenG expansion; row H244Q; PenG column computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.050215827338129494 s^-1*mM^-1; printed rounded column 50 M^-1*s^-1

normalized_value_unit_evidence: kcat normalized_value=0.0698 normalized_unit=s^-1; km normalized_value=1.39 normalized_unit=mM; kcat_over_km normalized_value=0.050215827338129494 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: PenG kcat raw_value=0.0698 +/- 0.0012 raw_unit=s^-1; Km raw_value=1.39 +/- 0.090 raw_unit=mM; printed kcat/Km raw_value=50 raw_unit=M^-1*s^-1; quotient raw_value=0.0698/1.39 raw_unit=s^-1*mM^-1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature I305L to reconstruct the assayed variant sequence.

proof_lines: mutant I305L, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature Y184H to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for PenN or PenG expansion; row Y184H; PenG column kcat (s^-1); metric kcat; normalized value 0.0798 s^-1 | Table 1. Kinetic parameters for PenN or PenG expansion; row Y184H; PenG column Km (mM); metric km; normalized value 0.95 mM | Table 1. Kinetic parameters for PenN or PenG expansion; row Y184H; PenG column computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.084 s^-1*mM^-1; printed rounded column 84 M^-1*s^-1

normalized_value_unit_evidence: kcat normalized_value=0.0798 normalized_unit=s^-1; km normalized_value=0.95 normalized_unit=mM; kcat_over_km normalized_value=0.084 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: PenG kcat raw_value=0.0798 +/- 0.0012 raw_unit=s^-1; Km raw_value=0.95 +/- 0.050 raw_unit=mM; printed kcat/Km raw_value=84 raw_unit=M^-1*s^-1; quotient raw_value=0.0798/0.95 raw_unit=s^-1*mM^-1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature L277Q to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for PenN or PenG expansion; row L277Q; PenG column kcat (s^-1); metric kcat; normalized value 0.1036 s^-1 | Table 1. Kinetic parameters for PenN or PenG expansion; row L277Q; PenG column Km (mM); metric km; normalized value 1.02 mM | Table 1. Kinetic parameters for PenN or PenG expansion; row L277Q; PenG column computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.10156862745098039 s^-1*mM^-1; printed rounded column 102 M^-1*s^-1

normalized_value_unit_evidence: kcat normalized_value=0.1036 normalized_unit=s^-1; km normalized_value=1.02 normalized_unit=mM; kcat_over_km normalized_value=0.10156862745098039 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: PenG kcat raw_value=0.1036 +/- 0.0012 raw_unit=s^-1; Km raw_value=1.02 +/- 0.020 raw_unit=mM; printed kcat/Km raw_value=102 raw_unit=M^-1*s^-1; quotient raw_value=0.1036/1.02 raw_unit=s^-1*mM^-1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature C155Y/Y184H/V275I/C281Y to reconstruct the assayed variant sequence.

proof_lines: mutant C155Y/Y184H/V275I/C281Y, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P18548 and applied mutation signature V275I/I305M to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for PenN or PenG expansion; row V275I/I305M; PenG column kcat (s^-1); metric kcat; normalized value 0.1458 s^-1 | Table 1. Kinetic parameters for PenN or PenG expansion; row V275I/I305M; PenG column Km (mM); metric km; normalized value 0.25 mM | Table 1. Kinetic parameters for PenN or PenG expansion; row V275I/I305M; PenG column computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.5832 s^-1*mM^-1; printed rounded column 583 M^-1*s^-1

normalized_value_unit_evidence: kcat normalized_value=0.1458 normalized_unit=s^-1; km normalized_value=0.25 normalized_unit=mM; kcat_over_km normalized_value=0.5832 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: PenG kcat raw_value=0.1458 +/- 0.0014 raw_unit=s^-1; Km raw_value=0.25 +/- 0.05 raw_unit=mM; printed kcat/Km raw_value=583 raw_unit=M^-1*s^-1; quotient raw_value=0.1458/0.25 raw_unit=s^-1*mM^-1


enzyme_display_name: mannokinase

organism: Escherichia coli

substrate_name: ATP

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

assay_conditions_summary: cofactor ATP

proof_lines:
reaction with D-mannose
ATP in form of MgATP2-

enzyme: mannokinase

substrate: ATP


substrate_name: D-fructose

column_label: Table II row Fructose; Km^a column raw cell 0.3 mM; normalized 0.3 mM.

raw_value_unit_evidence: Km raw_value=0.3 raw_unit=mM

row_label: Fructose

table_label: Table II. Substrate specificity of E. coli mannokinase

substrate: D-fructose


substrate_name: ITP

column_label: Table II row ITP; Km^a column raw cell 0.3 mM; normalized 0.3 mM.

row_label: ITP

substrate: ITP


substrate_name: GTP

column_label: Table II row GTP; Km^a column raw cell 0.5 mM; normalized 0.5 mM.

raw_value_unit_evidence: Km raw_value=0.5 raw_unit=mM

row_label: GTP

substrate: GTP


substrate_name: dATP

column_label: Table II row dATP; Km^a column raw cell 0.6 mM; normalized 0.6 mM.

raw_value_unit_evidence: Km raw_value=0.6 raw_unit=mM

row_label: dATP

substrate: dATP


substrate_name: UTP

column_label: Table II row UTP; Km^a column raw cell 2.0 mM; normalized 2.0 mM.

raw_value_unit_evidence: Km raw_value=2.0 raw_unit=mM

row_label: UTP

substrate: UTP


substrate_name: CTP

column_label: Table II row CTP; Km^a column raw cell 2.0 mM; normalized 2.0 mM.

row_label: CTP

substrate: CTP


substrate_name: D-glucose

column_label: Table II row Glucose; Km^a column raw cell 10.0 mM; normalized 10.0 mM.

raw_value_unit_evidence: Km raw_value=10.0 raw_unit=mM

row_label: Glucose

substrate: D-glucose


substrate_name: TTP

column_label: Table II row TTP; Km^a column raw cell 4.0 mM; normalized 4.0 mM.

raw_value_unit_evidence: Km raw_value=4.0 raw_unit=mM

row_label: TTP

substrate: TTP


substrate_name: D-glucosamine

column_label: Table II row Glucosamine; Km^a column raw cell 5.0 mM; normalized 5.0 mM.

raw_value_unit_evidence: Km raw_value=5.0 raw_unit=mM

row_label: Glucosamine

substrate: D-glucosamine


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

column_label: Table II row 2-deoxyglucose; Km^a column raw cell 10.0 mM; normalized 10.0 mM.


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: hydrogen dehydrogenase

organism: Cupriavidus necator

substrate_name: NADPH

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Table 4; NADPH-K3Fe(CN)6 row; Turnover no. (s^-1) / Hexamer column; raw value 2.

normalized_value_unit_evidence: 2 s^-1 = 2 s^-1 kcat-equivalent turnover number.

raw_value_unit_evidence: Table 4 reports NADPH-K3Fe(CN)6 hexamer Turnover no. = 2 s^-1.

row_label: NADPH-K3Fe(CN)6 activity assay; Turnover no. (s^-1) / Hexamer column

table_label: PMID 15838039, Table 4: Enzymatic activities of the purified tetrameric and hexameric SH

enzyme: hydrogen dehydrogenase

substrate: NADPH


substrate_name: ferrocyanide

proof_lines: pH 8.0, wild-type enzyme complex including HoxI, with NADPH

proof_lines: pH 8.0, wild-type enzyme complex including HoxI, with NADH

proof_lines: pH 8.0, wild-type enzyme complex including HoxI, with H2

substrate: ferrocyanide


mutation_signature: HoxI deletion mutant enzyme

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

smiles: [HH]

mutation_type: deletion

proof_lines: pH 8.0, HoxI deletion mutant enzyme, with oxidized benzyl viologen

proof_lines: pH 8.0, HoxI deletion mutant enzyme, with NAD+

proof_lines: pH 8.0, HoxI deletion mutant enzyme, with ferrocyanide


substrate_name: Oxidized benzyl viologen

proof_lines: pH 8.0, HoxI deletion mutant enzyme, with H2

substrate: Oxidized benzyl viologen


substrate_name: NAD+

substrate: NAD+


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

column_label: Table 4; H2-K3Fe(CN)6 row; Turnover no. (s^-1) / Hexamer column; raw value 372.

normalized_value_unit_evidence: 372 s^-1 = 372 s^-1 kcat-equivalent turnover number.

raw_value_unit_evidence: Table 4 reports H2-K3Fe(CN)6 hexamer Turnover no. = 372 s^-1.

row_label: H2-K3Fe(CN)6 activity assay; Turnover no. (s^-1) / Hexamer column


column_label: Table 4; H2-NAD+ row; Turnover no. (s^-1) / Hexamer column; raw value 143.

normalized_value_unit_evidence: 143 s^-1 = 143 s^-1 kcat-equivalent turnover number.

raw_value_unit_evidence: Table 4 reports H2-NAD+ hexamer Turnover no. = 143 s^-1.

row_label: H2-NAD+ activity assay; Turnover no. (s^-1) / Hexamer column


substrate_name: NADH

assay_conditions_summary: pH 8; cofactor NADH

substrate: NADH


proof_lines: pH 8.0, HoxI deletion mutant enzyme, with NADH


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22318 and applied mutation signature K3F with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NADH

proof_lines: reaction with K3Fe(CN)6, tetrameric enzyme form

proof_lines: reaction with K3Fe(CN)6, hexameric enzyme form


column_label: Table 4; NADH-K3Fe(CN)6 row; Turnover no. (s^-1) / Hexamer column; raw value 222.

normalized_value_unit_evidence: 222 s^-1 = 222 s^-1 kcat-equivalent turnover number.

raw_value_unit_evidence: Table 4 reports NADH-K3Fe(CN)6 hexamer Turnover no. = 222 s^-1.

row_label: NADH-K3Fe(CN)6 activity assay; Turnover no. (s^-1) / Hexamer column


enzyme_display_name: catechol 1,2-dioxygenase

organism: Pseudomonas reinekei

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

enzyme: catechol 1,2-dioxygenase


substrate_name: catechol

substrate: catechol


enzyme_display_name: salicylate 1-monooxygenase

enzyme: salicylate 1-monooxygenase


substrate_name: salicylate

substrate: salicylate


enzyme_display_name: D-amino-acid oxidase

organism: Rhodotorula toruloides

substrate_name: D-methionine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T60A/Q144R/K152E to reconstruct the assayed variant sequence.

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

column_label: Table 1. Substrate specificity of different RgDAAOs; row T60A/Q144R/K152E; substrate d-Met; column Km,app (mM); raw value 0.3 +/- 0.01 mM; normalized Km=0.3 mM.

normalized_value_unit_evidence: Km=0.3 mM

enzyme: D-amino-acid oxidase

substrate: D-methionine


substrate_name: D-alanine

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

column_label: Table 1. Substrate specificity of different RgDAAOs; row T60A/Q144R/K152E; substrate d-Ala; column Km,app (mM); raw value 0.6 +/- 0.06 mM; normalized Km=0.6 mM.

normalized_value_unit_evidence: Km=0.6 mM

substrate: D-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M213G to reconstruct the assayed variant sequence.

column_label: Table 1. Substrate specificity of different RgDAAOs; row M213G; substrate d-Met; column Km,app (mM); raw value 0.8 +/- 0.1 mM; normalized Km=0.8 mM.

normalized_value_unit_evidence: Km=0.8 mM

row_label: M213G / d-Met


substrate_name: D-valine

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

proof_lines:
immobilized wild type enzyme, at 25°C
pH 8.5, 25°C, wild-type enzyme
free wild type enzyme, at 25°C

substrate: D-valine


substrate_name: D-glutamine

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

column_label: Table 1. Substrate specificity of different RgDAAOs; row M213G; substrate d-Gln; column Km,app (mM); raw value 2.5 +/- 0.4 mM; normalized Km=2.5 mM.

normalized_value_unit_evidence: Km=2.5 mM

row_label: M213G / d-Gln

substrate: D-glutamine


column_label: Table 1. Substrate specificity of different RgDAAOs; row M213G; substrate d-Ala; column Km,app (mM); raw value 4.9 +/- 0.5 mM; normalized Km=4.9 mM.

normalized_value_unit_evidence: Km=4.9 mM

row_label: M213G / d-Ala


substrate_name: D-glutamate

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

column_label: Table 1. Substrate specificity of different RgDAAOs; row M213G; substrate d-Glu; column Km,app (mM); raw value 5.1 +/- 0.5 mM; normalized Km=5.1 mM.

normalized_value_unit_evidence: Km=5.1 mM

row_label: M213G / d-Glu

substrate: D-glutamate


column_label: Table 1. Substrate specificity of different RgDAAOs; row T60A/Q144R/K152E; substrate d-Gln; column Km,app (mM); raw value 6.0 +/- 0.4 mM; normalized Km=6.0 mM.

normalized_value_unit_evidence: Km=6.0 mM


substrate_name: D-Lysine

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

column_label: Table 1. Substrate specificity of different RgDAAOs; row M213G; substrate d-Lys; column Km,app (mM); raw value 8.0 +/- 1.0 mM; normalized Km=8.0 mM.

normalized_value_unit_evidence: Km=8.0 mM

row_label: M213G / d-Lys

substrate: D-Lysine


column_label: Table 1. Substrate specificity of different RgDAAOs; row Wild-type; substrate d-Lys; column Km,app (mM); raw value 14.6 +/- 1.4 mM; normalized Km=14.6 mM.

row_label: Wild-type / d-Lys


column_label: Table 1. Substrate specificity of different RgDAAOs; row T60A/Q144R/K152E; substrate d-Lys; column Km,app (mM); raw value 16.6 +/- 1.0 mM; normalized Km=16.6 mM.


column_label: Table 1. Substrate specificity of different RgDAAOs; row T60A/Q144R/K152E; substrate d-Glu; column Km,app (mM); raw value 101 +/- 14 mM; normalized Km=101.0 mM.


enzyme_display_name: valine dehydrogenase (NAD(+))

organism: Streptomyces virginiae

substrate_name: L-isoleucine

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

assay_conditions_summary: pH 10

enzyme: valine dehydrogenase (NAD(+))

substrate: L-isoleucine


substrate_name: L-leucine

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

substrate: L-leucine


substrate_name: L-norleucine

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

substrate: L-norleucine


substrate_name: L-norvaline

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

substrate: L-norvaline


substrate_name: L-valine

substrate: L-valine


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


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


substrate_name: pyruvate

substrate: pyruvate


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


enzyme_display_name: 2-enoate reductase

organism: Clostridium tyrobutyricum

substrate_name: 12-phenyldodec-2-enoic acid

enzyme: 2-enoate reductase

substrate: 12-phenyldodec-2-enoic acid


substrate_name: cinnamate

substrate: cinnamate


substrate_name: (2E)-2-methyl-3-phenylacrylic acid

substrate: (2E)-2-methyl-3-phenylacrylic acid


substrate_name: (2E)-2-methyl-3-phenylbut-2-enoic acid

substrate: (2E)-2-methyl-3-phenylbut-2-enoic acid


substrate_name: (2E)-3-phenylacrylic acid

substrate: (2E)-3-phenylacrylic acid


substrate_name: reduced methyl viologen

substrate: reduced methyl viologen


substrate_name: butenoate

smiles: CC=CC(=O)O

substrate: butenoate


substrate_name: 4-methoxy-2-methyl-4-oxobutanoic acid

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

substrate: 4-methoxy-2-methyl-4-oxobutanoic acid


substrate_name: (2E)-2-methylbut-2-enedioic acid

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

substrate: (2E)-2-methylbut-2-enedioic acid


substrate_name: 4-methoxy-3-methyl-4-oxobutanoic acid

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

substrate: 4-methoxy-3-methyl-4-oxobutanoic acid


substrate_name: pyridoxal 5'-phosphate

sequence_source: multiple

substrate: pyridoxal 5'-phosphate


substrate_name: pyridoxamine 5'-phosphate

substrate: pyridoxamine 5'-phosphate


smiles: CC(C(=O)CCCCCC(=O)[O-])N


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


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


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


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


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


smiles: N


enzyme_display_name: leucine dehydrogenase

organism: Geobacillus stearothermophilus

substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature K80A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.7; cofactor NADH

column_label: Table I; row Lys-80 -> Ala (K80A); column K_m, NADH; 0.022 +/- 0.003 mM.

normalized_value_unit_evidence: Paper K_m 0.022 mM = export K_m 0.022 mM; no unit conversion required.

table_label: Table I

enzyme: leucine dehydrogenase

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature K80Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 10.5; cofactor NAD+

column_label: Table I; row Lys-80 -> Gln (K80Q); column K_m, NAD+; 0.034 +/- 0.015 mM.

normalized_value_unit_evidence: Paper K_m 0.034 mM = export K_m 0.034 mM; no unit conversion required.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature K80R to reconstruct the assayed variant sequence.

column_label: Table I; row Lys-80 -> Arg (K80R); column K_m, NADH; 0.037 +/- 0.004 mM.

normalized_value_unit_evidence: Paper K_m 0.037 mM = export K_m 0.037 mM; no unit conversion required.


column_label: Table I; row Lys-80 -> Gln (K80Q); column K_m, NADH; 0.045 +/- 0.019 mM.

normalized_value_unit_evidence: Paper K_m 0.045 mM = export K_m 0.045 mM; no unit conversion required.


column_label: Table I; row Lys-80 -> Arg (K80R); column K_m, NAD+; 0.074 +/- 0.012 mM.

normalized_value_unit_evidence: Paper K_m 0.074 mM = export K_m 0.074 mM; no unit conversion required.


column_label: Table I; row Lys-80 -> Ala (K80A); column K_m, NAD+; 0.14 +/- 0.01 mM.

normalized_value_unit_evidence: Paper K_m 0.14 mM = export K_m 0.14 mM; no unit conversion required.


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

column_label: Table I; row Lys-80 -> Arg (K80R); column K_m, alpha-keto-iso-caproate; 0.99 +/- 0.15 mM.

normalized_value_unit_evidence: Paper K_m 0.99 mM = export K_m 0.99 mM; no unit conversion required.


substrate_name: L-Leu

column_label: Table I; row Lys-80 -> Ala (K80A); column K_m, L-leucine; 3.7 +/- 0.5 mM.

normalized_value_unit_evidence: Paper K_m 3.7 mM = export K_m 3.7 mM; no unit conversion required.

raw_value_unit_evidence: Table I cell: K_m = 3.7 +/- 0.5 mM.

substrate: L-Leu


column_label: Table I; row Lys-80 -> Ala (K80A); column K_m, alpha-keto-iso-caproate; 9.8 +/- 1.2 mM.

normalized_value_unit_evidence: Paper K_m 9.8 mM = export K_m 9.8 mM; no unit conversion required.

raw_value_unit_evidence: Table I cell: K_m = 9.8 +/- 1.2 mM.


column_label: Table I; row Lys-80 -> Gln (K80Q); column K_m, alpha-keto-iso-caproate; 25 +/- 8 mM.

normalized_value_unit_evidence: Paper K_m 25 mM = export K_m 25 mM; no unit conversion required.

raw_value_unit_evidence: Table I cell: K_m = 25 +/- 8 mM.


substrate_name: Unknown

assay_conditions_summary: buffer the paper-described 1 M ammonium

column_label: Table II; row Lys-80 -> Ala (K80A), iso-caproate; column K_i, iso-caproate; 33 +/- 3 mM.

normalized_value_unit_evidence: Paper K_i 33 mM = export K_i 33 mM; no unit conversion required.

raw_value_unit_evidence: Table II cell: K_i = 33 +/- 3 mM.

row_label: Lys-80 -> Ala (K80A), iso-caproate

table_label: Table II

substrate: Unknown


assay_conditions_summary: pH 7.3; cofactor NAD+


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature R198S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; cofactor NADP+

substrate: NADP+


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +10, so it is treated as a source-provided variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature D190N with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature R198K with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


organism: Neomoorella thermoacetica


substrate_name: L-norleucine

substrate: L-norleucine


substrate_name: L-Ile

substrate: L-Ile


substrate_name: L-norvaline

substrate: L-norvaline


substrate_name: L-Val

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

substrate: L-Val


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

organism: Rattus norvegicus

assay_conditions_summary: pH 7

enzyme: NAD(P)H dehydrogenase (quinone)


organism: Pseudomonas sp.

substrate_name: Fusidic acid

sequence: QVIAITGSASGIGAA

wild_type_sequence: QVIAITGSASGIGAA

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

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines:
pH 8.5, 37°C, with cofactor NAD+
pH 8.5, 37°C, with cofactor thio-NAD+

substrate: Fusidic acid


substrate_name: cholic acid

proof_lines:
pH 8.5, 37°C, with cofactor thio-NAD+
pH 8.5, 37°C, with cofactor NAD+

substrate: cholic acid


substrate_name: lithocholic acid

substrate: lithocholic acid


substrate_name: taurocholic acid

substrate: taurocholic acid


substrate_name: chenodeoxycholic acid

substrate: chenodeoxycholic acid


substrate_name: glycocholic acid

substrate: glycocholic acid


substrate_name: androsterone

substrate: androsterone


enzyme_display_name: isoeugenol monooxygenase

substrate_name: isoeugenol

proof_lines: wild-type, 30°C, pH not specified in the publication

enzyme: isoeugenol monooxygenase

substrate: isoeugenol


sequence_variant_note: Resolved canonical sequence from candidate_uniprot:C3VA26 and applied mutation signature F281Q to reconstruct the assayed variant sequence.

proof_lines: mutant F281Q, 30°C, pH not specified in the publication


enzyme_display_name: oxalate oxidase

substrate_name: oxalic acid

enzyme: oxalate oxidase

substrate: oxalic acid


enzyme_display_name: D-xylose 1-dehydrogenase

substrate_name: D-galactose

enzyme: D-xylose 1-dehydrogenase

substrate: D-galactose


enzyme_display_name: alanine dehydrogenase

organism: Shewanella sp.

assay_conditions_summary: cofactor NADP+

enzyme: alanine dehydrogenase


substrate_name: NAD+

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

substrate: NAD+


enzyme_display_name: haloalkane dehalogenase

organism: Sphingomonas paucimobilis

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

smiles: CCCCCCCl

enzyme: haloalkane dehalogenase


smiles: CCCCCCBr


substrate_name: bromocyclohexane

substrate: bromocyclohexane


smiles: CC(C)CBr


smiles: CCCCCCI


smiles: C(CCCl)CCCl


smiles: CCCCCCCCCl


smiles: CCCCCCCCl


smiles: CCCCBr


smiles: C(CBr)CBr


smiles: C=C(CCl)CCl


organism: Symbiobacterium thermophilum

substrate_name: NADPH

sequence_source: UniProtKB Q67PI3 (reconstructed mutant R35S)

assay_conditions_summary: pH 9.6; cofactor NADPH

substrate: NADPH


substrate_name: pyruvate

substrate: pyruvate


sequence_source: UniProtKB Q67PI3 (reconstructed mutant R71A)


sequence_source: UniProtKB Q67PI3


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

proof_lines: pH 8.5, 30°C, recombinant wild-type enzyme


substrate_name: NADP+

assay_conditions_summary: pH 9.6; cofactor NADP+

substrate: NADP+


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


enzyme_display_name: nitric-oxide reductase (cytochrome c)

organism: Paracoccus denitrificans

substrate_name: pseudoazurin

proof_lines:
apparent KM of native enzyme
apparent KM of recombinant enzyme

enzyme: nitric-oxide reductase (cytochrome c)

substrate: pseudoazurin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E122Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E198A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E125D 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:
recombinant wild type enzyme
native wild type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E267A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E125A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E122D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E125Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E122A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E202A to reconstruct the assayed variant sequence.


enzyme_display_name: alpha,alpha-phosphotrehalase

organism: Bacillus licheniformis

substrate_name: 4-nitrophenyl alpha-D-glucopyranoside

sequence_variant_note: Resolved canonical sequence from unresolved_ec_organism and applied mutation signature K292A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

enzyme: alpha,alpha-phosphotrehalase

substrate: 4-nitrophenyl alpha-D-glucopyranoside


substrate_name: alpha,alpha-trehalose 6-phosphate

substrate: alpha,alpha-trehalose 6-phosphate


sequence_variant_note: Resolved canonical sequence from unresolved_ec_organism and applied mutation signature H281A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from unresolved_ec_organism and applied mutation signature H282A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from unresolved_ec_organism and applied mutation signature K284A to reconstruct the assayed variant sequence.


enzyme_display_name: pyruvate decarboxylase

organism: Klebsiella pneumoniae

sequence_variant_note: Mutation signature A387L references residue 387, which is outside the resolved sequence length.

proof_lines: recombinant mutant A387L, pH and temperature not specified in the publication

enzyme: pyruvate decarboxylase


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


sequence_variant_note: Mutation signature A387I/F388W references residue 387, which is outside the resolved sequence length.

proof_lines: recombinant mutant A387I/F388W, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature A387I references residue 387, which is outside the resolved sequence length.

proof_lines: recombinant mutant A387I, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature L546W references residue 546, which is outside the resolved sequence length.

proof_lines: recombinant mutant L546W, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature V542I references residue 542, which is outside the resolved sequence length.

proof_lines: recombinant mutant V542I, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature F388W references residue 388, which is outside the resolved sequence length.

proof_lines: recombinant mutant F388W, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature T290L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: recombinant mutant T290L, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature Q383M references residue 383, which is outside the resolved sequence length.

proof_lines: recombinant mutant Q383M, pH and temperature not specified in the publication


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


enzyme_display_name: alanopine dehydrogenase

organism: Magallana gigas

substrate_name: NADH

sequence_source: UniProt I7HP94

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

assay_conditions_summary: pH 7; cofactor NADH

column_label: Abstract/kinetic-properties text: apparent Km values are 0.01 mM for NADH at pH 7.0; normalized 0.01 mM.

raw_value_unit_evidence: Km raw_value=0.01 raw_unit=mM; paper abstract/text reports apparent Km 0.01 mM for NADH at pH 7.0

row_label: NADH

table_label: Table 2. Apparent V and Km values for alanopine dehydrogenase obtained with different amino and keto acids

enzyme: alanopine dehydrogenase

substrate: NADH


column_label: Table 2 row Pyruvate; Apparent Km column raw cell 0.45 mM; normalized 0.45 mM.

raw_value_unit_evidence: Km raw_value=0.45 raw_unit=mM; reported with S.E. 0.03 mM

row_label: Pyruvate


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

column_label: Table 2 row 2-Oxobutyrate; Apparent Km column raw cell 3.45 mM; normalized 3.45 mM.

raw_value_unit_evidence: Km raw_value=3.45 raw_unit=mM; reported with S.E. 0.02 mM


substrate_name: glyoxylate

column_label: Table 2 row Glyoxylate; Apparent Km column raw cell 3.49 mM; normalized 3.49 mM.

raw_value_unit_evidence: Km raw_value=3.49 raw_unit=mM; reported with S.E. 0.66 mM

row_label: Glyoxylate

substrate: glyoxylate


substrate_name: Hydroxypyruvate

column_label: Table 2 row Hydroxypyruvate; Apparent Km column raw cell 6.48 mM; normalized 6.48 mM.

raw_value_unit_evidence: Km raw_value=6.48 raw_unit=mM; reported with S.E. 0.71 mM

row_label: Hydroxypyruvate

substrate: Hydroxypyruvate


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

column_label: Table 2 row 2-Oxovalerate; Apparent Km column raw cell 16 mM; normalized 16 mM.

raw_value_unit_evidence: Km raw_value=16 raw_unit=mM; reported with S.E. 3.7 mM


substrate_name: Gly

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

column_label: Table 2 row Glycine; Apparent Km column raw cell 96 mM; normalized 96 mM.

raw_value_unit_evidence: Km raw_value=96 raw_unit=mM; reported with S.E. 1.5 mM

row_label: Glycine

substrate: Gly


substrate_name: L-Ala

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

column_label: Table 2 row Alanine; Apparent Km column raw cell 98 mM; normalized 98 mM.

raw_value_unit_evidence: Km raw_value=98 raw_unit=mM; reported with S.E. 7.9 mM

row_label: Alanine

substrate: L-Ala


column_label: Table 2 row 2-Aminobutyrate; Apparent Km column raw cell 150 mM; normalized 150 mM.

raw_value_unit_evidence: Km raw_value=150 raw_unit=mM; reported with S.E. 12 mM


substrate_name: Ser

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

column_label: Table 2 row Serine; Apparent Km column raw cell 680 mM; normalized 680 mM.

raw_value_unit_evidence: Km raw_value=680 raw_unit=mM; reported with S.E. 55 mM

row_label: Serine

substrate: Ser


enzyme_display_name: azobenzene reductase

organism: Enterococcus faecalis

substrate_name: Methyl red

proof_lines:
wild-type, pH 7.0, 22°C
wild-type enzyme

enzyme: azobenzene reductase

substrate: Methyl red


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R18G with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R21G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R21G with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R18G to reconstruct the assayed variant sequence.


enzyme_display_name: 2,4-diacetylphloroglucinol hydrolase

organism: Pseudomonas fluorescens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E274A to reconstruct the assayed variant sequence.

enzyme: 2,4-diacetylphloroglucinol hydrolase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E160A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y121A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y229A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H214Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y229F/H214A to reconstruct the assayed variant sequence.

proof_lines: recombinant mutants Y229F and H214A, pH 7.1, 25°C


column_label: Table 2 'Table 2: Kinetic parameters of PhlG wild type and active-site mutants'; row Wild type; Km, kcat, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Wild type, normalized where unambiguous: kcat 4.7 s^-1; Km 0.272 mM; kcat/Km 17 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Wild type: Km 272 ± 42 uM; kcat 4.7 ± 0.1 s^-1; kcat/Km 17000.

row_label: Wild type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y229F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H214A to reconstruct the assayed variant sequence.


organism: Spinacia oleracea

substrate_name: acetoacetyl-CoA

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

assay_conditions_summary: cofactor CoA

substrate: acetoacetyl-CoA


enzyme_display_name: toluene 4-monooxygenase

organism: Ectopseudomonas mendocina

substrate_name: nitrobenzene

enzyme: toluene 4-monooxygenase

substrate: nitrobenzene


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


substrate_name: chlorobenzene

substrate: chlorobenzene


substrate_name: Benzene

substrate: Benzene


substrate_name: anisole

substrate: anisole


substrate_name: Toluene

proof_lines:
wild-type, pH 7.5, 4°C
wild-type, pH 7.5, 25°C

substrate: Toluene


proof_lines:
mutant T201A, pH 7.5, 4°C
mutant T201A, pH 7.5, 25°C


enzyme_display_name: glycine N-methyltransferase

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

column_label: Table 2 WT row, kcat and Gly Km columns and their same-row quotient.

raw_value_unit_evidence: Table 2 WT row: kcat 27(1) min^-1; Gly Km 0.43(4) mM.

row_label: WT / Gly

table_label: Table 2. Apparent Kinetic Parameters of WT and Mutated Enzymes

enzyme: glycine N-methyltransferase


substrate_name: S-adenosyl-L-methionine

proof_lines:
pH 7.2, mutant enzyme Y21F
mutant Y21F, pH 7.4, 37°C

substrate: S-adenosyl-L-methionine


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature Y194F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature Y220F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature Y33F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines:
pH 7.2, wild-type enzyme
wild-type, pH 7.4, 37°C


enzyme_display_name: galactokinase

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

enzyme: galactokinase


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


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: 3-dehydrosphinganine reductase

organism: Homo sapiens

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

enzyme: 3-dehydrosphinganine reductase


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH


enzyme_display_name: L-threonine 3-dehydrogenase

organism: Acetoanaerobium sticklandii

substrate_name: NAD+

assay_conditions_summary: pH 9; 310.15 K; cofactor NAD+

enzyme: L-threonine 3-dehydrogenase

substrate: NAD+


substrate_name: L-threonine

substrate: L-threonine


organism: Gallus gallus


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


enzyme_display_name: aromatic 2-oxoacid reductase

organism: Clostridium sporogenes

substrate_name: NADH

assay_conditions_summary: cofactor NADH

enzyme: aromatic 2-oxoacid reductase

substrate: NADH


substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


assay_conditions_summary: cofactor NAD+


substrate_name: indoleglycolate

substrate: indoleglycolate


substrate_name: indolelactate

substrate: indolelactate


substrate_name: p-hydroxyphenyllactate

substrate: p-hydroxyphenyllactate


enzyme_display_name: D-threo-aldose 1-dehydrogenase

organism: Sus scrofa

enzyme: D-threo-aldose 1-dehydrogenase


substrate_name: D-arabinose

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

substrate: D-arabinose


substrate_name: L-galactose

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

substrate: L-galactose


substrate_name: D-Lyxose

substrate: D-Lyxose


enzyme_display_name: 2-deoxy-D-gluconate 3-dehydrogenase

organism: Pseudomonas sp.

enzyme: 2-deoxy-D-gluconate 3-dehydrogenase


organism: Pectobacterium carotovorum subsp. carotovorum

assay_conditions_summary: pH 7.2; 318.15 K; cofactor NADPH


assay_conditions_summary: pH 7.2; 318.15 K; cofactor NADH


enzyme_display_name: GDP-mannose 6-dehydrogenase

organism: Ectocarpus siliculosus

proof_lines: pH and temperature not specified in the publication

enzyme: GDP-mannose 6-dehydrogenase


substrate_name: GDP-D-mannose

substrate: GDP-D-mannose


enzyme_display_name: sorbitol-6-phosphate 2-dehydrogenase

organism: Clostridium pasteurianum

assay_conditions_summary: buffer km_value=0.02 mM in phosphate; cofactor NADH

enzyme: sorbitol-6-phosphate 2-dehydrogenase


substrate_name: sorbitol 6-phosphate

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

assay_conditions_summary: buffer Tris-HCl

proof_lines:
Tris-HCl buffer
glycine-NaOH buffer

substrate: sorbitol 6-phosphate


assay_conditions_summary: buffer 0; cofactor NAD+

proof_lines:
0.11-0.45 mM NAD+, Tris-HCl buffer
0.11-0.45 mM NAD+, glycine-NaOH buffer
0.45-4.5 mM NAD+, Tris-HCl buffer


substrate_name: fructose 6-phosphate

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

assay_conditions_summary: buffer NADH-coupled notes in phosphate; cofactor NADH

proof_lines:
+ 0.43 mM NADH, phosphate buffer
+ 1.08 mM NADH, phosphate buffer

substrate: fructose 6-phosphate


organism: Cavia porcellus


proof_lines:
pH 7.4, 25°C
placental microsomes
Sf9 cell homogenate


substrate_name: Dehydrolithocholic acid

substrate: Dehydrolithocholic acid


substrate_name: all-trans-retinal

substrate: all-trans-retinal


assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.02 M potassium phosphate

proof_lines:
pH 7.4, 25°C
37°C, pH 7.4
recombinant enzyme


substrate_name: menadione

substrate: menadione


substrate_name: n-butyrophenone

substrate: n-butyrophenone


substrate_name: valerophenone

substrate: valerophenone


substrate_name: hexanophenone

substrate: hexanophenone


substrate_name: dehydroepiandrosterone

proof_lines: mutant C111S, presence of 2-mercatoethanol pH 7.4

substrate: dehydroepiandrosterone


substrate_name: NAD+

assay_conditions_summary: pH 7.4; cofactor NAD+

substrate: NAD+


proof_lines: mutant C111A, presence of 2-mercatoethanol pH 7.4


assay_conditions_summary: pH 7.4; 300.15 K; cofactor NAD+

proof_lines: pH 7.4, 27°C, chimeric S194G-1 mutant of the enzyme (3beta-HSD1)


substrate_name: Unknown

substrate: Unknown


assay_conditions_summary: pH 7.4; 300.15 K; buffer 0.02 M potassium phosphate

proof_lines: in 0.02 M potassium phosphate buffer, pH 7.4


substrate_name: pregnenolone

substrate: pregnenolone


proof_lines:
placental microsomes
Sf9 cell homogenate


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


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


substrate_name: diacetyl

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

substrate: diacetyl


substrate_name: benzil

substrate: benzil


substrate_name: isatin

substrate: isatin


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


substrate_name: NADP+

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: NADH

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NADH

proof_lines:
wild-type 3beta-HSD1, pH 7.4, 27°C
wild-type 3beta-HSD2, pH 7.4, 27°C

substrate: NADH


assay_conditions_summary: pH 7.4; 300.15 K; buffer 0.02 M potassium phosphate; cofactor NAD+


proof_lines: mutant enzyme S124T, in 0.02 M potassium phosphate, pH 7.4, at 27°C


enzyme_display_name: 11beta-hydroxysteroid dehydrogenase

organism: Felis catus

substrate_name: cortisone

proof_lines:
kidney enzyme, pH 7.4, 37°C
liver enzyme, pH 7.4, 37°C

enzyme: 11beta-hydroxysteroid dehydrogenase

substrate: cortisone


substrate_name: cortisol

substrate: cortisol


enzyme_display_name: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

organism: Equus caballus

assay_conditions_summary: pH 10.4; 298.15 K; cofactor NADPH


substrate_name: sepiapterin

enzyme: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

substrate: sepiapterin


assay_conditions_summary: pH 10.4; 298.15 K; cofactor NADP+


substrate_name: menadione

substrate: menadione


assay_conditions_summary: cofactor NADPH


enzyme_display_name: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming)

organism: Macaca fascicularis

substrate_name: D-xylose

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: oxidation reaction of mutant R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose

proof_lines: oxidation reaction of mutant R37D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose

substrate: D-xylose


proof_lines: oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose

proof_lines: oxidation reaction of mutant A36D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose

enzyme: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming)


proof_lines: oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose

proof_lines: oxidation reaction of mutant H76Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose

proof_lines: oxidation reaction of mutant H79Q, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose

proof_lines: oxidation reaction of mutant R41D, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose

proof_lines: oxidation reaction of mutant R37A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose

proof_lines: oxidation reaction of mutant R41A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM D-xylose

proof_lines: oxidation reaction of wild type enzyme, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant F279A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant W254Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant F154A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant W125Y, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


proof_lines: oxidation reaction of mutant W254A, 25 mM Tris-HCl pH 7.5, 0.25 mM NADP+, 50 mM d-xylose


enzyme_display_name: cinnamyl-alcohol dehydrogenase

organism: Eucalyptus gunnii

assay_conditions_summary: cofactor NAD+

enzyme: cinnamyl-alcohol dehydrogenase


assay_conditions_summary: cofactor NADP+


substrate_name: coniferyl alcohol

proof_lines:
with NADP+
with NAD+

substrate: coniferyl alcohol


proof_lines:
with NAD+
with NADP+
with NADH


organism: Hibiscus cannabinus

substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


substrate_name: sinapyl aldehyde

substrate: sinapyl aldehyde


organism: Nicotiana tabacum

proof_lines:
pH 10.5, 30°C, recombinant CAD1-1
pH 8.8, 30°C, recombinant CAD1-7


proof_lines:
pH 6.25, 30°C, recombinant CAD1-1
pH 6.25, 30°C, recombinant CAD1-7


organism: Plagiochasma appendiculatum

proof_lines:
isoform CAD1, at pH 6.0 and 25°C
isoform CAD2, at pH 6.0 and 25°C


substrate_name: sinapaldehyde

proof_lines:
isoform CAD2, at pH 6.0 and 25°C
isoform CAD1, at pH 6.0 and 25°C

substrate: sinapaldehyde


substrate_name: coniferaldehyde

substrate: coniferaldehyde


enzyme_display_name: (+)-borneol dehydrogenase

organism: Salvia officinalis

substrate_name: (+)-borneol

enzyme: (+)-borneol dehydrogenase

substrate: (+)-borneol


substrate_name: (-)-Thujol

substrate: (-)-Thujol


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: 1,3-propanediol dehydrogenase

organism: Limosilactobacillus reuteri

enzyme: 1,3-propanediol dehydrogenase


enzyme_display_name: uronate dehydrogenase

organism: Pseudomonas syringae pv. tomato

substrate_name: beta-D-galacturonate

assay_conditions_summary: pH 8; 298.15 K; buffer recombinant His-tagged enzyme

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer

enzyme: uronate dehydrogenase

substrate: beta-D-galacturonate


assay_conditions_summary: pH 8; 298.15 K; buffer pH 8; cofactor NAD+


substrate_name: D-galacturonate

assay_conditions_summary: buffer recombinant His-tagged enzyme

substrate: D-galacturonate


enzyme_display_name: IMP dehydrogenase

organism: Burkholderia thailandensis

substrate_name: IMP

proof_lines: pH 8.0, 30°C, recombinant enzyme, with MgATP

proof_lines: pH 8.0, 30°C, recombinant enzyme, without MgATP

enzyme: IMP dehydrogenase

substrate: IMP


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


organism: Eimeria tenella


substrate_name: Unknown

proof_lines: at a fixed concentration of 0.5 mM NAD+ and 0.03 mM IMP

substrate: Unknown


organism: Vigna unguiculata

substrate_name: inosine 5'-phosphate

substrate: inosine 5'-phosphate


assay_conditions_summary: pH 8.8; 303.15 K; cofactor NAD+


enzyme_display_name: tropinone reductase I

organism: Brugmansia arborea

proof_lines: pH 9.6, 22°C, recombinant His-tagged enzyme

enzyme: tropinone reductase I


substrate_name: tropinone

proof_lines: pH 6.4, 22°C, recombinant His-tagged enzyme

proof_lines: pH 6.4, temperature not specified in the publication

substrate: tropinone


substrate_name: Tropine

proof_lines: pH 9.6, temperature not specified in the publication

substrate: Tropine


substrate_name: testosterone

proof_lines:
membrane bound
solubilized with Triton X-100

substrate: testosterone


proof_lines:
solubilized with Triton X-100
membrane bound


organism: Mesocricetus auratus

substrate_name: farnesol

smiles: CC(=CCCC(=CCCC(=CCO)C)C)C

substrate: farnesol


substrate_name: geraniol

smiles: CC(=CCCC(=CCO)C)C

substrate: geraniol


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+


substrate_name: cis-benzene dihydrodiol

substrate: cis-benzene dihydrodiol


substrate_name: geranylgeraniol

smiles: CC(=CCCC(=CCCC(=CCCC(=CCO)C)C)C)C

substrate: geranylgeraniol


substrate_name: beta-ionol

substrate: beta-ionol


substrate_name: NADP+

proof_lines: pH 7.4, 25°C, with substrate S-camphorquinone

substrate: NADP+


substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: glycochenodeoxycholic acid

substrate: glycochenodeoxycholic acid


substrate_name: lithocholic acid

substrate: lithocholic acid


substrate_name: glycolithocholic acid

substrate: glycolithocholic acid


organism: Oryctolagus cuniculus


proof_lines:
pH 7.4, 25°C
pH 7.4, 25°C, recombinant enzyme


substrate_name: NAD+

substrate: NAD+


substrate_name: alpha-tetralone

substrate: alpha-tetralone


substrate_name: Naphthalene dihydrodiol

substrate: Naphthalene dihydrodiol


substrate_name: benzene dihydrodiol

substrate: benzene dihydrodiol


assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA


substrate_name: (S)-camphorquinone

substrate: (S)-camphorquinone


substrate_name: isatin

substrate: isatin


substrate_name: morphine

substrate: morphine


enzyme_display_name: methanol dehydrogenase

organism: Cupriavidus necator

substrate_name: methanol

smiles: CO

proof_lines: pH 9.5, 30°C, recombinant wild-type enzyme

enzyme: methanol dehydrogenase

substrate: methanol


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


enzyme_display_name: mannitol dehydrogenase

organism: Apium graveolens

assay_conditions_summary: pH 9.5; cofactor NAD+

proof_lines:
at pH 9.5
at pH 7.0

enzyme: mannitol dehydrogenase


substrate_name: D-mannitol

smiles: C(C(C(C(C(CO)O)O)O)O)O

substrate: D-mannitol


enzyme_display_name: sn-glycerol-1-phosphate dehydrogenase

organism: Aeropyrum pernix

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

enzyme: sn-glycerol-1-phosphate dehydrogenase


substrate_name: NADPH

substrate: NADPH


substrate_name: dihydroxyacetone phosphate

assay_conditions_summary: cofactor NADH

proof_lines: mutant enzyme H271A, with NADH as coenzyme

substrate: dihydroxyacetone phosphate


proof_lines: mutant enzyme D144A, with NADPH as coenzyme

proof_lines: mutant enzyme D144A, with NADH as coenzyme


proof_lines: mutant enzyme H287A, with NADH as coenzyme


proof_lines: mutant enzyme D191N, with NADH as coenzyme


proof_lines: wild type enzyme, with NADPH as coenzyme


proof_lines: mutant enzyme D144N, with NADPH as coenzyme

proof_lines: mutant enzyme D144N, with NADH as coenzyme


assay_conditions_summary: pH 7; 338.15 K; cofactor NADPH


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


assay_conditions_summary: pH 7; 338.15 K; cofactor NAD+


proof_lines: in the presence of 0.32 mM NADPH, pH 7.0, 65°C

proof_lines: in the presence of 0.32 mM NADH, pH 7.0, 65°C


assay_conditions_summary: pH 7; 338.15 K; cofactor NADH


enzyme_display_name: 2-(S)-hydroxypropyl-CoM dehydrogenase

organism: Xanthobacter autotrophicus

smiles: CC(CSCCS(=O)(=O)O)O

enzyme: 2-(S)-hydroxypropyl-CoM dehydrogenase


smiles: CCC(=O)C


smiles: CCC(C)O


smiles: CC(C)O


smiles: CC(=O)CSCCS(=O)(=O)O


substrate_name: Unknown

substrate: Unknown


organism: Ensifer adhaerens

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: pH 7.5, mutant enzyme D176A, cofactor: NADPH


assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: pH 8.0, mutant enzyme H180A, cofactor: NADPH


assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines: pH 6.5, mutant enzyme K94G, cofactor: NADPH


proof_lines: pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH

proof_lines: pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH


proof_lines: pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH

proof_lines: pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH


proof_lines: pH 6.5, mutant enzyme A13G, cofactor: NADH

proof_lines: pH 6.5, mutant enzyme A13G, cofactor: NADPH


proof_lines: pH 6.5, mutant enzyme S10G, cofactor: NADPH


proof_lines: pH 6.5 recombinant wild-type enzyme, cofactor: NADPH

proof_lines: pH 6.5, native wild-type enzyme, cofactor: NADPH


proof_lines: pH 6.5, mutant enzyme G206I, cofactor: NADPH


proof_lines:
pH 6.5 recombinant wild-type enzyme
pH 6.5, native wild-type enzyme


substrate_name: NADH

assay_conditions_summary: pH 6.5; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

proof_lines: mutant enzyme A13G/S33D, at pH 6.5 and 30°C


substrate_name: D-glucosone

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

substrate: D-glucosone


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH


proof_lines: mutant enzyme A13G/S10G, at pH 6.5 and 30°C


enzyme_display_name: sulfopropanediol 3-dehydrogenase

organism: Cupriavidus pinatubonensis

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

enzyme: sulfopropanediol 3-dehydrogenase


enzyme_display_name: sulfoacetaldehyde reductase (NADPH)

organism: Chromohalobacter israelensis

assay_conditions_summary: pH 9; 296.15 K; buffer 0.02 mMTris/H2SO4; cofactor NADPH

proof_lines: in 0.02 mMTris/H2SO4 buffer, pH 9.0, at 23°C

enzyme: sulfoacetaldehyde reductase (NADPH)


assay_conditions_summary: pH 9; 296.15 K; buffer 0.02 mMTris/H2SO4


organism: Klebsiella oxytoca

substrate_name: isethionate

substrate: isethionate


substrate_name: NADP+

assay_conditions_summary: pH 10; 295.15 K; cofactor NADP+

substrate: NADP+


enzyme_display_name: 11-cis-retinol dehydrogenase

organism: Homo sapiens

substrate_name: all-trans retinol

enzyme: 11-cis-retinol dehydrogenase

substrate: all-trans retinol


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+


substrate_name: NAD+

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH


substrate_name: all-trans retinal

substrate: all-trans retinal


proof_lines:
pH 7.4, 37°C
microsomal preparations of RDH10


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: microsomal preparations of RDH10, cofactor: NAD+


substrate_name: 11-cis-retinol-[cellular retinaldehyde binding protein]


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

substrate: 11-cis-retinol-[cellular retinaldehyde binding protein]


substrate_name: all-trans-retinal

substrate: all-trans-retinal


enzyme_display_name: eugenol synthase

organism: Clarkia breweri

substrate_name: coniferyl acetate

proof_lines:
CbEGS2, pH 6.5, 28°C
CbEGS1, pH 6.5, 28°C

enzyme: eugenol synthase

substrate: coniferyl acetate


enzyme_display_name: secoisolariciresinol dehydrogenase

organism: Dysosma pleiantha

substrate_name: (-)-secoisolariciresinol

proof_lines: pH 8.8, 20°C, recombinant His-tagged enzyme

enzyme: secoisolariciresinol dehydrogenase

substrate: (-)-secoisolariciresinol


enzyme_display_name: phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating)

organism: Neomoorella thermoacetica

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NAD+

proof_lines: mutant enzyme A30D/R31I/T32I, in 100 mM HEPES (pH 7.5), at 50°C


proof_lines: mutant enzyme A30C/R31I/T32K, in 100 mM HEPES (pH 7.5), at 50°C

enzyme: phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating)


proof_lines: mutant enzyme R31T, in 100 mM HEPES (pH 7.5), at 50°C


proof_lines: mutant enzyme A30E/R31I/T32D, in 100 mM HEPES (pH 7.5), at 50°C


proof_lines: wild type enzyme, in 100 mM HEPES (pH 7.5), at 50°C


proof_lines: mutant enzyme R31I/T32K, in 100 mM HEPES (pH 7.5), at 50°C


proof_lines: mutant enzyme R31I, in 100 mM HEPES (pH 7.5), at 50°C


enzyme_display_name: acetoacetyl-CoA reductase

organism: Candidatus Accumulibacter phosphatis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

enzyme: acetoacetyl-CoA reductase


substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: recombinant enzyme, with NADPH as cosubstrate, at pH 7.5 and 25°C

proof_lines: recombinant enzyme, with NADH as cosubstrate, at pH 7.5 and 25°C

substrate: acetoacetyl-CoA


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


enzyme_display_name: (S)-malate dehydrogenase (NAD(+), oxaloacetate-forming)

organism: Flavobacterium frigidimaris

assay_conditions_summary: pH 10; 303.15 K; cofactor NAD+


substrate_name: (S)-malate

enzyme: (S)-malate dehydrogenase (NAD(+), oxaloacetate-forming)

substrate: (S)-malate


organism: Malassezia pachydermatis

substrate_name: oxaloacetate

assay_conditions_summary: pH 7.6; buffer note "in 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer (pH 7.6), 1 mM MgCl2

substrate: oxaloacetate


organism: Tritrichomonas suis

assay_conditions_summary: cofactor NADH


enzyme_display_name: L-arabinose 1-dehydrogenase [NAD(P)(+)]

organism: Rhizobium leguminosarum bv. trifolii

substrate_name: L-arabinose

assay_conditions_summary: pH 9; 296.15 K; cofactor NADP+

proof_lines: with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C

proof_lines: with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C

enzyme: L-arabinose 1-dehydrogenase [NAD(P)(+)]

substrate: L-arabinose


proof_lines: L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C


substrate_name: D-galactose

substrate: D-galactose


assay_conditions_summary: pH 9; 296.15 K; cofactor NAD+


substrate_name: D-fucose

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

substrate: D-fucose


organism: Haemophilus influenzae

substrate_name: D-ribulose 5-phosphate

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

substrate: D-ribulose 5-phosphate


substrate_name: D-arabinose 5-phosphate

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

substrate: D-arabinose 5-phosphate


substrate_name: D-ribulose

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

substrate: D-ribulose


substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


substrate_name: NADPH

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: NADH

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.1; 303.15 K; cofactor NADPH


substrate_name: ribulose 5-phosphate

substrate: ribulose 5-phosphate


substrate_name: D-ribitol 5-phosphate

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

proof_lines:
presence of CTP, pH 7.1, 30°C
pH 7.1, 30°C

substrate: D-ribitol 5-phosphate


organism: Arabidopsis thaliana

proof_lines: mutant enzyme S133A, pH and temperature not specified in the publication


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


proof_lines: mutant enzyme S133T, pH and temperature not specified in the publication


enzyme_display_name: isocitrate dehydrogenase (NADP(+))

organism: Psychromonas marina

substrate_name: isocitrate

enzyme: isocitrate dehydrogenase (NADP(+))

substrate: isocitrate


organism: Thermoplasma acidophilum

substrate_name: NADP+

assay_conditions_summary: pH 7.5; 333.15 K; cofactor NADP+

substrate: NADP+


enzyme_display_name: phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating)

organism: Arthrobacter globiformis

assay_conditions_summary: cofactor NADP+


enzyme: phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating)


organism: Neurospora crassa

proof_lines: wild-type, mutant col 10, heterocaryon col-10-wild-type


proof_lines:
heterocaryon col-3-wild-type
heterocaryon col-10-wild-type


proof_lines:
heterocaryon col-3-col-10
source of enzyme: peak I
source of enzyme: whole cells


organism: Ovis aries

assay_conditions_summary: cofactor NADPH


proof_lines: 50 mM Tris-acetate, 5-10 mM MgCl2, pH 7.7


assay_conditions_summary: pH 7.7; 296.65 K; cofactor NADP+

proof_lines:
10 mM Tris-acetate, 10 mM MgCl2, pH 7.7
10 mM Tris-acetate, 80 mM KCl, pH 7.7
50 mM Tris-acetate, pH 7.7


organism: Synechococcus sp.


enzyme_display_name: polyprenol dehydrogenase [NAD(P)H]

organism: Homo sapiens

substrate_name: NAD+

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: pH 8.0, 37°C, cosubstrate: ditrans,polycis-polyprenol

enzyme: polyprenol dehydrogenase [NAD(P)H]

substrate: NAD+


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


substrate_name: ditrans,polycis-polyprenol

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

proof_lines:
pH 8.0, 37°C, cosubstrate: NAD+
pH 8.0, 37°C, cosubstrate: NADPH

substrate: ditrans,polycis-polyprenol


assay_conditions_summary: pH 8; 310.15 K; cofactor NADH


enzyme_display_name: glucose 1-dehydrogenase [NAD(P)(+)]

organism: Gluconobacter oxydans

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

enzyme: glucose 1-dehydrogenase [NAD(P)(+)]


substrate_name: D-glucose

substrate: D-glucose


organism: Pseudomonas sp.

assay_conditions_summary: cofactor NAD+


enzyme_display_name: pyridoxine 4-dehydrogenase

organism: Schizosaccharomyces pombe

enzyme: pyridoxine 4-dehydrogenase


substrate_name: pyridoxal

substrate: pyridoxal


enzyme_display_name: mannitol 2-dehydrogenase

organism: Cereibacter sphaeroides

enzyme: mannitol 2-dehydrogenase


substrate_name: D-mannitol

substrate: D-mannitol


substrate_name: D-arabinitol

smiles: C(C(C(C(CO)O)O)O)O

substrate: D-arabinitol


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: gluconate 5-dehydrogenase

organism: Aspergillus niger

assay_conditions_summary: pH 7

proof_lines: pH 7, temperature not specified in the publication

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: gluconate 5-dehydrogenase


substrate_name: D-gluconate

assay_conditions_summary: pH 8

proof_lines: pH 8, temperature not specified in the publication

proof_lines: pH 8.0, temperature not specified in the publication

substrate: D-gluconate


enzyme_display_name: glyoxylate reductase (NADP(+))

organism: Chlamydomonas reinhardtii

substrate_name: glyoxylate

enzyme: glyoxylate reductase (NADP(+))

substrate: glyoxylate


enzyme_display_name: hydroxypyruvate reductase

substrate_name: phenylpyruvate

proof_lines:
pH 7, 30°C
pH 7.0, 30°C, recombinant enzyme

enzyme: hydroxypyruvate reductase

substrate: phenylpyruvate


substrate_name: Hydroxypyruvate

proof_lines:
pH 7, 30°C
pH 7.0, 30°C, recombinant enzyme
GLYR1, at pH 7.8 and 22°C

substrate: Hydroxypyruvate


enzyme_display_name: ketol-acid reductoisomerase (NADP(+))

organism: Hordeum vulgare

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

enzyme: ketol-acid reductoisomerase (NADP(+))

substrate: NADPH


substrate_name: Unknown

proof_lines: pH 7.5, 25°C, with 2-aceto-2-hydroxybutyrate as substrate

proof_lines: pH 7.5, 25°C, with 2-acetolactate as substrate

substrate: Unknown


organism: Meiothermus ruber

assay_conditions_summary: pH 7; 323.15 K; cofactor NADPH

proof_lines: wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C

proof_lines: wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C


proof_lines: mutant enzyme T84S, with NADH as cosubstrate, at pH 7.0 and 50°C

proof_lines: mutant enzyme T84S, with NADPH as cosubstrate, at pH 7.0 and 50°C


organism: Streptomyces coelicolor


substrate_name: pyruvate

substrate: pyruvate


organism: Streptomyces griseus


organism: Streptomyces pristinaespiralis


organism: Vigna radiata var. radiata

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


enzyme_display_name: hydroxymethylglutaryl-CoA reductase

organism: Delftia acidovorans

substrate_name: NADH

assay_conditions_summary: pH 7.4; cofactor NADH

proof_lines: at pH 7.4, temperature not specified in the publication

enzyme: hydroxymethylglutaryl-CoA reductase

substrate: NADH


assay_conditions_summary: pH 7.4; cofactor CoA


enzyme_display_name: phosphoglycerate dehydrogenase

organism: Beta vulgaris

enzyme: phosphoglycerate dehydrogenase


organism: Marchantia polymorpha

assay_conditions_summary: pH 9

proof_lines: pH 9.0, temperature not specified in the publication


assay_conditions_summary: pH 9; cofactor NAD+


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

organism: Pseudomonas aeruginosa

substrate_name: L-lactate

proof_lines: pH 7.4, temperature not specified in the publication

enzyme: L-lactate dehydrogenase (cytochrome)

substrate: L-lactate


organism: Wickerhamomyces anomalus


enzyme_display_name: methanol dehydrogenase (cytochrome c)

organism: Hyphomicrobium denitrificans

substrate_name: ferricytochrome cL

proof_lines: pH 5.5, ionic strength: 0.0160 M, steady-state kinetic parameter

proof_lines: pH 6.0, ionic strength: 0.0172 M, steady-state kinetic parameter

proof_lines: pH 6.5, ionic strength: 0.0183 M, steady-state kinetic parameter

enzyme: methanol dehydrogenase (cytochrome c)

substrate: ferricytochrome cL


substrate_name: methanol

smiles: CO

substrate: methanol


enzyme_display_name: pyranose oxidase

organism: Phlebiopsis gigantea

proof_lines: pH 7.3, 22°C, recombinant wild-type enzyme

enzyme: pyranose oxidase


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


substrate_name: D-xylose

substrate: D-xylose


substrate_name: L-sorbose

substrate: L-sorbose


substrate_name: methyl-beta-D-glucoside

substrate: methyl-beta-D-glucoside


substrate_name: D-glucose

substrate: D-glucose


substrate_name: oxygen

smiles: O=O

substrate: oxygen


enzyme_display_name: alcohol oxidase

organism: Komagataella pastoris

proof_lines:
methanol concentration 1 mM
methanol concentration 10 mM
methanol concentration 100 mM

enzyme: alcohol oxidase


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


substrate_name: ethylene glycol

smiles: C(CO)O

substrate: ethylene glycol


smiles: CC(C)O


proof_lines:
at pH 7.4 and 30°C
pH 6.5, 22°C, immobilized enzyme
oxygen concentration 0.19 mM


enzyme_display_name: choline oxidase

organism: Arthrobacter globiformis

substrate_name: Betaine aldehyde

enzyme: choline oxidase

substrate: Betaine aldehyde


proof_lines: mutant enzyme S101A, in 50 mM sodium diphosphate, pH 10.0, at 25°C


substrate_name: choline

smiles: C[N+](C)(C)CCO

substrate: choline


proof_lines:
pH 7.0, 25°C, mutant N510A
pH 10.0, 25°C, mutant N510A


proof_lines:
pH 7.0, 25°C, mutant N510H
pH 10.0, 25°C, mutant N510H


proof_lines:
pH 7.0, 25°C, wild-type enzyme
wild-type, 30°C, pH 8
wild type enzyme, at pH 7.0 and 25°C


smiles: CC(C)(C)CCO


proof_lines:
pH 5.5, 25°C, mutant H466A
pH 5.5, 25°C, recombinant mutant H466A
pH 6.0, 25°C, recombinant mutant H466A


proof_lines: mutant enzyme H351Q, in 50 mM potassium phosphate (pH 7.0), at 25°C


proof_lines: wild type enzyme, in 50 mM potassium phosphate (pH 7.0), at 25°C


substrate_name: betaine-aldehyde

substrate: betaine-aldehyde


proof_lines: previously stored at pH 6 and -20°C, measured at pH 7 and 25°C

proof_lines: previously stored at pH 6 and 0°C, measured at pH 7 and 25°C


proof_lines: wild type enzyme, in 50 mM sodium diphosphate, pH 10.0, at 25°C


proof_lines: apparent, H99N mutant, substrate choline, pH 7, 25°C. Measuring the rate of oxygen consumption with a computer-interfaced Oxy-32 oxygen monitoring system


proof_lines: pH 10, 25°C, cosubstrate betaine aldehyde


substrate_name: N-Methylethanolamine

smiles: CNCCO

substrate: N-Methylethanolamine


substrate_name: N,N-dimethylethanolamine

smiles: CN(C)CCO

substrate: N,N-dimethylethanolamine


substrate_name: Unknown

substrate: Unknown


proof_lines: mutant enzyme M62A/F357A, at pH 7.0 and 25°C


enzyme_display_name: long-chain-alcohol oxidase

organism: Lotus japonicus

proof_lines: pH and temperature not specified in the publication

enzyme: long-chain-alcohol oxidase


smiles: CCCCCCCCCCCCCCCCO

proof_lines: 1 mM, purified active LjFAO1 protein, compared to substrate preferences with the AtFAO3 gene of Arabidopsis thaliana


smiles: C(CCCCCCCCO)CCCCCCCO


smiles: CCCCCCCCCCCCO

proof_lines: 5 mM, purified active LjFAO1 protein, compared to substrate preferences with the AtFAO3 gene of Arabidopsis thaliana


organism: [Candida] cloacae

substrate_name: Dodecanol

substrate: Dodecanol


enzyme_display_name: glucose oxidase

organism: Cladosporium neopsychrotolerans

substrate_name: beta-D-glucose

enzyme: glucose oxidase

substrate: beta-D-glucose


proof_lines: pH 7.0, 20-25°C, mutant enzyme Y169C/A211C


enzyme_display_name: aryl-alcohol oxidase

organism: Pleurotus eryngii

substrate_name: benzyl alcohol

proof_lines: mutant F501A expressed in Emericella nidulans

enzyme: aryl-alcohol oxidase

substrate: benzyl alcohol


substrate_name: 3-anisyl alcohol

substrate: 3-anisyl alcohol


smiles: CC=CC=CCO


substrate_name: 4-anisyl alcohol

substrate: 4-anisyl alcohol


substrate_name: veratryl alcohol

substrate: veratryl alcohol


proof_lines:
pH 6.0, 24°C, wild-type enzyme
pH 8.0, 25°C, wild-type enzyme


proof_lines: mutant F501Y expressed in Emericella nidulans


proof_lines: wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0


substrate_name: 3-fluorobenzyl alcohol

substrate: 3-fluorobenzyl alcohol


proof_lines: pH 8.0, 25°C, recombinant enzyme from Escherichia coli


substrate_name: 3-Chlorobenzyl alcohol

substrate: 3-Chlorobenzyl alcohol


substrate_name: 4-fluorobenzyl alcohol

substrate: 4-fluorobenzyl alcohol


substrate_name: 3-chloro-4-anisyl alcohol

proof_lines: pH 8.0, 25°C, recombinant enzyme from Emericella nidulans

substrate: 3-chloro-4-anisyl alcohol


substrate_name: 4-Chlorobenzyl alcohol

substrate: 4-Chlorobenzyl alcohol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: isovanillyl alcohol

substrate: isovanillyl alcohol


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


proof_lines:
pH 6.0, 25°C, mutant H502S
pH 60, 25°C, mutant H502S


proof_lines:
pH 6.0, 25°C, mutant H502A
pH 60, 25°C, mutant H502A


proof_lines:
pH 6.0, 25°C, mutant H546A
pH 60, 25°C, mutant H546A


proof_lines:
pH 6.0, 25°C, mutant H546S
pH 60, 25°C, mutant H546S


proof_lines: recombinant protein from wild-type Saccharomyces cerevisiae, pH 6, 25°C

proof_lines: recombinant wild-type enzyme, pH 6.0, 24°C


proof_lines: recombinant protein from glycosylation-deficient Saccharomyces cerevisiae, pH 6, 25°C


proof_lines: recombinant protein from wild-type Pichia pastoris, pH 6, 25°C


proof_lines: pH 6.0, 25°C, wild-type enzyme, overall reaction


proof_lines:
pH 6, 25°C, presence of 1 mM H2O2
pH 6, 25°C, presence of 15 mM H2O2
pH 6, 25°C


proof_lines: pH 6, 25°C, presence of 6 mM formylfurancarboxylic acid

proof_lines: pH 6, 25°C, presence of 0.8 mM formylfurancarboxylic acid

proof_lines: substrate alpha-deuterated 4-methoxybenzyl alcohol, pH 6.0, 25°C


proof_lines: with 3-fluorobenzyl alcohol, 25°C, pH 6.0, recombinant enzyme

proof_lines: with 2,4-hexadien-1-ol, 25°C, pH 6.0, recombinant enzyme

proof_lines: with 4-anisyl alcohol, 25°C, pH 6.0, recombinant enzyme


substrate_name: 2,4-Dimethoxybenzyl alcohol

substrate: 2,4-Dimethoxybenzyl alcohol


proof_lines: mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0


substrate_name: veratraldehyde

proof_lines: wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0

substrate: veratraldehyde


smiles: CC=CC=CC=O

proof_lines: wild type enzyme, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0


substrate_name: benzaldehyde

substrate: benzaldehyde


proof_lines: recombinant H91N FX7 mutant, pH 6.0, 24°C


proof_lines: pH 6.0, 25°C, mutant F501A, overall reaction

proof_lines: mutant F501A expressed in Emericella nidulans

proof_lines: pH 6.0, 25°C, mutant F501A, oxidative half-reaction


proof_lines: pH 6.0, 25°C, mutant F501W, overall reaction

proof_lines: pH 6.0, 25°C, mutant F501W, oxidative half-reaction


proof_lines: pH 6.0, 25°C, mutant F501Y, overall reaction

proof_lines: mutant F501Y expressed in Emericella nidulans

proof_lines: pH 6.0, 25°C, mutant F501Y, oxidative half-reaction


enzyme_display_name: L-gulonolactone oxidase

organism: Capra hircus

enzyme: L-gulonolactone oxidase


enzyme_display_name: galactose oxidase

organism: Aspergillus sp.

enzyme: galactose oxidase


substrate_name: D-galactose

substrate: D-galactose


organism: Fusarium subglutinans


enzyme_display_name: glycerol-3-phosphate dehydrogenase

organism: Cyberlindnera jadinii

substrate_name: DL-alpha-glycerophosphate

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

enzyme: glycerol-3-phosphate dehydrogenase

substrate: DL-alpha-glycerophosphate


organism: Mus musculus

substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: malate dehydrogenase (quinone)

organism: Mycolicibacterium smegmatis

enzyme: malate dehydrogenase (quinone)


substrate_name: (S)-malate

substrate: (S)-malate


enzyme_display_name: alcohol dehydrogenase (quinone)

organism: Gluconobacter oxydans

substrate_name: pyrroloquinoline quinone

proof_lines: pH 5.0, 25°C, quinone-bound enzyme, in presence of N-dodecyl-beta-D-maltoside

proof_lines: ubiquinone-bound enzyme, in the presence of dodecylmaltoside, at pH 5.0 and 25°C

proof_lines: pH 5.0, 25°C, quinone-free enzyme, in presence of N-dodecyl-beta-D-maltoside

enzyme: alcohol dehydrogenase (quinone)

substrate: pyrroloquinoline quinone


organism: Gluconobacter sp.

substrate_name: ethanol

substrate: ethanol


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Acinetobacter calcoaceticus

substrate_name: quinate

proof_lines: pH 6.5, 25°C,with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor

substrate: quinate


substrate_name: shikimate

proof_lines: pH 6.5, 25°C, with potassium ferricyanide or a combination of phenazine methosulfate and 2,6-dichlorophenol indophenol as electron acceptor

substrate: shikimate


substrate_name: potassium ferricyanide

substrate: potassium ferricyanide


substrate_name: 2,6-dichlorophenol indophenol

substrate: 2,6-dichlorophenol indophenol


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


substrate_name: oxidized coenzyme F420

substrate: oxidized coenzyme F420


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


enzyme_display_name: choline dehydrogenase

organism: Rattus norvegicus

substrate_name: phenazine methosulfate

proof_lines:
at 10 mM choline
with choline

enzyme: choline dehydrogenase

substrate: phenazine methosulfate


substrate_name: p-benzoquinone

substrate: p-benzoquinone


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


proof_lines: inhibits the oxidation of choline competitively


substrate_name: choline

proof_lines: electron acceptor: phenazine methosulfate

substrate: choline


enzyme_display_name: cellobiose dehydrogenase (acceptor)

organism: Hypoxylon haematostroma

substrate_name: D-glucose

enzyme: cellobiose dehydrogenase (acceptor)

substrate: D-glucose


substrate_name: cytochrome c

substrate: cytochrome c


substrate_name: maltose

substrate: maltose


organism: Stachybotrys bisbyi

proof_lines:
at pH 5.0 and 30°C
at pH 5.5 and 30°C


proof_lines:
at pH 5.0 and 30°C
at pH 5.5 and 30°C
at pH 5.?5 and 30°C


organism: Trametes cinnabarina

substrate_name: cellobiose

substrate: cellobiose