Information on EC 1.2.1.58 - phenylglyoxylate dehydrogenase (acylating)

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.2.1.58
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RECOMMENDED NAME
GeneOntology No.
phenylglyoxylate dehydrogenase (acylating)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phenylglyoxylate + NAD+ + CoA = benzoyl-S-CoA + CO2 + NADH
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylalanine metabolism
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SYSTEMATIC NAME
IUBMB Comments
phenylglyoxylate:NAD+ oxidoreductase
Requires thiamine diphosphate as cofactor. The enzyme from the denitrifying bacterium Azoarcus evansii is specific for phenylglyoxylate. 2-Oxoisovalerate is oxidized at 15% of the rate for phenylglyoxylate. Also reduces viologen dyes. Contains iron-sulfur centres and FAD.
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CAS REGISTRY NUMBER
COMMENTARY hide
205510-78-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoisovalerate + NAD+ + CoA-SH
?
show the reaction diagram
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at 15% of the activity relative to phenylglyoxylate
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phenylglyoxylate + benzyl viologen + CoA-SH
benzoyl-S-CoA + CO2 + reduced benzyl viologen
show the reaction diagram
phenylglyoxylate + FAD + CoA-SH
benzoyl-S-CoA + CO2 + FADH2
show the reaction diagram
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phenylglyoxylate + FMN + CoA-SH
benzoyl-S-CoA + CO2 + FMNH
show the reaction diagram
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phenylglyoxylate + methyl viologen + CoA-SH
benzoyl-S-CoA + CO2 + reduced methyl viologen
show the reaction diagram
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phenylglyoxylate + NAD+ + CoA-SH
benzoyl-S-CoA + CO2 + NADH
show the reaction diagram
additional information
?
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enzyme catalyzes a NAD(H):viologen dye transhydrogenation
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phenylglyoxylate + NAD+ + CoA-SH
benzoyl-S-CoA + CO2 + NADH
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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contains 1.1 mol FAD per mol of enzyme
thiamine diphosphate
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reaction is strictly dependent on
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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iron-sulfur protein, contains 35 mol Fe and 36 mol acid-labile sulfur per mol of enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.055
CoA
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0.074
NAD+
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0.045
phenylglyoxylate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
46
benzyl viologen
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
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NAD+-dependent reaction
7.4
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benzyl viologen-dependent reaction
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11500
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2 * 50000 + 2 * 48000 + 2 * 43000 + 2 * 24000 + 2 * 11500, SDS-PAGE. The enzyme complex consists of a core enzyme of 4 subunits with the composition alpha2beta2gamma2delta2, this complex is able to reduce viologen dyes. The holoenzyme contains in addition an epsilon2 unit that catalyzes the transfer of electrons from a small ferredoxin-like subunit of the core complex to NAD, this unit also catalyzes the transhydrogenase reaction, carries FAD and resembles ferredoxin:NAD(P)+-oxidoreductase
24000
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2 * 50000 + 2 * 48000 + 2 * 43000 + 2 * 24000 + 2 * 11500, SDS-PAGE. The enzyme complex consists of a core enzyme of 4 subunits with the composition alpha2beta2gamma2delta2, this complex is able to reduce viologen dyes. The holoenzyme contains in addition an epsilon2 unit that catalyzes the transfer of electrons from a small ferredoxin-like subunit of the core complex to NAD, this unit also catalyzes the transhydrogenase reaction, carries FAD and resembles ferredoxin:NAD(P)+-oxidoreductase
43000
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2 * 50000 + 2 * 48000 + 2 * 43000 + 2 * 24000 + 2 * 11500, SDS-PAGE. The enzyme complex consists of a core enzyme of 4 subunits with the composition alpha2beta2gamma2delta2, this complex is able to reduce viologen dyes. The holoenzyme contains in addition an epsilon2 unit that catalyzes the transfer of electrons from a small ferredoxin-like subunit of the core complex to NAD, this unit also catalyzes the transhydrogenase reaction, carries FAD and resembles ferredoxin:NAD(P)+-oxidoreductase
48000
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2 * 50000 + 2 * 48000 + 2 * 43000 + 2 * 24000 + 2 * 11500, SDS-PAGE. The enzyme complex consists of a core enzyme of 4 subunits with the composition alpha2beta2gamma2delta2, this complex is able to reduce viologen dyes. The holoenzyme contains in addition an epsilon2 unit that catalyzes the transfer of electrons from a small ferredoxin-like subunit of the core complex to NAD, this unit also catalyzes the transhydrogenase reaction, carries FAD and resembles ferredoxin:NAD(P)+-oxidoreductase
50000
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2 * 50000 + 2 * 48000 + 2 * 43000 + 2 * 24000 + 2 * 11500, SDS-PAGE. The enzyme complex consists of a core enzyme of 4 subunits with the composition alpha2beta2gamma2delta2, this complex is able to reduce viologen dyes. The holoenzyme contains in addition an epsilon2 unit that catalyzes the transfer of electrons from a small ferredoxin-like subunit of the core complex to NAD, this unit also catalyzes the transhydrogenase reaction, carries FAD and resembles ferredoxin:NAD(P)+-oxidoreductase
370000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
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2 * 50000 + 2 * 48000 + 2 * 43000 + 2 * 24000 + 2 * 11500, SDS-PAGE. The enzyme complex consists of a core enzyme of 4 subunits with the composition alpha2beta2gamma2delta2, this complex is able to reduce viologen dyes. The holoenzyme contains in addition an epsilon2 unit that catalyzes the transfer of electrons from a small ferredoxin-like subunit of the core complex to NAD, this unit also catalyzes the transhydrogenase reaction, carries FAD and resembles ferredoxin:NAD(P)+-oxidoreductase
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
6°C, 1 mM phenylglyoxal, half-life: 2 days
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6°C, 10% glycerol, half-life: 4 days
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6°C, without glycerol or substrate, half-life: 10 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Show AA Sequence (353 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.58)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)