Information on EC 1.17.5.1 - phenylacetyl-CoA dehydrogenase

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The expected taxonomic range for this enzyme is: Thauera aromatica

EC NUMBER
COMMENTARY hide
1.17.5.1
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RECOMMENDED NAME
GeneOntology No.
phenylacetyl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phenylacetyl-CoA + H2O + 2 quinone = phenylglyoxylyl-CoA + 2 quinol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phenylacetate degradation II (anaerobic)
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Phenylalanine metabolism
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SYSTEMATIC NAME
IUBMB Comments
phenylacetyl-CoA:quinone oxidoreductase
The enzyme from Thauera aromatica is a membrane-bound molybdenum---iron---sulfur protein. The enzyme is specific for phenylacetyl-CoA as substrate. Phenylacetate, acetyl-CoA, benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates. The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen. Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone [1]. A second enzyme, EC 3.1.2.25, phenylacetyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate.
CAS REGISTRY NUMBER
COMMENTARY hide
210756-43-7
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210756-43-7
cf. 3.1.25
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; strain DSM 6984
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phenylacetyl-CoA + H2O + 2,6-dichlorophenolindophenol
phenylglyoxylyl-CoA + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
phenylacetyl-CoA + H2O + duroquinone
phenylglyoxylyl-CoA + duroquinol
show the reaction diagram
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at 0.3 mM duroquinone, 150% of the activity with 0.25 mM 2,6-dichlorophenolindophenol
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?
phenylacetyl-CoA + H2O + menadione
phenylglyoxylyl-CoA + menadiol
show the reaction diagram
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at 0.3 mM menadione, 60% of the activity with 0.25 mM 2,6-dichlorophenolindophenol
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?
phenylacetyl-CoA + H2O + quinone
phenylglyoxylyl-CoA + quinol
show the reaction diagram
phenylacetyl-CoA + H2O + ubiquinone
phenylglyoxylyl-CoA + ubiquinol
show the reaction diagram
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ubiquinone is most likely the natural electron acceptor, involved in anaerobic metabolism of phenylalanine, catalyzes the first step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the second step being carried out by EC 3.1.2.25
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?
additional information
?
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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
phenylacetyl-CoA + H2O + ubiquinone
phenylglyoxylyl-CoA + ubiquinol
show the reaction diagram
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ubiquinone is most likely the natural electron acceptor, involved in anaerobic metabolism of phenylalanine, catalyzes the first step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the second step being carried out by EC 3.1.2.25
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?
additional information
?
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anaerobic metabolism of phenylacetate, catalyzes the first step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the second step being carried out by EC 3.1.2.25, cytochrome c probably does not act as physiological electron acceptor
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
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molybdenum-iron-sulfur enzyme, contains 30 mol Fe and 25 mol acid-labile sulfur per mol of native enzyme
molybdenum cofactor
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molybdenum-iron-sulfur enzyme, contains 0.66 mol Mo per mol of native enzyme
molybdopterin
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presence of a molybdopterin cofactor, contains 0.66 mol Mo per mol of native enzyme
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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low enzyme activity in cells grown with phenylglyoxylate, no activity in cells grown with benzoate and nitrate or after aerobic growth with phenylacetate, not inhibited by sodium salts of azide, thiocyanate, nitrate, nitrite, fluoride, cyanate, bipyridine, hydroxylamine, hydroxyurea, each at 10 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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enzyme activity is induced under denitrifying conditions with phenylalanine and phenylacetate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
phenylacetyl-CoA
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pH 7.5, 30°C, 2,6-dichlorophenolindophenol as electron acceptor
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
phenylacetyl-CoA
Thauera aromatica
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pH 7.5, 30°C, duroquinone as electron acceptor
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
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pH 7.5, 30°C
0.18
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pH 7.5, 30°C, 2,6-dichlorophenolindophenol as electron acceptor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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with 50 mM potassium phosphate buffer: 60% of optimum activity at pH 6.5, 87% of optimum activity at pH 7.5, with 50 mM Tris-HCl buffer: 60% of optimum activity at pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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alpha2beta2gamma2, 2 * 93000 + 2 * 27000 + 2 * 26000, SDS-PAGE
27000
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alpha2beta2gamma2, 2 * 93000 + 2 * 27000 + 2 * 26000, SDS-PAGE
93000
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alpha2beta2gamma2, 2 * 93000 + 2 * 27000 + 2 * 26000, SDS-PAGE
280000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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alpha2beta2gamma2, 2 * 93000 + 2 * 27000 + 2 * 26000, SDS-PAGE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen-insensitive, 73% of the initial activity is recovered after 3 h incubation in air on ice
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644662
remarkably stable with respect to oxygen
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644661
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% (w/v) glycerol, 0.1% (w/v) lauryldimethylamine oxide, partially purified enzyme, several weeks, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
12fold, partial
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