enzyme_display_name: UniProt P00492

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.4

enzyme: UniProt P00492


enzyme_display_name: UniProt P20035

organism: Plasmodium falciparum

substrate_name: xanthine

source_db: skid

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY-NC-ND 4.0

km_unit: mM

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

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=23°C, pH=7.4

data_origin: experimental

enzyme: UniProt P20035

substrate: xanthine

source: skid


substrate_name: hypoxanthine

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=28°C, pH=7.4
Raw SKiD Env: Temp=23°C, pH=7.4

substrate: hypoxanthine


substrate_name: guanine

substrate: guanine


organism: Homo sapiens

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=28°C, pH=7.4


kcat_display: Not reported

kcat_over_km_display: Not reported


substrate_name: diphosphate

substrate: diphosphate


enzyme_display_name: UniProt Q07010

organism: Trypanosoma brucei brucei

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

enzyme: UniProt Q07010

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


enzyme_display_name: UniProt Q5ZVC1

organism: Legionella pneumophila

enzyme: UniProt Q5ZVC1


enzyme_display_name: UniProt Q9NJI5

organism: Leishmania tarentolae

substrate_name: 5-phosphoribosyl 1-diphosphate

enzyme: UniProt Q9NJI5

substrate: 5-phosphoribosyl 1-diphosphate


enzyme_display_name: hypoxanthine phosphoribosyltransferase

organism: Mycobacterium tuberculosis

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

source_license: CC BY 4.0

enzyme: hypoxanthine phosphoribosyltransferase

status: unverified

source: oed


organism: Trypanosoma cruzi

substrate_name: myristoyl-CoA

source_db: brenda

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

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

substrate: myristoyl-CoA

source: brenda


enzyme_display_name: fatty-acid synthase system

organism: Anas platyrhynchos

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

proof_lines:
pH 7.0, 37°C, substrate acetyl-CoA
pH 7.0, 37°C, substrate NADPH
pH 7.0, 37°C, substrate malonyl-CoA

enzyme: fatty-acid synthase system

substrate: Unknown


substrate_name: CAP5.5 peptide

proof_lines:
source Trypanosoma cruzi, pH 7.4, 30°C
source Trypanosoma brucei, pH 7.4, 30°C
pH 7.4, 30°C

substrate: CAP5.5 peptide


enzyme_display_name: UniProt P9WHK9

substrate_name: Orotate

enzyme: UniProt P9WHK9

substrate: Orotate


substrate_name: orotidine 5'-phosphate

substrate: orotidine 5'-phosphate


enzyme_display_name: UniProt P13298

organism: Saccharomyces cerevisiae

enzyme: UniProt P13298


enzyme_display_name: UniProt Q8T6J6

organism: Vigna mungo

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

assay_conditions_summary: pH 8

enzyme: UniProt Q8T6J6


enzyme_display_name: UniProt P43490

substrate_name: phosphate

enzyme: UniProt P43490

substrate: phosphate


substrate_name: ATP

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.5

substrate: ATP


substrate_name: ADP

substrate: ADP


enzyme_display_name: UniProt Q9STG9

organism: Arabidopsis thaliana

enzyme: UniProt Q9STG9


enzyme_display_name: UniProt G7JFL4

organism: Medicago truncatula

enzyme: UniProt G7JFL4


enzyme_display_name: UniProt Q5HSJ4

organism: Campylobacter jejuni

enzyme: UniProt Q5HSJ4


enzyme_display_name: sterol 3beta-glucosyltransferase

organism: Zea mays

substrate_name: UDP-glucose

proof_lines: slightly lowered by phosphatidylcholine and phosphatidylglycerol

enzyme: sterol 3beta-glucosyltransferase

substrate: UDP-glucose


substrate_name: sitosterol

proof_lines: strongly lowered by phosphatidylcholine and phosphatidylglycerol

substrate: sitosterol


organism: Sus scrofa

substrate_name: asialo-mucin of Cowper's gland

proof_lines: calculated on the basis of terminal N-galactosaminyl residues

substrate: asialo-mucin of Cowper's gland


substrate_name: UDP-galactose

substrate: UDP-galactose


enzyme_display_name: trihydroxystilbene synthase

organism: Arachis hypogaea

substrate_name: malonyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: trihydroxystilbene synthase

substrate: malonyl-CoA


assay_conditions_summary: pH 4; 303.15 K; cofactor CoA

proof_lines: pH 4.0, 30°C, recombinant STS, uncompetitive inhibition

proof_lines: pH 4.0, 30°C, recombinant STS, competitive inhibition


enzyme_display_name: UniProt P9WJJ7

substrate_name: quinolinic acid

enzyme: UniProt P9WJJ7

substrate: quinolinic acid


enzyme_display_name: UniProt Q15274

enzyme: UniProt Q15274


enzyme_display_name: UniProt Q05603

organism: Salmonella enterica

substrate_name: beta-nicotinate D-ribonucleotide

enzyme: UniProt Q05603

substrate: beta-nicotinate D-ribonucleotide


enzyme_display_name: UniProt P42085

organism: Bacillus subtilis

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.6

enzyme: UniProt P42085

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


substrate_name: Arabidopsis thaliana protein CDPK6-derived peptide


organism: Bos taurus

substrate_name: AQPTPPP

proof_lines: derived from the bovine myelin basic protein sequence

proof_lines: derived from the major acceptor sequence in myelin basic protein

substrate: AQPTPPP


enzyme_display_name: malate synthase

substrate_name: acetyl-CoA

enzyme: malate synthase

substrate: acetyl-CoA


substrate_name: glyoxylate

substrate: glyoxylate


enzyme_display_name: UniProt I0B503

organism: Schistosoma mansoni

enzyme: UniProt I0B503


substrate_name: adenosine

substrate: adenosine


enzyme_display_name: UniProt Q7XA67

enzyme: UniProt Q7XA67


enzyme_display_name: UniProt Q8YBL1

organism: Brucella melitensis

enzyme: UniProt Q8YBL1


enzyme_display_name: UniProt Q9T0I8

enzyme: UniProt Q9T0I8


enzyme_display_name: UniProt P50389

organism: Saccharolobus solfataricus

enzyme: UniProt P50389


substrate_name: S-adenosylhomocysteine

substrate: S-adenosylhomocysteine


enzyme_display_name: UniProt C9Z6T8

organism: Streptomyces scabiei

substrate_name: NAD+

enzyme: UniProt C9Z6T8

substrate: NAD+


enzyme_display_name: UniProt Q8N5Y8

organism: Homo sapiens

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

enzyme: UniProt Q8N5Y8


enzyme_display_name: N-acetyllactosamine synthase

substrate_name: D-glucose

enzyme: N-acetyllactosamine synthase

substrate: D-glucose


enzyme_display_name: UniProt Q9HZK1

organism: Pseudomonas aeruginosa

substrate_name: adenine

enzyme: UniProt Q9HZK1

substrate: adenine


enzyme_display_name: alpha-tubulin N-acetyltransferase

enzyme: alpha-tubulin N-acetyltransferase


organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

substrate_name: pABA (at 70 degrees Celsius)

source_db: uniprot

substrate: pABA (at 70 degrees Celsius)

source: uniprot


organism: Triticum aestivum

substrate_name: Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg

substrate: Gly-Asn-Ala-Ala-Ser-Ala-Arg-Arg


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


enzyme_display_name: UniProt Q9BXR0

substrate_name: queuine

enzyme: UniProt Q9BXR0

substrate: queuine


substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Enterococcus faecalis

substrate_name: Unknown

assay_conditions_summary: pH 8; 291.15 K; cofactor CoA

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: Unknown


organism: Escherichia coli

proof_lines: pH 7.5, 30°C, noncompetitive inhibition against (R)-3-hydroxymyristoyl-[acyl-carrier protein]


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

substrate_name: gentamicin C1a

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: gentamicin C1a


enzyme_display_name: UniProt P13721

organism: Rattus norvegicus

substrate_name: CMP-N-acetylneuraminate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P13721

substrate: CMP-N-acetylneuraminate


enzyme_display_name: UniProt P15907

substrate_name: CMP-N-acetyl-beta-neuraminate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.4

enzyme: UniProt P15907

substrate: CMP-N-acetyl-beta-neuraminate


enzyme_display_name: UniProt A8QYL1

organism: Photobacterium sp.

substrate_name: lactose

enzyme: UniProt A8QYL1

substrate: lactose


substrate_name: methyl-beta-D-galactopyranoside

substrate: methyl-beta-D-galactopyranoside


enzyme_display_name: UniProt Q02745

organism: Sus scrofa

enzyme: UniProt Q02745


enzyme_display_name: UniProt Q15KI8

organism: Pasteurella multocida

enzyme: UniProt Q15KI8


enzyme_display_name: UniProt A5LHX0

organism: Photobacterium phosphoreum

enzyme: UniProt A5LHX0


proof_lines: pH 8.0, 25°C, recombinant His6-tagged LpxD


organism: Gallus gallus

substrate_name: acetyl-CoA

proof_lines:
acetyl-CoA hydrolysis
0.005 mM acetoacetyl-CoA
reombinant enzyme

substrate: acetyl-CoA


enzyme_display_name: 2-methylcitrate synthase

substrate_name: propionyl-CoA

enzyme: 2-methylcitrate synthase

substrate: propionyl-CoA


substrate_name: S-(3-Oxobutyl)-CoA; Acetyl-CoA; H2O

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

substrate: S-(3-Oxobutyl)-CoA; Acetyl-CoA; H2O


enzyme_display_name: sterol 3beta-glucosyltransferase

organism: Gossypium hirsutum

substrate_name: UDP-glucose

enzyme: sterol 3beta-glucosyltransferase

substrate: UDP-glucose


substrate_name: UDP-Gal

substrate: UDP-Gal


substrate_name: acetoacetyl-CoA

proof_lines:
cytoplasmic isozymes I-IV
recombinant enzyme, hydrolase reaction

substrate: acetoacetyl-CoA


enzyme_display_name: UniProt P24173

substrate_name: ADP-L-glycero-beta-D-manno-heptose

enzyme: UniProt P24173

substrate: ADP-L-glycero-beta-D-manno-heptose


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


enzyme_display_name: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate_name: GDP-L-fucose

proof_lines:
H-gene encoded enzyme
enzyme from plasma
reaction with GM1, recombinant enzyme

substrate: GDP-L-fucose


proof_lines:
recombinant enzyme
enzyme from gastric mucosa
H-gene encoded enzyme

enzyme: type 1 galactoside alpha-(1,2)-fucosyltransferase


substrate_name: N-acetylglucosamine

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

proof_lines:
recombinant enzyme
recombinant N-deglycosylated enzyme

substrate: N-acetylglucosamine


substrate_name: lactosylceramide

substrate: lactosylceramide


substrate_name: N-acetyl-D-galactosamine

substrate: N-acetyl-D-galactosamine


enzyme_display_name: Geranylgeranyl pyrophosphate synthase BTS1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


substrate_name: isopentenyl diphosphate

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

enzyme: Geranylgeranyl pyrophosphate synthase BTS1

substrate: isopentenyl diphosphate


enzyme_display_name: UniProt P45741

organism: Paenibacillus thiaminolyticus

enzyme: UniProt P45741


enzyme_display_name: Thiamine-phosphate synthase

organism: Escherichia coli (strain K12)

substrate_name: HMP-PP

enzyme: Thiamine-phosphate synthase

substrate: HMP-PP


substrate_name: THZ-P

substrate: THZ-P


enzyme_display_name: UniProt P31153

substrate_name: L-methionine

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P31153

substrate: L-methionine


enzyme_display_name: UniProt Q980S9

organism: Saccharolobus solfataricus

substrate_name: L-ethionine

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=65°C, pH=8

enzyme: UniProt Q980S9

substrate: L-ethionine


substrate_name: ATP

proof_lines:
Raw SKiD Env: Temp=65°C, pH=8
Raw SKiD Env: Temp=37°C, pH=8

substrate: ATP


enzyme_display_name: UniProt P13444

enzyme: UniProt P13444


enzyme_display_name: UniProt Q72I53

organism: Thermus thermophilus

enzyme: UniProt Q72I53


substrate_name: methionine

substrate: methionine


enzyme_display_name: UniProt P0A749

substrate_name: phosphoenolpyruvate

enzyme: UniProt P0A749

substrate: phosphoenolpyruvate


enzyme_display_name: UniProt P33038

organism: Enterobacter cloacae

substrate_name: UDP-N-acetyl-D-glucosamine

enzyme: UniProt P33038

substrate: UDP-N-acetyl-D-glucosamine


enzyme_display_name: N-acetyllactosamine synthase

organism: Mus musculus

substrate_name: asialo-agalacto-transferrin

enzyme: N-acetyllactosamine synthase

substrate: asialo-agalacto-transferrin


organism: Homo sapiens

proof_lines: pH 7.2, temperature not specified in the publication


substrate_name: UDP-alpha-D-galactose

proof_lines:
at pH 6.3 and 37°C
recombinant enzyme
recombinant N-deglycosylated enzyme

substrate: UDP-alpha-D-galactose


organism: Methanosarcina barkeri

substrate_name: N-Furfurylformamide

substrate: N-Furfurylformamide


substrate_name: L-histidine

substrate: L-histidine


substrate_name: N-acetylglucosamine

substrate: N-acetylglucosamine


substrate_name: Gly-Ser-Ser-Lys-Pro-Lys-Asp-Lys-Asp-Pro

substrate: Gly-Ser-Ser-Lys-Pro-Lys-Asp-Lys-Asp-Pro


organism: Mycobacterium tuberculosis

smiles: CCCCCCCCCCC(C)O


organism: Plasmodium falciparum

substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: phloroglucinol synthase

organism: Pseudomonas fluorescens

substrate_name: malonyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: pH and temperature not specified in the publication

enzyme: phloroglucinol synthase

substrate: malonyl-CoA


enzyme_display_name: ATP citrate synthase

organism: Rattus norvegicus

substrate_name: citrate

enzyme: ATP citrate synthase

substrate: citrate


substrate_name: UDPgalactose

substrate: UDPgalactose


proof_lines:
enzyme from liver microsomal membrane
enzyme from serum
enzyme from liver


substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


enzyme_display_name: UniProt Q25704

enzyme: UniProt Q25704


enzyme_display_name: UniProt Q81VW8

organism: Bacillus anthracis

substrate_name: sulfanilamide

enzyme: UniProt Q81VW8

substrate: sulfanilamide


substrate_name: sulfisoxazole

substrate: sulfisoxazole


substrate_name: sulfamethoxazole

substrate: sulfamethoxazole


substrate_name: sulfamethizole

substrate: sulfamethizole


substrate_name: Sulfadiazine

substrate: Sulfadiazine


substrate_name: sulfathiazole

substrate: sulfathiazole


substrate_name: dapson

substrate: dapson


enzyme_display_name: UniProt P0AC13

organism: Escherichia coli MC4100

enzyme: UniProt P0AC13


enzyme_display_name: UniProt P53848

organism: Saccharomyces cerevisiae

enzyme: UniProt P53848


substrate_name: p-Aminobenzoic acid

substrate: p-Aminobenzoic acid


enzyme_display_name: UniProt P9WND1

enzyme: UniProt P9WND1


enzyme_display_name: UniProt P09158

organism: Escherichia coli

substrate_name: S-adenosylmethioninamine

enzyme: UniProt P09158

substrate: S-adenosylmethioninamine


enzyme_display_name: UniProt Q31QK9

organism: Synechococcus elongatus

substrate_name: putrescine

smiles: C(CCN)CN

enzyme: UniProt Q31QK9

substrate: putrescine


substrate_name: p60src-derived peptide

substrate: p60src-derived peptide


enzyme_display_name: cytochrome-b5 reductase

substrate_name: testosterone

enzyme: cytochrome-b5 reductase

substrate: testosterone


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

substrate_name: acetyl-CoA

proof_lines: absence of acetoacetyl-CoA, hydrolysis reaction

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: acetyl-CoA


enzyme_display_name: type 1 galactoside alpha-(1,2)-fucosyltransferase

substrate_name: GDP-L-fucose

proof_lines: reaction with porcine submaxillary mucin or intestinal glycoprotein

substrate: GDP-L-fucose


substrate_name: CoA

substrate: CoA


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: CDP

enzyme: ribonucleoside-diphosphate reductase

substrate: CDP


substrate_name: N-acetylglucosamine

substrate: N-acetylglucosamine


substrate_name: aquacobalamin

assay_conditions_summary: cofactor NADH

substrate: aquacobalamin


enzyme_display_name: catechol 1,2-dioxygenase

organism: Rhizobium leguminosarum

substrate_name: catechol

enzyme: catechol 1,2-dioxygenase

substrate: catechol


enzyme_display_name: protocatechuate 3,4-dioxygenase

substrate_name: protocatechuate

enzyme: protocatechuate 3,4-dioxygenase

substrate: protocatechuate


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

organism: Pseudomonas aeruginosa

substrate_name: gentamicin C1

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: gentamicin C1


enzyme_display_name: trimethylamine monooxygenase

organism: Ruegeria pomeroyi

substrate_name: N,N,N-trimethylamine

smiles: CN(C)C

assay_conditions_summary: pH 7.6; 295.15 K; buffer 80 mM PIPES

proof_lines: recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C

enzyme: trimethylamine monooxygenase

substrate: N,N,N-trimethylamine


enzyme_display_name: trans-aconitate 3-methyltransferase

substrate_name: Itaconate

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

enzyme: trans-aconitate 3-methyltransferase

substrate: Itaconate


enzyme_display_name: cysteine dioxygenase

substrate_name: Unknown

enzyme: cysteine dioxygenase

substrate: Unknown


enzyme_display_name: benzoate 1,2-dioxygenase

organism: Rhodococcus opacus

enzyme: benzoate 1,2-dioxygenase


enzyme_display_name: ferroxidase

substrate_name: Fe(II)

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication

enzyme: ferroxidase

substrate: Fe(II)


substrate_name: myristoyl-CoA

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

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
pH 8.0, 30°C, continuous assay
chemical transformation step
with Gly-Asn-Ala-Ala-Ser-Tyr-Arg-Arg

substrate: myristoyl-CoA


enzyme_display_name: alcohol O-acetyltransferase

substrate_name: isoamyl alcohol

smiles: CC(C)CCO

proof_lines: Yeast alcohol acetyltransferase review context only; no row-specific accession anchor preserved.

enzyme: alcohol O-acetyltransferase

substrate: isoamyl alcohol


proof_lines:
wild-type, pH 6.0
wild-type, pH 6.5, 4°C


substrate_name: Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys

substrate: Gly-Ser-Ser-Lys-Ser-Lys-Pro-Lys


enzyme_display_name: UniProt P31570

organism: Salmonella enterica

substrate_name: cob(II)inamide

enzyme: UniProt P31570

substrate: cob(II)inamide


substrate_name: ATP

substrate: ATP


enzyme_display_name: UniProt Q96EY8

enzyme: UniProt Q96EY8


substrate_name: cob(I)alamin

substrate: cob(I)alamin


enzyme_display_name: UniProt Q9HIA7

organism: Thermoplasma acidophilum

substrate_name: Cobalamin

enzyme: UniProt Q9HIA7

substrate: Cobalamin


substrate_name: hydroxocobalamin

substrate: hydroxocobalamin


substrate_name: dATP

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=70°C, pH=8

substrate: dATP


enzyme_display_name: glutathione transferase

organism: Chlamys islandica

substrate_name: glutathione

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

enzyme: glutathione transferase

substrate: glutathione


enzyme_display_name: UniProt M2QJS8

organism: Gelatoporia subvermispora

substrate_name: cumene hydroperoxide

enzyme: UniProt M2QJS8

substrate: cumene hydroperoxide


substrate_name: 4-methylumbelliferyl acetate

substrate: 4-methylumbelliferyl acetate


substrate_name: 5-chloromethylfluorescein diacetate

substrate: 5-chloromethylfluorescein diacetate


enzyme_display_name: UniProt O49235

organism: Glycine max

enzyme: UniProt O49235


enzyme_display_name: UniProt P30711

organism: Homo sapiens

substrate_name: iodobutane

smiles: CCC(C)I

enzyme: UniProt P30711

substrate: iodobutane


substrate_name: iodohexane

smiles: CCCCCCI

substrate: iodohexane


substrate_name: iodomethane

smiles: CI

substrate: iodomethane


enzyme_display_name: UniProt P09211

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.4
Raw SKiD Env: Temp=25°C, pH=6.5
Raw SKiD Env: Temp=30°C, pH=6.5

enzyme: UniProt P09211


enzyme_display_name: UniProt A8R5V3

organism: Bombyx mori

enzyme: UniProt A8R5V3


smiles: CCCCCC(C=CC=O)O


substrate_name: Ethacrynic acid

substrate: Ethacrynic acid


proof_lines:
Raw SKiD Env: Temp=-----, pH=6.5
Raw SKiD Env: Temp=30°C, pH=6.5
Raw SKiD Env: Temp=25°C, pH=6.5


enzyme_display_name: UniProt Q5CCJ4

enzyme: UniProt Q5CCJ4


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=6.5


enzyme_display_name: UniProt Q9FQE8

enzyme: UniProt Q9FQE8


substrate_name: fluorodifen

substrate: fluorodifen


substrate_name: tert-butyl peroxide

smiles: CC(C)(C)OOC(C)(C)C

substrate: tert-butyl peroxide


organism: Isoptericola variabilis

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


enzyme_display_name: UniProt Q9S400

organism: Streptococcus pneumoniae

substrate_name: phosphate

enzyme: UniProt Q9S400

substrate: phosphate


enzyme_display_name: UniProt P0A6D3

enzyme: UniProt P0A6D3


substrate_name: shikimate 3-phosphate

substrate: shikimate 3-phosphate


enzyme_display_name: UniProt P37268

substrate_name: farnesyl diphosphate

enzyme: UniProt P37268

substrate: farnesyl diphosphate


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

substrate_name: Unknown

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, competitive inhibition, substrate acetyl-CoA

proof_lines: pH 8.0, mixed inhibition, substrate acetoacetyl-CoA

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: Unknown


substrate_name: NADH

assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADH

proof_lines: using ubiquinone-2 as substrate, in 20 mM MOPS/KOH, 1 mM EDTA, 0.03% (v/v) Triton X-100, 200 mM KCl, pH 6.2, temperature not specified in the publication

substrate: NADH


substrate_name: acetyl-CoA

proof_lines:
strain NCYC 366
isoamyl acetate synthesis
ethyl acetate synthesis

substrate: acetyl-CoA


enzyme_display_name: cytochrome-b5 reductase

organism: Rattus norvegicus

enzyme: cytochrome-b5 reductase


organism: Saccharomyces cerevisiae

proof_lines:
apparent value, at pH 7.5 and 30°C
at pH 7.5 and 25°C
competitive inhibition


enzyme_display_name: sterol 14alpha-demethylase

enzyme: sterol 14alpha-demethylase


enzyme_display_name: UniProt P58758

organism: Agrobacterium tumefaciens

enzyme: UniProt P58758


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


substrate_name: AMP

substrate: AMP


enzyme_display_name: geranylgeranyl diphosphate synthase

organism: Capsicum annuum

enzyme: geranylgeranyl diphosphate synthase


substrate_name: geranyl diphosphate

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

substrate: geranyl diphosphate


organism: Sinapis alba


substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


enzyme_display_name: UniProt Q12051

substrate_name: (2E,6E)-farnesyl diphosphate

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

sequence_source: multiple

source_databases_merged: skid uniprot

enzyme: UniProt Q12051

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: UniProt Q94IE8

organism: Eucommia ulmoides

enzyme: UniProt Q94IE8


enzyme_display_name: UniProt P55984

organism: Helicobacter pylori

enzyme: UniProt P55984


enzyme_display_name: UniProt O82827

organism: Micrococcus luteus

substrate_name: (2Z,6E,10E)-geranylgeranyl diphosphate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=37°C, pH=7.5

enzyme: UniProt O82827

substrate: (2Z,6E,10E)-geranylgeranyl diphosphate


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.3
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.5


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: thioredoxin

enzyme: ribonucleoside-diphosphate reductase

substrate: thioredoxin


enzyme_display_name: malate synthase

substrate_name: glyoxylate

enzyme: malate synthase

substrate: glyoxylate


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: UDP-galactose

substrate: UDP-galactose


enzyme_display_name: UniProt Q50EL0

organism: Aspergillus fumigatus

substrate_name: L-tryptophan methyl ester

enzyme: UniProt Q50EL0

substrate: L-tryptophan methyl ester


substrate_name: L-o-tyrosine

substrate: L-o-tyrosine


substrate_name: L-abrine

substrate: L-abrine


substrate_name: L-m-tyrosine

substrate: L-m-tyrosine


substrate_name: cyclo-L-Trp-L-Trp

substrate: cyclo-L-Trp-L-Trp


substrate_name: cyclo-L-Trp-L-Pro

substrate: cyclo-L-Trp-L-Pro


enzyme_display_name: ferroxidase

smiles: O=O

enzyme: ferroxidase


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Serratia marcescens

substrate_name: ribostamycin

proof_lines:
full length enzyme, pH 7.5, 25°C
isolated AAC(6') domain, pH 7.5, 25°C

enzyme: aminoglycoside 6'-N-acetyltransferase

substrate: ribostamycin


enzyme_display_name: mercury(II) reductase

enzyme: mercury(II) reductase


organism: Solanum tuberosum


enzyme_display_name: monodehydroascorbate reductase (NADH)

substrate_name: monodehydroascorbate

enzyme: monodehydroascorbate reductase (NADH)

substrate: monodehydroascorbate


enzyme_display_name: catechol 2,3-dioxygenase

organism: Sphingomonas sp.

substrate_name: catechol

proof_lines:
hybrid enzyme, pH 7.5, 25°C
native enzyme, pH 7.5, 25°C

enzyme: catechol 2,3-dioxygenase

substrate: catechol


enzyme_display_name: ferredoxin hydrogenase

organism: Sporomusa sphaeroides

smiles: [HH]

enzyme: ferredoxin hydrogenase


enzyme_display_name: UniProt P49366

organism: Homo sapiens

substrate_name: spermidine

smiles: C(CCNCCCN)CN

enzyme: UniProt P49366

substrate: spermidine


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: UniProt A8YBP8

organism: Microcystis aeruginosa

substrate_name: O-acetyl-L-serine

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

enzyme: UniProt A8YBP8

substrate: O-acetyl-L-serine


enzyme_display_name: UniProt A8YBS4

enzyme: UniProt A8YBS4


enzyme_display_name: UniProt D2Z027

organism: Streptomyces lavendulae

substrate_name: thiosulfate

enzyme: UniProt D2Z027

substrate: thiosulfate


enzyme_display_name: Cysteine synthase A

organism: Escherichia coli (strain K12)

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

enzyme: Cysteine synthase A


substrate_name: thioglycolate

substrate: thioglycolate


organism: Spinacia oleracea

substrate_name: O-acetylserine

substrate: O-acetylserine


substrate_name: sulfide

substrate: sulfide


enzyme_display_name: cystathionine gamma-synthase

organism: Lysinibacillus sphaericus

substrate_name: O-succinyl-L-homoserine

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

enzyme: cystathionine gamma-synthase

substrate: O-succinyl-L-homoserine


substrate_name: O-acetyl-L-homoserine

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

substrate: O-acetyl-L-homoserine


enzyme_display_name: NADPH:quinone reductase

organism: Staphylococcus aureus

enzyme: NADPH:quinone reductase


enzyme_display_name: ectoine hydroxylase

organism: Stutzerimonas stutzeri

substrate_name: L-homoectoine

enzyme: ectoine hydroxylase

substrate: L-homoectoine


enzyme_display_name: nitric oxide reductase (cytochrome c)

substrate_name: Unknown

enzyme: nitric oxide reductase (cytochrome c)

substrate: Unknown


enzyme_display_name: catechol 1,2-dioxygenase

proof_lines: pH 8.5, temperature not specified in the publication

enzyme: catechol 1,2-dioxygenase


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Sus scrofa

substrate_name: acetyl-CoA

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: acetyl-CoA


enzyme_display_name: biflaviolin synthase

organism: Streptomyces coelicolor

substrate_name: flaviolin

verification_status: corrected

column_label: PMID 15659395 page 11601, Results section 'An Endogenous Function and Probable Biological Role of CYP158A2'; metric label turnover number for flaviolin oxidation.

raw_value_unit_evidence: Results prose reports turnover number 1.4 min^-1 for flaviolin oxidation.

enzyme: biflaviolin synthase

substrate: flaviolin

status: corrected


enzyme_display_name: N-acetyllactosamine synthase

substrate_name: N-acetylglucosamine

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

enzyme: N-acetyllactosamine synthase

substrate: N-acetylglucosamine


enzyme_display_name: beta-pyrazolylalanine synthase

organism: Citrullus lanatus

enzyme: beta-pyrazolylalanine synthase


substrate_name: pyrazole

substrate: pyrazole


enzyme_display_name: UniProt G3XCJ9

organism: Pseudomonas aeruginosa

substrate_name: D-erythrose 4-phosphate

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

enzyme: UniProt G3XCJ9

substrate: D-erythrose 4-phosphate


enzyme_display_name: UniProt P0AB91

organism: Escherichia coli

substrate_name: phosphoenolpyruvate

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

enzyme: UniProt P0AB91

substrate: phosphoenolpyruvate


enzyme_display_name: UniProt Q9K169

organism: Neisseria meningitidis

proof_lines:
Raw SKiD Env: Temp=25°C, pH=6.8
Raw SKiD Env: Temp=30°C, pH=6.8

enzyme: UniProt Q9K169


enzyme_display_name: UniProt O66496

organism: Aquifex aeolicus

proof_lines:
Raw SKiD Env: Temp=40°C, pH=7.5
Raw SKiD Env: Temp=40°C, pH=5
Raw SKiD Env: Temp=60°C, pH=7.5

enzyme: UniProt O66496


substrate_name: D-arabinose 5-phosphate

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=40°C, pH=7.5
Raw SKiD Env: Temp=40°C, pH=5

substrate: D-arabinose 5-phosphate


enzyme_display_name: UniProt P0A715

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.3

enzyme: UniProt P0A715


enzyme_display_name: UniProt Q9JZ55

enzyme: UniProt Q9JZ55


substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


substrate_name: UDP-GalNAc

substrate: UDP-GalNAc


substrate_name: Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro

substrate: Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: 1-linoleoyl lysophosphatidylcholine

proof_lines: inhibition of the ferric form of 12-lipoxygenase, free enzyme

proof_lines: inhibition of the ferric form of 12-lipoxygenase, substrate-bound form of enzyme

enzyme: arachidonate 12-lipoxygenase

substrate: 1-linoleoyl lysophosphatidylcholine


enzyme_display_name: NADPH-hemoprotein reductase

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: kidney spleen

enzyme: NADPH-hemoprotein reductase

substrate: NADPH


substrate_name: linoleic acid

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

substrate: linoleic acid


substrate_name: GDP-L-fucose

substrate: GDP-L-fucose


organism: Taeniopygia guttata

substrate_name: GAGADDDYAVTPGPDDDAGAG

proof_lines: pH and temperature not specified in the publication

substrate: GAGADDDYAVTPGPDDDAGAG


organism: Takifugu rubripes

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


substrate_name: deglycosylated swine trachea mucin

substrate: deglycosylated swine trachea mucin


smiles: CCCCCCC=CC=CCC=CCC=CCCCC(=O)O


enzyme_display_name: UniProt P9WP53

organism: Mycobacterium tuberculosis

substrate_name: O-phospho-L-serine

enzyme: UniProt P9WP53

substrate: O-phospho-L-serine


enzyme_display_name: nitrite reductase (NO-forming)

organism: uncultured bacterium

substrate_name: nitrite

enzyme: nitrite reductase (NO-forming)

substrate: nitrite


enzyme_display_name: trihydroxystilbene synthase

organism: Vitis vinifera

substrate_name: Unknown

proof_lines:
pH 4.0, 30°C, uncompetitive inhibition
pH 4.0, 30°C, competitive inhibition

enzyme: trihydroxystilbene synthase

substrate: Unknown


enzyme_display_name: sterol 3beta-glucosyltransferase

organism: Zea mays

enzyme: sterol 3beta-glucosyltransferase


enzyme_display_name: fatty-acid synthase system

organism: Mus musculus

substrate_name: palmitoyl-CoA

assay_conditions_summary: 298.15 K; cofactor CoA

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

enzyme: fatty-acid synthase system

substrate: palmitoyl-CoA


substrate_name: methylmalonyl-CoA

substrate: methylmalonyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


substrate_name: malonyl-CoA

mutation_type: substitution

proof_lines: didomain construct bearing mutation R606A, pH not specified in the publication, 25°C

substrate: malonyl-CoA


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


enzyme_display_name: nitrate reductase (NADH)

substrate_name: nitrate

enzyme: nitrate reductase (NADH)

substrate: nitrate


organism: Homo sapiens

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

substrate: NADPH


proof_lines: mutant enzyme A635G/R636S, at pH 7.5 and 25°C


enzyme_display_name: cytochrome-b5 reductase

substrate_name: NADH

enzyme: cytochrome-b5 reductase

substrate: NADH


substrate_name: ferricytochrome b5

substrate: ferricytochrome b5


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH

proof_lines: lysosome- and detergent-solubilized enzyme


assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM potassium phosphate; cofactor NADH

proof_lines: wild type enzyme, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


enzyme_display_name: NADPH:quinone reductase

smiles: CCCCCCC=CC=O

enzyme: NADPH:quinone reductase


smiles: CC(=O)C=C


smiles: CCC=CC=O


smiles: CC=CC(=O)C


smiles: CCCCCC=CC(=O)C


smiles: CCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCC(C=CC=O)O


substrate_name: propenal

smiles: C=CC=O

substrate: propenal


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


enzyme_display_name: UniProt P9WFF7

substrate_name: neryl diphosphate

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

enzyme: UniProt P9WFF7

substrate: neryl diphosphate


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: Dehydrodolichyl diphosphate synthase 1

organism: Arabidopsis thaliana

substrate_name: farnesyl diphosphate (FPP)

enzyme: Dehydrodolichyl diphosphate synthase 1

substrate: farnesyl diphosphate (FPP)


substrate_name: geranylgeranyl diphosphate (GGPP)

substrate: geranylgeranyl diphosphate (GGPP)


substrate_name: isopentenyl diphosphate (IPP)

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

substrate: isopentenyl diphosphate (IPP)


enzyme_display_name: UniProt P0AD57

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

enzyme: UniProt P0AD57


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


substrate_name: isopentenyl diphosphate

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: isopentenyl diphosphate


enzyme_display_name: UniProt B8XA40

organism: Solanum habrochaites

enzyme: UniProt B8XA40


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: with 0.08 mM 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.5 and 25°C

proof_lines: with 0.06 mM 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.5 and 25°C


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


enzyme_display_name: xanthine oxidase

organism: Bos taurus

enzyme: xanthine oxidase


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Sus scrofa


enzyme_display_name: demethylphylloquinol methyltransferase

substrate_name: menadione

enzyme: demethylphylloquinol methyltransferase

substrate: menadione


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

proof_lines: recombinant NAD(P)H:quinone acceptor oxidoreductase 2

enzyme: NAD(P)H dehydrogenase (quinone)


substrate_name: Methyl red

proof_lines: recombinant NAD(P)H:quinone acceptor oxidoreductase 1

substrate: Methyl red


organism: Gluconobacter oxydans


substrate_name: (2E,6E,10E)-geranylgeranyl diphosphate

substrate: (2E,6E,10E)-geranylgeranyl diphosphate


proof_lines:
pH 7.5, 37°C, mutant enzyme A197V
mutant A197V, pH 7.5, 37°C


substrate_name: NADPH

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: mutant N143A, pH 7.5, temperature not specified in the publication

substrate: NADPH


proof_lines: mutant N143L, pH 7.5, temperature not specified in the publication


proof_lines: mutant W139A, pH 7.5, temperature not specified in the publication


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


proof_lines: mutant W139F, pH 7.5, temperature not specified in the publication


proof_lines: mutant Y140F, pH 7.5, temperature not specified in the publication


proof_lines: mutant W139I, pH 7.5, temperature not specified in the publication


proof_lines:
pH 7.5, 37°C, mutant enzyme F190W
mutant F190W, pH 7.5, 37°C


proof_lines:
pH 7.5, 37°C, mutant enzyme F190A
mutant F190A, pH 7.5, 37°C


proof_lines:
pH 7.5, 37°C, wild-type enzyme
wild-type, pH 7.5, 37°C


proof_lines:
pH 7.5, 37°C, mutant enzyme A70V
mutant A70V, pH 7.5, 37°C


proof_lines:
pH 7.5, 37°C, mutant enzyme A70G
mutant A70G, pH 7.5, 37°C


enzyme_display_name: UniProt A0A1B0UHJ4

organism: Aspergillus terreus

enzyme: UniProt A0A1B0UHJ4


substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


substrate_name: (2E,6Z)-farnesyl diphosphate

substrate: (2E,6Z)-farnesyl diphosphate


enzyme_display_name: UniProt P29848

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: thiosulfate

enzyme: UniProt P29848

substrate: thiosulfate


substrate_name: O-acetyl-L-serine

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

substrate: O-acetyl-L-serine


organism: Thermotoga maritima


enzyme_display_name: all-trans-nonaprenyl diphosphate synthase [geranyl-diphosphate specific]

organism: Micrococcus luteus


substrate_name: farnesyl diphosphate

enzyme: all-trans-nonaprenyl diphosphate synthase [geranyl-diphosphate specific]

substrate: farnesyl diphosphate


substrate_name: farnesyl phosphosulfate

smiles: CCC(C)CCCC(C)CCCC(C)COS(=O)(=O)OP(=O)=O

substrate: farnesyl phosphosulfate


substrate_name: Geranyl phosphosulfate

smiles: CC(=CCCC(=CC(=O)OS(=O)(=O)OP(=O)=O)C)C

substrate: Geranyl phosphosulfate


enzyme_display_name: 4-O-dimethylallyl-L-tyrosine synthase

organism: Aspergillus niger

enzyme: 4-O-dimethylallyl-L-tyrosine synthase


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: D-tyrosine

proof_lines:
at pH 7.5 and 37°C
pH 7.5, 37°C

substrate: D-tyrosine


substrate_name: alpha-methyl-L-tyrosine

substrate: alpha-methyl-L-tyrosine


substrate_name: dimethylallyl diphosphate

proof_lines: with 3-iodo-L-tyrosine as cosubstrate, at pH 7.5 and 37°C

substrate: dimethylallyl diphosphate


substrate_name: geranylgeranyl diphosphate

protein_accession_database: NCBI Protein

sequence_source: GenBank AB006850.1 (protein_id BAA32241.1)

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

substrate: geranylgeranyl diphosphate


substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines:
pH 7.5, 37°C, mutant enzyme N193A
mutant N193A, pH 7.5, 37°C

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

organism: Trypanosoma cruzi


substrate_name: isopentenyl diphosphate

proof_lines: pH 7.4, 37°C, cosubstrate: farnesyl diphosphate

proof_lines: pH 7.4, 37°C, cosubstrate: geranyl diphosphate

proof_lines: pH 7.4, 37°C, cosubstrate: geranylgeranyl diphosphate

enzyme: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

substrate: isopentenyl diphosphate


organism: Paracoccus denitrificans


substrate_name: all-E-geranylgeranyl diphosphate

substrate: all-E-geranylgeranyl diphosphate


organism: Plenodomus lingam

substrate_name: (2Z)-3-chlorobut-2-en-1-yl diphosphate

proof_lines: cosubstrate 4-hydroxyphenylalanine, pH 7.5, 37°C

proof_lines: cosubstrate 4-aminophenylalanine, pH 7.5, 37°C

substrate: (2Z)-3-chlorobut-2-en-1-yl diphosphate


proof_lines: with L-tyrosine as cosubstrate, at pH 7.5 and 35°C


organism: Cereibacter sphaeroides

substrate_name: (2E,6E,10E)-geranylgeranyl diphosphate

substrate: (2E,6E,10E)-geranylgeranyl diphosphate


substrate_name: geranyl geranyl diphosphate

substrate: geranyl geranyl diphosphate


substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


enzyme_display_name: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]

organism: Thermococcus kodakarensis


enzyme: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]


proof_lines: 65°C, cosubstrate: dimethylallyl diphosphate


enzyme_display_name: geranylfarnesyl diphosphate synthase

enzyme: geranylfarnesyl diphosphate synthase


substrate_name: all-trans-farnesyl diphosphate

proof_lines: pH 7.7, 37°C, in presence of high molecular mass faction

proof_lines: pH 7.7, 37°C, in absence of high molecular mass fraction

substrate: all-trans-farnesyl diphosphate


organism: Solanum lycopersicum


column_label: Table 2 columns Km, kcat, and kcat/Km for At-SPS2-delta / FPP give 6.89, 3.77, and 0.547.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 3.77 s^-1; Km 0.00689 mM; kcat/Km 547 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row At-SPS2-delta FPP: Km 6.89 +/- 0.74 microM; kcat 3.77 +/- 0.15 s^-1; kcat/Km 0.547 s^-1 microM^-1.

row_label: At-SPS2-delta / FPP / 500 microM IPP

table_label: Table 2. Kinetic Parameters of At-SPS2 and At-SPS2-delta


column_label: Table 2 columns Km, kcat, and kcat/Km for At-SPS2-delta / GGPP give 0.843, 2.33, and 2.77.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 2.33 s^-1; Km 0.000843 mM; kcat/Km 2770 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row At-SPS2-delta GGPP: Km 0.843 +/- 0.157 microM; kcat 2.33 +/- 0.13 s^-1; kcat/Km 2.77 s^-1 microM^-1.

row_label: At-SPS2-delta / GGPP / 100 microM IPP


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

column_label: Table 2 separates At-SPS2-delta IPP and At-SPS2 IPP rows; the exported tuple combines metrics across those rows.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 2.83 s^-1; Km 0.182 mM; kcat/Km 15.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 At-SPS2-delta IPP with 20 microM FPP: Km 182 +/- 30 microM, kcat 2.83 +/- 0.21 s^-1, kcat/Km 0.0155 s^-1 microM^-1. Full-length At-SPS2 IPP with 20 microM FPP: Km 248 +/- 40 microM and no kcat.

row_label: At-SPS2-delta IPP / 20 microM FPP vs At-SPS2 IPP / 20 microM FPP


organism: Homo sapiens

substrate_name: Isopentenyl diphosphate; trans,trans-Farnesyl diphosphate

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


enzyme_display_name: adenosyl-chloride synthase

organism: Streptomyces noursei

substrate_name: S-adenosyl-L-methionine

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

enzyme: adenosyl-chloride synthase

substrate: S-adenosyl-L-methionine


enzyme_display_name: (2Z,6Z)-farnesyl diphosphate synthase

organism: Plasmodium falciparum

proof_lines: pH 7.5, 37°C, recombinant enzyme, with dimethylallyl diphosphate

enzyme: (2Z,6Z)-farnesyl diphosphate synthase


proof_lines: pH 7.5, 37°C, recombinant enzyme, with isopentenyl diphosphate


substrate_name: methylallyl diphosphate

substrate: methylallyl diphosphate


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Umezawaea tangerina


organism: uncultured bacterium

proof_lines:
isoform ClA2, at pH 7.8 and 37°C
isoform ClA1, at pH 7.8 and 37°C


proof_lines:
isoform ClA1, at pH 7.8 and 37°C
isoform ClA2, at pH 7.8 and 37°C


organism: Streptantibioticus cattleyicolor

proof_lines: 37°C, direct displacement reaction in the absence of L-methionine or S-adenosyl-L-methionine, pH not specified in the publication


substrate_name: L-o-tyrosine

substrate: L-o-tyrosine


enzyme_display_name: aspartate transaminase

organism: Bubalus bubalis

substrate_name: L-aspartate

enzyme: aspartate transaminase

substrate: L-aspartate


enzyme_display_name: UniProt P00509

organism: Escherichia coli

substrate_name: L-glutamate

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

enzyme: UniProt P00509

substrate: L-glutamate


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=8


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: L-Phe

assay_conditions_summary: pH 8

substrate: L-Phe


enzyme_display_name: UniProt Q4D080

enzyme: UniProt Q4D080


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-methionine

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

substrate: L-methionine


enzyme_display_name: Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase

organism: Comamonas testosteroni


enzyme_display_name: UniProt P52894

organism: Hordeum vulgare

substrate_name: pyruvate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=20°C, pH=8

enzyme: UniProt P52894

substrate: pyruvate


substrate_name: L-alanine

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

substrate: L-alanine


enzyme_display_name: UniProt H8WR05

organism: Variovorax paradoxus

substrate_name: (S)-beta-phenylalanine

enzyme: UniProt H8WR05

substrate: (S)-beta-phenylalanine


organism: Streptomyces sp.

verification_status: verified

column_label: Table 1. Steady-state kinetic parameters of Fur7; row 1,3-DHN / GPP; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.00013 normalized_unit=s^-1; Km normalized_value=0.32 normalized_unit=mM; kcat/Km normalized_value=0.00040625 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.13 +/- 0.05 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.32 +/- 0.02 raw_unit=mM; kcat/Km raw_value=0.41 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.00013/0.32 raw_unit=s^-1*mM^-1

row_label: 1,3-DHN / GPP

status: verified


column_label: Table 1. Steady-state kinetic parameters of Fur7; row compound 4 (2-methoxy-3-methylflaviolin) / GPP; Table 1 first row printed as Fur-P1; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.00066 normalized_unit=s^-1; Km normalized_value=0.054 normalized_unit=mM; kcat/Km normalized_value=0.0122222222222222 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.66 +/- 0.02 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.054 +/- 0.005 raw_unit=mM; kcat/Km raw_value=12 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.00066/0.054 raw_unit=s^-1*mM^-1


substrate_name: flaviolin

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / GPP; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.028 normalized_unit=s^-1; Km normalized_value=0.048 normalized_unit=mM; kcat/Km normalized_value=0.583333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=28 +/- 3 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.048 +/- 0.002 raw_unit=mM; kcat/Km raw_value=580 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.028/0.048 raw_unit=s^-1*mM^-1

row_label: Flaviolin 1 / GPP

substrate: flaviolin


substrate_name: geranyl diphosphate

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / GPP; column(s) Prenyl donor Km for GPP

raw_value_unit_evidence: Km raw_value=0.059 +/- 0.010 raw_unit=mM

source_databases_merged: brenda uniprot

substrate: geranyl diphosphate


substrate_name: dimethylallyl diphosphate

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / DMAPP; column(s) Prenyl donor Km for DMAPP

raw_value_unit_evidence: Km raw_value=0.72 +/- 0.06 raw_unit=mM

row_label: Flaviolin 1 / DMAPP

substrate: dimethylallyl diphosphate


organism: Solanum habrochaites

proof_lines:
pH 7.6, 30°C, mutant zFPS-M2
pH 7.6, 30°C, mutant zFPS-M10


substrate_name: isopentenyl diphosphate

proof_lines:
pH 7.6, 30°C, mutant zFPS-M10
pH 7.6, 30°C, mutant zFPS-M2

substrate: isopentenyl diphosphate


substrate_name: neryl diphosphate

substrate: neryl diphosphate


enzyme_display_name: Polyamine aminopropyltransferase

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: norspermidine (at pH 9 and 37 degrees Celsius)

smiles: C(CN)CNCCCN

assay_conditions_summary: pH 9

proof_lines: kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 de

enzyme: Polyamine aminopropyltransferase


substrate_name: S-adenosylmethioninamine (at pH 9 and 37 degrees Celsius)


substrate_name: spermidine (at pH 9 and 37 degrees Celsius)

smiles: C(CCNCCCN)CN


substrate_name: mitsubishine (at pH 9 and 37 degrees Celsius)

smiles: C(CN)CN(CCCN)CCCN


enzyme_display_name: Dehydrodolichyl diphosphate synthase complex subunit NUS1

column_label: Table 1 WT hcis-PT row lists Km IPP [uM]=11.1 (+/-1.3); converted to 0.0111 mM.

raw_value_unit_evidence: Km raw_value=11.1 (+/-1.3) raw_unit=uM for isopentenyl diphosphate

row_label: hcis-PT, WT

table_label: Table 1: Kinetic properties of purified hcis-PT and mutants


substrate_name: (2E,6E)-farnesyl diphosphate

column_label: Table 1 WT hcis-PT row lists Km FPP [uM]=0.68 (+/-0.14); converted to 0.00068 mM.

raw_value_unit_evidence: Km raw_value=0.68 (+/-0.14) raw_unit=uM for (2E,6E)-farnesyl diphosphate

enzyme: Dehydrodolichyl diphosphate synthase complex subunit NUS1

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: Dehydrodolichyl diphosphate synthase complex subunit DHDDS


enzyme: Dehydrodolichyl diphosphate synthase complex subunit DHDDS


enzyme_display_name: UniProt Q8N5Z0

substrate_name: oxaloacetate

enzyme: UniProt Q8N5Z0

substrate: oxaloacetate


substrate_name: hydroxyphenylpyruvate

substrate: hydroxyphenylpyruvate


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


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


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


substrate_name: glyoxylate

substrate: glyoxylate


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


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


substrate_name: Mercaptopyruvate

substrate: Mercaptopyruvate


enzyme_display_name: UniProt Q16773

enzyme: UniProt Q16773


substrate_name: L-kynurenine

substrate: L-kynurenine


substrate_name: L-cysteine

substrate: L-cysteine


enzyme_display_name: ornithine aminotransferase

organism: Aspergillus nidulans

enzyme: ornithine aminotransferase


substrate_name: L-ornithine

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

substrate: L-ornithine


enzyme_display_name: UniProt P04181

proof_lines:
Raw SKiD Env: Temp=15°C, pH=8
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P04181


enzyme_display_name: UniProt S8EY38

organism: Toxoplasma gondii

enzyme: UniProt S8EY38


substrate_name: acetylornithine

substrate: acetylornithine


enzyme_display_name: Geranylfarnesyl diphosphate synthase, chloroplastic

organism: Leucosceptrum canum

substrate_name: dimethylallyl diphosphate (in the presence of isopentenyl diphosphate)

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

proof_lines: kcat is 16.9x10(-6) sec(-1) with dimethylallyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 8.2x10(-6) sec(-1) with isopentenyl diphosphate as substrate (in the presence of geranylgeranyl


substrate_name: geranyl diphosphate (in the presence of isopentenyl diphosphate)

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

enzyme: Geranylfarnesyl diphosphate synthase, chloroplastic


substrate_name: farnesyl diphosphate (in the presence of isopentenyl diphosphate)


enzyme_display_name: 4-hydroxybenzoate geranyltransferase

organism: Lithospermum erythrorhizon

substrate_name: geranyl diphosphate

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

enzyme: 4-hydroxybenzoate geranyltransferase


enzyme_display_name: Solanesyl diphosphate synthase 1, chloroplastic

organism: Arabidopsis thaliana

substrate_name: farnesyl diphosphate (in the presence of 500 uM of isopentenyl diphosphate)

proof_lines: kcat is 29.7 sec(-1) with farnesyl diphosphate as substrate (in the presence of 500 uM of isopentenyl diphosphate). kcat is 21.0 sec(-1) with geranylgeranyl diphosphate as substrate (in the presence of 100 uM of isopentenyl diphosphate). kc


substrate_name: geranylgeranyl diphosphate (in the presence of 100 uM of isopentenyl diphosphate)

enzyme: Solanesyl diphosphate synthase 1, chloroplastic


substrate_name: isopentenyl diphosphate (in the presence of 20 uM of farnesyl diphosphate)

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


enzyme_display_name: flaviolin linalyltransferase

organism: Streptomyces virginiae

substrate_name: flaviolin

proof_lines: kcat is 0.013 min(-1) for flaviolin. kcat is 0.14 min(-1) for 4-hydroxybenzoate.

enzyme: flaviolin linalyltransferase


column_label: Primary prose labels GPP Km 2.1 uM under the flaviolin condition.

raw_value_unit_evidence: GPP Km 2.1 uM using flaviolin 0.25 mM

row_label: GPP with flaviolin as aromatic substrate

table_label: Section 3.4 Biochemical properties of Fnq26


organism: Streptomyces anulatus

substrate_name: dimethylallyl diphosphate

column_label: PubMed abstract prose, metric label Km, substrate dimethylallyl diphosphate, raw value 116 uM.

normalized_value_unit_evidence: 116 uM = 0.116 mM, matching the expected export Km 0.116 mM.

raw_value_unit_evidence: PubMed abstract reports the Km value for dimethylallyl diphosphate as 116 uM.

row_label: PpzP / dimethylallyl diphosphate

table_label: PubMed abstract prose for PMID 19339241


enzyme_display_name: UniProt Q84II6

organism: Janthinobacterium sp. J3

enzyme: UniProt Q84II6


enzyme_display_name: UniProt Q8RTL4

organism: Comamonas sp.

substrate_name: nitrobenzene

enzyme: UniProt Q8RTL4

substrate: nitrobenzene


enzyme_display_name: 2,4-dinitrotoluene dioxygenase

organism: Burkholderia sp.

smiles: O=O

enzyme: 2,4-dinitrotoluene dioxygenase


enzyme_display_name: UniProt Q71RI9

organism: Mus musculus

substrate_name: L-glutamine

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

enzyme: UniProt Q71RI9

substrate: L-glutamine


enzyme_display_name: UniProt P17169

organism: Escherichia coli

substrate_name: D-fructose 6-phosphate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.2
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.5

enzyme: UniProt P17169

substrate: D-fructose 6-phosphate


substrate_name: L-gamma-glutamyl-p-nitroanilide

substrate: L-gamma-glutamyl-p-nitroanilide


enzyme_display_name: UniProt P80147

organism: Sus scrofa

substrate_name: (R,S)-4-amino-3-fluorobutanoic acid

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

enzyme: UniProt P80147

substrate: (R,S)-4-amino-3-fluorobutanoic acid


substrate_name: gamma-aminobutanoic acid

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

substrate: gamma-aminobutanoic acid


substrate_name: L-Aspartate

substrate: L-Aspartate


enzyme_display_name: 4-aminobutyrate transaminase

substrate_name: 4-Aminobutanoate; 2-Oxoglutarate

enzyme: 4-aminobutyrate transaminase

substrate: 4-Aminobutanoate; 2-Oxoglutarate


smiles: NCCCC(=O)O


organism: Malus domestica


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E211S to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I50Q/G295Y to reconstruct the assayed variant sequence.

column_label: Table 2; row I50Q/G295Y; columns kcat, kcat/KGABA, and KGABA; raw kcat=0.028 +/- 0.001 s^-1, kcat/KGABA=5.9 +/- 0.3 M^-1 s^-1, KGABA=4.7 +/- 0.2 mM; normalized kcat=0.028 s^-1, Km=4.7 mM, kcat/Km=0.0059 s^-1*mM^-1.

normalized_value_unit_evidence: kcat=0.028 s^-1; Km=4.7 mM; kcat/Km=0.0059 s^-1*mM^-1 from printed kcat/KGABA

row_label: I50Q/G295Y / GABA (4-aminobutanoate)

table_label: Table 2. GABA/R-ketoglutarate transamination analysis of wild-type GABA-AT and its mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V241A to reconstruct the assayed variant sequence.

column_label: Table 2; row V241A; columns kcat, kcat/KGABA, and KGABA; raw kcat=1.93 +/- 0.08 s^-1, kcat/KGABA=64 +/- 6 M^-1 s^-1, KGABA=30 +/- 2 mM; normalized kcat=1.93 s^-1, Km=30.0 mM, kcat/Km=0.064 s^-1*mM^-1.

normalized_value_unit_evidence: kcat=1.93 s^-1; Km=30.0 mM; kcat/Km=0.064 s^-1*mM^-1 from printed kcat/KGABA

row_label: V241A / GABA (4-aminobutanoate)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E211S/I50H/V80T to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat=0.106 s^-1; Km=146.0 mM; kcat/Km=0.00073 s^-1*mM^-1 from printed kcat/KGABA

row_label: E211S/I50H/V80T / GABA (4-aminobutanoate)


column_label: Table 2; row wild type; columns kcat, kcat/KGABA, and KGABA; raw kcat=47.4 +/- 1.0 s^-1, kcat/KGABA=8172 +/- 590 M^-1 s^-1, KGABA=5.8 +/- 0.4 mM; normalized kcat=47.4 s^-1, Km=5.8 mM, kcat/Km=8.172 s^-1*mM^-1.

normalized_value_unit_evidence: kcat=47.4 s^-1; Km=5.8 mM; kcat/Km=8.172 s^-1*mM^-1 from printed kcat/KGABA

row_label: wild type / GABA (4-aminobutanoate)


substrate_name: pyruvate

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

substrate: pyruvate


substrate_name: glyoxylate

smiles: O=CC(=O)O


organism: Rattus norvegicus

substrate_name: L-Glutamine; D-Fructose 6-phosphate

substrate: L-Glutamine; D-Fructose 6-phosphate


organism: Corynebacterium glutamicum


substrate_name: 2-Oxoglutarate; 4-Aminobutanoate

substrate: 2-Oxoglutarate; 4-Aminobutanoate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I50Q to reconstruct the assayed variant sequence.

column_label: Table 2; row I50Q; columns kcat, kcat/KGABA, and KGABA; raw kcat=13.5 +/- 0.3 s^-1, kcat/KGABA=199 +/- 18 M^-1 s^-1, KGABA=68 +/- 6 mM; normalized kcat=13.5 s^-1, Km=68.0 mM, kcat/Km=0.199 s^-1*mM^-1.

normalized_value_unit_evidence: kcat=13.5 s^-1; Km=68.0 mM; kcat/Km=0.199 s^-1*mM^-1 from printed kcat/KGABA

row_label: I50Q / GABA (4-aminobutanoate)


enzyme_display_name: nitroarene dioxygenase

organism: Acidovorax sp.

enzyme: nitroarene dioxygenase


enzyme_display_name: glutamine---pyruvate transaminase

substrate_name: L-Glutamine; Glyoxylate

enzyme: glutamine---pyruvate transaminase

substrate: L-Glutamine; Glyoxylate


enzyme_display_name: glutamine-pyruvate transaminase

substrate_name: L-methionine

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

enzyme: glutamine-pyruvate transaminase

substrate: L-methionine


substrate_name: L-methionine (SR)-sulfoxide

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

substrate: L-methionine (SR)-sulfoxide


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


substrate: glyoxylate


organism: Pseudomonas aeruginosa


substrate_name: putrescine

smiles: C(CCN)CN

substrate: putrescine


substrate_name: L-ornithine

substrate: L-ornithine


proof_lines: with glyoxylate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C

proof_lines: with pyruvate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C


proof_lines: in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C


proof_lines: with L-alanine as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C


substrate_name: L-alanine

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

proof_lines: with 4-oxobutanoate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C

substrate: L-alanine


substrate_name: Unknown

substrate: Unknown


organism: Nicotiana tabacum


enzyme_display_name: carbazole 1,9a-dioxygenase

enzyme: carbazole 1,9a-dioxygenase


organism: Schistocerca gregaria


enzyme_display_name: D-amino-acid transaminase

organism: Bradyrhizobium japonicum

enzyme: D-amino-acid transaminase


substrate_name: D-alanine

substrate: D-alanine


organism: Lathyrus oleraceus


substrate_name: Naphthalene

substrate: Naphthalene


enzyme_display_name: steroid 9alpha-monooxygenase

organism: Mycolicibacterium fortuitum

substrate_name: NADH

enzyme: steroid 9alpha-monooxygenase

substrate: NADH


enzyme_display_name: salicylate 1-monooxygenase

organism: Solanum lycopersicum

substrate_name: salicylate

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

enzyme: salicylate 1-monooxygenase

substrate: salicylate


substrate_name: L-glutamine

substrate: L-glutamine


enzyme_display_name: beta-alanine-pyruvate transaminase

organism: Bacillus cereus

substrate_name: beta-Alanine

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

enzyme: beta-alanine-pyruvate transaminase

substrate: beta-Alanine


organism: Mycolicibacterium smegmatis


organism: Streptomyces sp.

table_label: Table 1. Steady-state kinetic parameters of Fur7


row_label: compound 4 (2-methoxy-3-methylflaviolin) / GPP; Table 1 first row printed as Fur-P1


substrate_name: flaviolin

substrate: flaviolin


substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


organism: Bacillus sp. (in: firmicutes)

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y31A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; cofactor NADH

column_label: PMID 8977094 PDF text lines 141-153; Table 1 row Y31A, kcat column, value 0.5 s^-1.

raw_value_unit_evidence: Table 1 row Y31A, column kcat: 0.5 s^-1.

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E32A to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32A, kcat column, value 1.3 s^-1.

raw_value_unit_evidence: Table 2 row E32A, column kcat: 1.3 s^-1.

table_label: Table 2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E32Q to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32Q, kcat column, value 13.4 s^-1.

raw_value_unit_evidence: Table 2 row E32Q, column kcat: 13.4 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K35A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 141-153; Table 1 row K35A, kcat column, value 84.3 s^-1.

raw_value_unit_evidence: Table 1 row K35A, column kcat: 84.3 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E32D to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32D, kcat column 85.6 s^-1, Km D-alanine column 1.2 mM, kcat/Km D-alanine column 6.8 x 10^4 M^-1 s^-1.

raw_value_unit_evidence: Table 2 row E32D: kcat 85.6 s^-1; Km D-alanine 1.2 mM; kcat/Km D-alanine 6.8 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V33A to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 141-153; Table 1 row V33A, kcat column, value 145.1 s^-1.

raw_value_unit_evidence: Table 1 row V33A, column kcat: 145.1 s^-1.


column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32Q, Km alpha-KG column, value 1.4 mM.

normalized_value_unit_evidence: km=1.4 mM

raw_value_unit_evidence: Table 2 row E32Q, column Km alpha-KG: 1.4 mM.


column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32A, Km alpha-KG column, value 1.8 mM.

normalized_value_unit_evidence: km=1.8 mM

raw_value_unit_evidence: Table 2 row E32A, column Km alpha-KG: 1.8 mM.


column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32D, Km alpha-KG column, value 2.1 mM.

normalized_value_unit_evidence: km=2.1 mM

raw_value_unit_evidence: Table 2 row E32D, column Km alpha-KG: 2.1 mM.


column_label: PMID 8977094 PDF text lines 141-153; Table 1 row Y31A, Km alpha-ketoglutarate column, value 10.1 mM.

raw_value_unit_evidence: Table 1 row Y31A, column Km alpha-ketoglutarate: 10.1 mM.


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

column_label: PMID 8977094 PDF text lines 141-153; Table 1 row V33A, Km alpha-ketoisovalerate column, value 15.5 mM.

raw_value_unit_evidence: Table 1 row V33A, column Km alpha-ketoisovalerate: 15.5 mM.


column_label: PMID 8977094 PDF text lines 141-153; Table 1 row K35A, Km alpha-ketoisovalerate column, value 32.2 mM.

raw_value_unit_evidence: Table 1 row K35A, column Km alpha-ketoisovalerate: 32.2 mM.


column_label: PMID 8977094 PDF text lines 141-153; Table 1 row K35A, Km alpha-ketoglutarate column, value 35.6 mM.

raw_value_unit_evidence: Table 1 row K35A, column Km alpha-ketoglutarate: 35.6 mM.


enzyme_display_name: Nonaprenyl diphosphate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: IPP

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

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

proof_lines: kcat is 0.3 min(-1) with GPP as substrate. kcat is 0.7 min(-1) with FPP as substrate. kcat is 0.17 min(-1) with DMAPP as substrate.

enzyme: Nonaprenyl diphosphate synthase

substrate: IPP


substrate_name: GPP

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

assay_conditions_summary: pH 7; buffer 50 mM sodium phosphate pH 7

column_label: Table 1 row Rv0562; GPP KM column; value 2.3 +/- 0.8 uM.

normalized_value_unit_evidence: 2.3 uM normalizes to 0.0023 mM.

raw_value_unit_evidence: Table 1 row Rv0562 reports GPP KM 2.3 +/- 0.8 uM.

row_label: Rv0562 / GPP

table_label: Table 1: Kinetic analysis of confirmed GGPP synthases

substrate: GPP


substrate_name: FPP

column_label: Table 1 row Rv0562; FPP KM column; value 11 +/- 3 uM.

normalized_value_unit_evidence: 11 uM normalizes to 0.011 mM.

raw_value_unit_evidence: Table 1 row Rv0562 reports FPP KM 11 +/- 3 uM.

row_label: Rv0562 / FPP

substrate: FPP


substrate_name: DMAPP

column_label: Table 1 row Rv0562; DMAPP KM column; value 5 +/- 2 uM.

normalized_value_unit_evidence: 5 uM normalizes to 0.005 mM.

raw_value_unit_evidence: Table 1 row Rv0562 reports DMAPP KM 5 +/- 2 uM.

row_label: Rv0562 / DMAPP

substrate: DMAPP


enzyme_display_name: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

organism: Arabidopsis thaliana

substrate_name: geranylgeranyl diphosphate

column_label: Table 2 columns Enzyme, Substrate, Counter-substrate, Km list At-SPS2 / GGPP / 100 microM IPP / 0.565 +/- 0.178.

normalized_value_unit_evidence: Paper-normalized metrics: Km 0.000565 mM.

raw_value_unit_evidence: Table 2 row At-SPS2 GGPP: Km 0.565 +/- 0.178 microM; kcat not determined.

row_label: At-SPS2 / GGPP / 100 microM IPP

substrate: geranylgeranyl diphosphate


substrate_name: farnesyl diphosphate

column_label: Table 2 columns Enzyme, Substrate, Counter-substrate, Km list At-SPS2 / FPP / 500 microM IPP / 5.12 +/- 0.57.

normalized_value_unit_evidence: Paper-normalized metrics: Km 0.00512 mM.

raw_value_unit_evidence: Table 2 row At-SPS2 FPP: Km 5.12 +/- 0.57 microM; kcat not determined.

row_label: At-SPS2 / FPP / 500 microM IPP

enzyme: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

substrate: farnesyl diphosphate


substrate_name: isopentenyl diphosphate

proof_lines: pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate, His6-tagged At-SPS2 fusion protein

proof_lines: pH 8.0, 30°C, cosubstrate: farnesyl diphosphate, His6-tagged At-SPS2 fusion protein

proof_lines: kcat is 3.77 sec(-1) with farnesyl diphosphate as substrate (in the presence of 500 uM of isopentenyl diphosphate). kcat is 2.33 sec(-1) with geranylgeranyl diphosphate as substrate (in the presence of 100 uM of isopentenyl diphosphate). kc

substrate: isopentenyl diphosphate


organism: Metapseudomonas resinovorans

proof_lines: CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

organism: Homo sapiens

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

proof_lines: 3.6 kcat is sec(-1) with L-glutamine as substrate (PubMed:32019926, PubMed:35229715). 1.7 kcat is sec(-1) with D-fructose 6-phosphate as substrate (PubMed:32019926, PubMed:35229715).


substrate_name: D-fructose 6-phosphate

enzyme: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

substrate: D-fructose 6-phosphate


enzyme_display_name: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2

proof_lines: 3.7 kcat is sec(-1) with L-glutamine as substrate (PubMed:35229715). 1.8 kcat is sec(-1) with D-fructose 6-phosphate as substrate (PubMed:35229715).


enzyme: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2


organism: Pseudomonas sp.


assay_conditions_summary: cofactor NADH


enzyme_display_name: Polyamine aminopropyltransferase

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: agmatine (at pH 9 and 37 degrees Celsius)

smiles: C(CCN=C(N)N)CN

proof_lines: kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 de

enzyme: Polyamine aminopropyltransferase


enzyme_display_name: Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase

substrate_name: D-alanine

column_label: PMC Supplementary Figure 1 caption reports pyruvate-formation kinetic parameters with KM = 7.3 +/- 1.06 mM.

raw_value_unit_evidence: Km raw_value=7.3 +/- 1.06 raw_unit=mM for pyruvate formation from the D-Ala-side DAAT assay

row_label: Supplementary Figure 1 panel B pyruvate formation / Rv0812 DAAT activity

table_label: PMID 33950161 PMC Supplementary Figure 1 caption

substrate: D-alanine


substrate_name: D-glutamate

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

column_label: PMC Supplementary Figure 1 caption reports D-Glu consumption kinetic parameters with KM = 0.24 +/- 0.05 mM.

raw_value_unit_evidence: Km raw_value=0.24 +/- 0.05 raw_unit=mM for D-Glu consumption

row_label: Supplementary Figure 1 panel C D-Glu consumption / Rv0812 DAAT activity

enzyme: Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase

substrate: D-glutamate


enzyme_display_name: Fluorinase

organism: Nocardia brasiliensis (strain ATCC 700358 / HUJEG-1)

substrate_name: S-adenosyl-L-methionine

enzyme: Fluorinase

substrate: S-adenosyl-L-methionine


enzyme_display_name: (2Z,6Z)-farnesyl diphosphate synthase

organism: Solanum habrochaites

proof_lines: pH 7.8, 30°C, 0.035 mM isopentenyl diphosphate

proof_lines: pH 7.8, 30°C, 0.18 mM isopentenyl diphosphate

proof_lines: pH 7.8, 30°C, 0.21 mM isopentenyl diphosphate

source_databases_merged: brenda skid uniprot

enzyme: (2Z,6Z)-farnesyl diphosphate synthase


organism: Streptomyces sp

substrate_name: S-adenosyl-L-methionine (for fluorinase activity)

proof_lines: kcat is 0.262 min(-1) for fluorinase activity (PubMed:24449539). kcat is 0.22 min(-1) for fluorinase activity (PubMed:27739177). kcat is 0.017 min(-1) for SAM hydrolase activity (PubMed:36996195). kcat is 0.008 min(-1) for chlorinase activi


organism: Achromobacter denitrificans

substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: UniProt P22256

organism: Escherichia coli

proof_lines: kcat is 47.4 sec(-1) with 4-aminobutanoate as substrate (at 25 degrees Celsius and pH 7.8).

enzyme: UniProt P22256


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


enzyme_display_name: deoxyhypusine monooxygenase

substrate_name: 6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A

enzyme: deoxyhypusine monooxygenase


organism: Streptomyces sp. (strain KO-3988)


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

substrate_name: sym-nor-spermidine (at 78 degrees Celsius and at pH 7.5)

smiles: C(CN)CNCCCN


enzyme_display_name: norspermine synthase

organism: Thermus thermophilus

enzyme: norspermine synthase


enzyme_display_name: Decaprenyl diphosphate synthase

substrate_name: NPP (at pH 7.9 and 37 degrees Celsius)

column_label: Official PMC HTML Table 2 row NPP column Km=29 uM.

normalized_value_unit_evidence: Km 0.029 mM for NPP; this is the only required metric for the row.

raw_value_unit_evidence: Km 29 uM for NPP.

row_label: NPP

table_label: Table 2. Kinetic parameters for Rv2361c.

enzyme: Decaprenyl diphosphate synthase

substrate: NPP (at pH 7.9 and 37 degrees Celsius)


enzyme_display_name: 4-aminobutyrate aminotransferase GabT

organism: Escherichia coli (strain K12)

substrate_name: 5-aminopentanoate (measured for a coupled GabT/GabD reaction)

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

enzyme: 4-aminobutyrate aminotransferase GabT


enzyme_display_name: 4-hydroxybenzoate geranyltransferase

organism: Lithospermum erythrorhizon

substrate_name: Geranyl diphosphate; 4-Hydroxybenzoate

enzyme: 4-hydroxybenzoate geranyltransferase

substrate: Geranyl diphosphate; 4-Hydroxybenzoate


substrate_name: 4-Hydroxybenzoate; Geranyl diphosphate

substrate: 4-Hydroxybenzoate; Geranyl diphosphate


enzyme_display_name: adenosyl-chloride synthase

organism: Salinispora tropica

substrate_name: Cl-; S-Adenosyl-L-methionine

enzyme: adenosyl-chloride synthase

substrate: Cl-; S-Adenosyl-L-methionine


organism: Bos taurus

substrate_name: D-Fructose 6-phosphate; L-Glutamine

substrate: D-Fructose 6-phosphate; L-Glutamine


substrate_name: L-Glutamine; D-Fructose 6-phosphate

substrate: L-Glutamine; D-Fructose 6-phosphate


enzyme_display_name: 4-aminobutyrate transaminase

organism: Sus scrofa

substrate_name: 4-Aminobutanoate; 2-Oxoglutarate

enzyme: 4-aminobutyrate transaminase

substrate: 4-Aminobutanoate; 2-Oxoglutarate


enzyme_display_name: D-amino-acid transaminase

organism: Arabidopsis thaliana

substrate_name: D-Alanine; 2-Oxoglutarate

enzyme: D-amino-acid transaminase

substrate: D-Alanine; 2-Oxoglutarate


organism: Bacillus sp.

substrate_name: 2-Oxoglutarate; D-Alanine

substrate: 2-Oxoglutarate; D-Alanine


organism: Lysinibacillus sphaericus


organism: Rattus norvegicus


substrate_name: N-succinyldiaminopimelate

substrate: N-succinyldiaminopimelate


enzyme_display_name: Alanine--glyoxylate aminotransferase 2, mitochondrial

substrate_name: D-beta-aminoisobutyrate

substrate: D-beta-aminoisobutyrate


substrate_name: 2-Oxoglutarate; D-Glutamate

substrate: 2-Oxoglutarate; D-Glutamate


organism: Homo sapiens

smiles: NCCCC(=O)O


substrate_name: 2-Oxoglutarate; 4-Aminobutanoate

substrate: 2-Oxoglutarate; 4-Aminobutanoate


enzyme_display_name: geranylfarnesyl diphosphate synthase

organism: Leucosceptrum canum

substrate_name: isopentenyl diphosphate

proof_lines: kcat is 16.9x10(-6) sec(-1) with dimethylallyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 8.2x10(-6) sec(-1) with isopentenyl diphosphate as substrate (in the presence of geranylgeranyl

enzyme: geranylfarnesyl diphosphate synthase

substrate: isopentenyl diphosphate


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


substrate_name: Isopentenyl diphosphate

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

substrate: Isopentenyl diphosphate


substrate_name: trans,trans-Farnesyl diphosphate; Isopentenyl diphosphate

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


organism: Plasmodium falciparum

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: (2Z,6Z)-farnesyl diphosphate synthase, chloroplastic

organism: Solanum habrochaites

substrate_name: nerylpyrophosphate in the presence of 180 uM isopentenyl diphosphate

proof_lines: isopentenyl diphosphate acts as activator of its own catalysis.


enzyme_display_name: 4,4'-diapophytoene synthase

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

enzyme: 4,4'-diapophytoene synthase


organism: Vigna radiata var. radiata


enzyme_display_name: beta-alanine-pyruvate transaminase

organism: Achromobacter denitrificans

substrate_name: L-beta-amino-n-butyric acid

enzyme: beta-alanine-pyruvate transaminase

substrate: L-beta-amino-n-butyric acid


enzyme_display_name: 4-aminobutyrate aminotransferase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: 4-aminobutyrate aminotransferase


enzyme_display_name: Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: aminodeoxychorismate

proof_lines: kcat is 1.9 sec(-1) with aminodeoxychorismate as substrate. kcat is 1.46 sec(-1) with D-alanine as substrate. kcat is 0.25 sec(-1) with D-glutamate as substrate.

substrate: aminodeoxychorismate


organism: Salinispora tropica CNB-440

substrate_name: Iodide

assay_conditions_summary: pH 7.9; 310.15 K; buffer 50 mM phosphate

column_label: Official PMC Table 1 row I- (Forward reaction): kcat 0.3 +/- 0.1 min^-1 | Km 260 +/- 20 mM | kcat/Km 0.00115 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.005 normalized_unit=s^-1; Km normalized_value=260.0 normalized_unit=mM; kcat/Km ratio normalized_value=0.00001923076923076923 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=0.000019166666666666667 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Forward reaction row I-: kcat raw_value=0.3 +/- 0.1 raw_unit=min^-1; Km raw_value=260 +/- 20 raw_unit=mM; kcat/Km raw_value=0.00115 raw_unit=mM^-1 min^-1.

row_label: I-

table_label: Table 1. Apparent kinetic constants of SalL wild type and relative activity of point mutants

substrate: Iodide


substrate_name: bromide

column_label: Official PMC Table 1 row Br- (Forward reaction): kcat 0.8 +/- 0.1 min^-1 | Km 150 +/- 15 mM | kcat/Km 0.0053 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.013333333333333334 normalized_unit=s^-1; Km normalized_value=150.0 normalized_unit=mM; kcat/Km ratio normalized_value=0.00008888888888888889 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=0.00008833333333333333 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Forward reaction row Br-: kcat raw_value=0.8 +/- 0.1 raw_unit=min^-1; Km raw_value=150 +/- 15 raw_unit=mM; kcat/Km raw_value=0.0053 raw_unit=mM^-1 min^-1.

row_label: Br-

substrate: bromide


substrate_name: S-adenosyl-L-methionine

column_label: Official PMC Table 1 row SAM (Forward reaction): kcat 0.9 +/- 0.1 min^-1 | Km (1 +/- 0.2) x 10^-3 mM | kcat/Km 900 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.015 normalized_unit=s^-1; Km normalized_value=0.001 normalized_unit=mM; kcat/Km ratio normalized_value=15.0 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=15.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Forward reaction row SAM: kcat raw_value=0.9 +/- 0.1 raw_unit=min^-1; Km raw_value=(1 +/- 0.2) x 10^-3 raw_unit=mM; kcat/Km raw_value=900 raw_unit=mM^-1 min^-1.

row_label: SAM

substrate: S-adenosyl-L-methionine


substrate_name: chloride

column_label: Official PMC Table 1 row Cl- (Forward reaction): kcat 0.9 +/- 0.1 min^-1 | Km 45 +/- 5 mM | kcat/Km 0.02 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.015 normalized_unit=s^-1; Km normalized_value=45.0 normalized_unit=mM; kcat/Km ratio normalized_value=0.0003333333333333333 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=0.0003333333333333333 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Forward reaction row Cl-: kcat raw_value=0.9 +/- 0.1 raw_unit=min^-1; Km raw_value=45 +/- 5 raw_unit=mM; kcat/Km raw_value=0.02 raw_unit=mM^-1 min^-1.

row_label: Cl-

substrate: chloride


substrate_name: L-methionine

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

column_label: Official PMC Table 1 row L-Met (Reverse reaction): kcat 12 +/- 1 min^-1 | Km 2.6 +/- 0.2 mM | kcat/Km 4.6 mM^-1 min^-1.

raw_value_unit_evidence: Table 1 Reverse reaction row L-Met: kcat raw_value=12 +/- 1 raw_unit=min^-1; Km raw_value=2.6 +/- 0.2 raw_unit=mM; kcat/Km raw_value=4.6 raw_unit=mM^-1 min^-1.

row_label: L-Met

source_databases_merged: brenda skid

substrate: L-methionine


column_label: Official PMC Table 1 row 5'-ClDA (Reverse reaction): kcat 12 +/- 1 min^-1 | Km (2 +/- 1) x 10^-4 mM | kcat/Km 60,000 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.2 normalized_unit=s^-1; Km normalized_value=0.0002 normalized_unit=mM; kcat/Km ratio normalized_value=1000.0 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=1000.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Reverse reaction row 5'-ClDA: kcat raw_value=12 +/- 1 raw_unit=min^-1; Km raw_value=(2 +/- 1) x 10^-4 raw_unit=mM; kcat/Km raw_value=60,000 raw_unit=mM^-1 min^-1.


proof_lines: in 50 mM phosphate buffer (pH 7.9) at 37°C


enzyme_display_name: UniProt P9WNP7

organism: Mycobacterium tuberculosis

substrate_name: NADH

enzyme: UniProt P9WNP7

substrate: NADH


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase

enzyme: 3-hydroxyacyl-CoA dehydrogenase


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G116F to reconstruct the assayed variant sequence.


organism: Caenorhabditis elegans

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R204A/Y209A to reconstruct the assayed variant sequence.


organism: Metallosphaera sedula


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


enzyme_display_name: glyoxylate reductase

organism: Arabidopsis thaliana

substrate_name: glyoxylate

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

assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADPH

proof_lines: mutant T335A, cosubstrate NADPH, pH 6.2, 25°C

proof_lines: mutant T335A, cosubstrate NADH, pH 6.2, 25°C

enzyme: glyoxylate reductase

substrate: glyoxylate


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

proof_lines: wild-type, cosubstrate NADPH, pH 6.2, 25°C

proof_lines: wild-type, cosubstrate NADH, pH 6.2, 25°C


substrate_name: NADPH

substrate: NADPH


proof_lines: mutant T335D, cosubstrate NADPH, pH 6.2, 25°C

proof_lines: mutant T335D, cosubstrate NADH, pH 6.2, 25°C


assay_conditions_summary: cofactor CoA

proof_lines: mitochondrial enzyme, oxidation of (S)-3-hydroxyoctanoyl-CoA


proof_lines: mitochondrial enzyme, oxidation of (S)-3-hydroxyhexanoyl-CoA


assay_conditions_summary: cofactor NAD+


proof_lines: mitochondrial enzyme, oxidation of (S)-3-hydroxybutyryl-CoA


proof_lines: mitochondrial enzyme, oxidation of (S)-3-hydroxydecanoyl-CoA


assay_conditions_summary: cofactor NADPH


substrate_name: acetoacetyl-pantetheine

substrate: acetoacetyl-pantetheine


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Mycolicibacterium smegmatis


substrate_name: acetoacetyl-N-acetyl-cysteamine

substrate: acetoacetyl-N-acetyl-cysteamine


enzyme_display_name: 4-O-dimethylallyl-L-tyrosine synthase

organism: Leptosphaeria maculans

substrate_name: cyclohex-1-en-1-ylmethyl diphosphate

normalized_value_unit_evidence: kcat normalized_value=0.0055 normalized_unit=s^-1; Km normalized_value=0.13 normalized_unit=mM; kcat/Km normalized_value=0.04166666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.33 raw_unit=min^-1; Km raw_value=0.13 raw_unit=mM; kcat/Km raw_value=2.5 raw_unit=mM^-1*min^-1

row_label: A4 / cyclohex-1-en-1-ylmethyl diphosphate

table_label: Table 1. Kinetic parameters for SirD with L-Tyr and alkyl-PP analogues

enzyme: 4-O-dimethylallyl-L-tyrosine synthase

substrate: cyclohex-1-en-1-ylmethyl diphosphate


substrate_name: dimethylallyl diphosphate

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

normalized_value_unit_evidence: kcat normalized_value=0.6833333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.23 normalized_unit=mM; kcat/Km normalized_value=2.966666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=41 raw_unit=min^-1; Km raw_value=0.23 raw_unit=mM; kcat/Km raw_value=178 raw_unit=mM^-1*min^-1

row_label: A1 / dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


substrate_name: 2-cyclohexylideneethyl diphosphate

normalized_value_unit_evidence: kcat normalized_value=0.05833333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.21 normalized_unit=mM; kcat/Km normalized_value=0.2666666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3.5 raw_unit=min^-1; Km raw_value=0.21 raw_unit=mM; kcat/Km raw_value=16 raw_unit=mM^-1*min^-1

row_label: A5 / 2-cyclohexylideneethyl diphosphate

substrate: 2-cyclohexylideneethyl diphosphate


normalized_value_unit_evidence: kcat normalized_value=0.003666666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.17 normalized_unit=mM; kcat/Km normalized_value=0.02166666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.22 raw_unit=min^-1; Km raw_value=0.17 raw_unit=mM; kcat/Km raw_value=1.3 raw_unit=mM^-1*min^-1

row_label: A19 / (2E)-2-methylpenta-2,4-dien-1-yl diphosphate


substrate_name: (2E)-3-methylpent-2-en-1-yl diphosphate

smiles: CC/C(C)=C/COP(=O)(O)OP(=O)(O)O

column_label: Table 1 row A2; raw cells kcat 18 min^-1, KM 0.2 mM, kcat/KM 90 mM^-1 min^-1; normalized cells 0.3 s^-1, 0.2 mM, 1.5 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1; Km normalized_value=0.2 normalized_unit=mM; kcat/Km normalized_value=1.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=18 raw_unit=min^-1; Km raw_value=0.2 raw_unit=mM; kcat/Km raw_value=90 raw_unit=mM^-1*min^-1

row_label: A2 / (2E)-3-methylpent-2-en-1-yl diphosphate

substrate: (2E)-3-methylpent-2-en-1-yl diphosphate


normalized_value_unit_evidence: kcat normalized_value=0.01233333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.12 normalized_unit=mM; kcat/Km normalized_value=0.1016666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.74 raw_unit=min^-1; Km raw_value=0.12 raw_unit=mM; kcat/Km raw_value=6.1 raw_unit=mM^-1*min^-1

row_label: A20 / (2E,4Z)-2-methylhexa-2,4-dien-1-yl diphosphate


smiles: CC(C)=C/C=C/COP(=O)(O)OP(=O)(O)O

normalized_value_unit_evidence: kcat normalized_value=0.001666666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.73 normalized_unit=mM; kcat/Km normalized_value=0.002333333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.1 raw_unit=min^-1; Km raw_value=0.73 raw_unit=mM; kcat/Km raw_value=0.14 raw_unit=mM^-1*min^-1

row_label: A18 / (2E)-5-methylhexa-2,4-dien-1-yl diphosphate


substrate_name: (2E)-but-2-en-1-yl diphosphate

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

substrate: (2E)-but-2-en-1-yl diphosphate


substrate_name: (2E)-penta-2,4-dien-1-yl diphosphate

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

normalized_value_unit_evidence: kcat normalized_value=0.0008333333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.26 normalized_unit=mM; kcat/Km normalized_value=0.003333333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.05 raw_unit=min^-1; Km raw_value=0.26 raw_unit=mM; kcat/Km raw_value=0.2 raw_unit=mM^-1*min^-1

row_label: A17 / (2E)-penta-2,4-dien-1-yl diphosphate

substrate: (2E)-penta-2,4-dien-1-yl diphosphate


substrate_name: (2Z)-3-chlorobut-2-en-1-yl diphosphate

smiles: C/C(Cl)=C/COP(=O)(O)OP(=O)(O)O

normalized_value_unit_evidence: kcat normalized_value=0.0006666666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.05 normalized_unit=mM; kcat/Km normalized_value=0.01666666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.04 raw_unit=min^-1; Km raw_value=0.05 raw_unit=mM; kcat/Km raw_value=1 raw_unit=mM^-1*min^-1

row_label: A11 / (2Z)-3-chlorobut-2-en-1-yl diphosphate

substrate: (2Z)-3-chlorobut-2-en-1-yl diphosphate


organism: Bos taurus


enzyme_display_name: acetoacetyl-CoA reductase

organism: Methylorubrum rhodesianum

proof_lines:
cofactor NADPH
cofactor NADH

enzyme: acetoacetyl-CoA reductase


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


proof_lines: recombinant mutant R204A/Y209A, pH 7.0, 25°C

proof_lines: recombinant mutants R204A and Y209A, pH 7.0, 25°C


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


organism: Clostridium acetobutylicum

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


organism: Candida tropicalis

mutation_signature: Δ2

mutation_type: deletion


organism: Homo sapiens

assay_conditions_summary: pH 8; cofactor CoA

proof_lines:
isozyme SCHAD II, at pH 8.0
isozyme SCHAD II, at pH 7.0
enzyme from brain, pH 7.0


proof_lines:
isozyme SCHAD I, at pH 8.5
isozyme SCHAD II, at pH 9.3
enzyme from brain


assay_conditions_summary: pH 8.5; cofactor CoA

proof_lines:
isozyme SCHAD I, at pH 8.5
isozyme SCHAD I, at pH 8.0
isozyme SCHAD II, at pH 8.0


assay_conditions_summary: pH 7; cofactor NAD+

proof_lines: enzyme from brain, substrate 17beta-estradiol


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


assay_conditions_summary: pH 9.5; 303.15 K; cofactor CoA


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


organism: Rattus norvegicus

assay_conditions_summary: pH 5; cofactor CoA

proof_lines: pH 5.0, recombinant His-tagged mutant S137C


proof_lines: pH 5.0, recombinant His-tagged mutant S137T


proof_lines: pH 5.0, recombinant His-tagged mutant S137A


proof_lines: pH 5.0, recombinant His-tagged wild-type enzyme


organism: Sus scrofa


assay_conditions_summary: pH 7; cofactor CoA


assay_conditions_summary: cofactor NADH


organism: Zoogloea ramigera

substrate_name: butyrylacetyl-CoA

substrate: butyrylacetyl-CoA


assay_conditions_summary: cofactor CoA


organism: Cupriavidus necator

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
enzyme Had, at pH 8.0 and 30°C
enzyme PaaH1, at pH 8.0 and 30°C


proof_lines:
enzyme PaaH1, at pH 8.0 and 30°C
enzyme Had, at pH 8.0 and 30°C


substrate_name: androsterone

substrate: androsterone


organism: Digitalis purpurea

substrate_name: NADH

substrate: NADH


assay_conditions_summary: cofactor NADPH


assay_conditions_summary: pH 7.8; 295.15 K; cofactor NADPH

proof_lines: pH 7.8, 22°C, recombinant His6-tagged enzyme


substrate_name: S-acetoacetyl-N-acetylcysteamine

substrate: S-acetoacetyl-N-acetylcysteamine


organism: Spinacia oleracea

proof_lines: NADPH, cytosolic enzyme type with preference for hydroxypyruvate as substrate

proof_lines: NADH, peroxisomal enzyme type with preference for hydroxypyruvate and NADH as substrates


substrate_name: Hydroxypyruvate

proof_lines: NADPH, cytosolic enzyme type with preference for hydroxypyruvate and NADPH as substrates

substrate: Hydroxypyruvate


organism: Digitalis lanata


assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH


enzyme_display_name: (R)-3-hydroxyacid-ester dehydrogenase

organism: Saccharomyces cerevisiae

substrate_name: ethyl 3-oxohexanoate

smiles: CCCC(=O)CC(=O)OCC

enzyme: (R)-3-hydroxyacid-ester dehydrogenase

substrate: ethyl 3-oxohexanoate


substrate_name: ethyl 3-oxobutanoate

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

substrate: ethyl 3-oxobutanoate


proof_lines:
in presence of NADH
in presence of NADPH


substrate_name: Unknown

substrate: Unknown


substrate_name: acetoacetyl-pantetheine

substrate: acetoacetyl-pantetheine


substrate_name: acetoacetyl-N-acetylcysteamine

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

substrate: acetoacetyl-N-acetylcysteamine


organism: Azotobacter vinelandii

substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: NADPH

substrate: NADPH


substrate_name: glyoxylate

substrate: glyoxylate


organism: Streptomyces coelicolor


proof_lines:
cofactor NADPH
cofactor NADH


proof_lines: pH 6.5, 30°C, recombinant enzyme in presence of 0.1 mM acetyl-CoA


organism: Escherichia coli


organism: Metallosphaera sedula

assay_conditions_summary: pH 8; 343.15 K; cofactor CoA


substrate_name: NAD+

assay_conditions_summary: pH 8; 338.15 K; cofactor NAD+

substrate: NAD+


organism: Unknown

substrate_name: SPC_39_Cell; SPC_38_Cell; SPC_2019_Cell

substrate: SPC_39_Cell; SPC_38_Cell; SPC_2019_Cell


organism: Pigeon


substrate_name: beta-ketopalmitoyl-CoA

substrate: beta-ketopalmitoyl-CoA


enzyme_display_name: 4-pyridoxic acid dehydrogenase

organism: Pseudomonas sp. MA-1

proof_lines: electron acceptor phenazine methosulfate, pH 8.0, 25°C

proof_lines: electron acceptor 2,6-dichloroindophenol, pH 8.0, 25°C

enzyme: 4-pyridoxic acid dehydrogenase


enzyme_display_name: serine 3-dehydrogenase (NADP+)

substrate_name: L-serine

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

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

enzyme: serine 3-dehydrogenase (NADP+)

substrate: L-serine


substrate_name: L-allo-threonine

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

substrate: L-allo-threonine


substrate_name: NADP+

substrate: NADP+


substrate_name: Glyoxylate

substrate: Glyoxylate


organism: Zea mays

substrate_name: NADPH; H+; Glyoxylate

substrate: NADPH; H+; Glyoxylate


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: pH 7.4, 37°C recombinant His-tagged enzyme


organism: Mesorhizobium loti

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, temperature not specified in the publication


organism: Saccharolobus solfataricus

substrate_name: NADH

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

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NADH

proof_lines: pH 7.5, 70°C, recombinant enzyme and native enzyme from xylose-grown cell extract

substrate: NADH


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

assay_conditions_summary: pH 5

proof_lines:
mutant E149Q, pH 8.0, 30°C
mutant E149Q, pH 5.0, 30°C


assay_conditions_summary: pH 8


assay_conditions_summary: pH 8; cofactor NADH


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADH

proof_lines: kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


substrate_name: beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor CoA


substrate_name: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)


substrate_name: NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)


enzyme_display_name: Acetoacetyl-CoA reductase

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

substrate_name: acetoacetyl-CoA

enzyme: Acetoacetyl-CoA reductase


substrate_name: NADPH


substrate_name: tetramyristoyl cardiolipin

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

substrate: tetralinoleoyl cardiolipin


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetoacetyl-CoA (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 4.3 sec(-1) with beta-ketododecanoyl-CoA as substrate. kcat is 3.5 sec(-1) with beta-ketooctanoyl-CoA as substrate. kcat is 1.9 sec(-1) with acetoacetyl-CoA as substrate. kcat is 2.6 sec(-1) with NADPH as substrate (PubMed:11932442)


substrate_name: NADPH (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor NADPH


substrate_name: H+; Glyoxylate; NADH

assay_conditions_summary: cofactor NAD+

substrate: H+; Glyoxylate; NADH


organism: Thermococcus litoralis

substrate_name: NADH; Glyoxylate; H+

substrate: NADH; Glyoxylate; H+


enzyme_display_name: UniProt P34439

organism: Caenorhabditis elegans

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

enzyme: UniProt P34439


organism: Drosophila melanogaster

substrate_name: NAD (in the presence of (3S)-3-hydroxybutanoyl-CoA, at pH 9.3 and 25 degrees Celsius)


enzyme_display_name: Fatty acid oxidation complex subunit alpha

organism: Escherichia coli (strain K12)

substrate_name: L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)

assay_conditions_summary: cofactor CoA


enzyme_display_name: Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

substrate_name: acetoacetyl-CoA at pH 5.0

assay_conditions_summary: pH 5; cofactor CoA

substrate: acetoacetyl-CoA at pH 5.0