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 . A second enzyme, EC 3.1.2.25, phenylacetyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate.
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The enzyme appears in viruses and cellular organisms
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, propionyl-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, a second enzyme, EC 3.1.2.25, phenylglyoxylyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate
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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.
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
four-electron oxidation, uses dichlorophenolindophenol as artificial electron acceptor, 2 mol dichlorophenolindophenol is reduced per mol phenylacetyl-CoA, catalyzes the anaerobic oxidation of the methylene group in the alpha-position to the CoA-activated carboxyl group, molecular oxygen is not required for the oxidation
four-electron oxidation, catalyzes an alpha-oxidation without utilizing molecular oxygen, ubiquinone is most likely the natural electron acceptor, specific for phenylacetyl-CoA, enzyme preparation catalyzes the reaction phenylacetyl-CoA + 2 H2O + 2 quinone = phenylglyoxylate + 2 quinone H2 + CoASH with phenylglyoxylyl-CoA as free intermediate, which is subsequently hydrolyzed
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
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
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
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
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
Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica
Phenylacetyl-CoA:acceptor oxidoreductase, a new a-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica