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- Name help_outline phenylacetyl-CoA Identifier CHEBI:57390 Charge -4 Formula C29H38N7O17P3S InChIKeyhelp_outline ZIGIFDRJFZYEEQ-CECATXLMSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)Cc1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
a ubiquinone
Identifier
CHEBI:16389
(CAS: 1339-63-5)
help_outline
Charge
0
Formula
C9H10O4(C5H8)n
Search links
Involved in 58 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9565Polymer name: a ubiquinonePolymerization index help_outline nFormula C9H10O4(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phenylglyoxylyl-CoA Identifier CHEBI:58811 Charge -4 Formula C29H36N7O18P3S InChIKeyhelp_outline FISPFQWSJIRGHD-SVHODSNWSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)C(=O)c1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
a ubiquinol
Identifier
CHEBI:17976
(CAS: 56275-39-9)
help_outline
Charge
0
Formula
C9H12O4(C5H8)n
Search links
Involved in 55 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9566Polymer name: a ubiquinolPolymerization index help_outline nFormula C9H12O4(C5H8)nCharge (0)(0)nMol File for the polymer
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Cross-references
| RHEA:15705 | RHEA:15706 | RHEA:15707 | RHEA:15708 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica.
Rhee S.K., Fuchs G.
Phenylacetic acids are common intermediates in the microbial metabolism of various aromatic substrates including phenylalanine. In the denitrifying bacterium Thauera aromatica phenylacetate is oxidized, under anoxic conditions, to the common intermediate benzoyl-CoA via the intermediates phenylace ... >> More
Phenylacetic acids are common intermediates in the microbial metabolism of various aromatic substrates including phenylalanine. In the denitrifying bacterium Thauera aromatica phenylacetate is oxidized, under anoxic conditions, to the common intermediate benzoyl-CoA via the intermediates phenylacetyl-CoA and phenylglyoxylate (benzoylformate). The enzyme that catalyzes the four-electron oxidation of phenylacetyl-CoA has been purified from this bacterium and studied. The enzyme preparation catalyzes the reaction phenylacetyl-CoA + 2 quinone + 2 H2O --> phenylglyoxylate + 2 quinone H2 + CoASH. Phenylacetyl-CoA:acceptor oxidoreductase is a membrane-bound molybdenum-iron-sulfur protein. The purest preparations contained three subunits of 93, 27, and 26 kDa. Ubiquinone is most likely to act as the electron acceptor, and the oxygen atom introduced into the product is derived from water. The protein preparations contained 0.66 mol Mo, 30 mol Fe, and 25 mol acid-labile sulfur per mol of native enzyme, assuming a native molecular mass of 280 kDa. Phenylglyoxylyl-CoA, but not mandelyl-CoA, was observed as a free intermediate. All enzyme preparations also catalyzed the subsequent hydrolytic release of coenzyme A from phenylglyoxylyl-CoA but not from phenylacetyl-CoA. The enzyme is reversibly inactivated by a low concentration of cyanide, but is remarkably stable with respect to oxygen. This new member of the molybdoproteins represents the first example of an enzyme which catalyzes the alpha-oxidation of a CoA-activated carboxylic acid without utilizing molecular oxygen. << Less
Eur J Biochem 262:507-515(1999) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Phenylacetyl-CoA:acceptor oxidoreductase, a new alpha-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica.
Schneider S., Fuchs G.
Anaerobic oxidation of phenylalanine and phenylacetate proceeds via alpha-oxidation of phenylacetyl-CoA to phenylglyoxylate. This four-electron oxidation system was studied in the denitrifying bacterium Thauera aromatica. It is membrane-bound and was solubilized with Triton X-100. The system used ... >> More
Anaerobic oxidation of phenylalanine and phenylacetate proceeds via alpha-oxidation of phenylacetyl-CoA to phenylglyoxylate. This four-electron oxidation system was studied in the denitrifying bacterium Thauera aromatica. It is membrane-bound and was solubilized with Triton X-100. The system used dichlorophenolindophenol as an artificial electron acceptor; a spectrophotometric assay was developed. No other products besides phenylglyoxylate and coenzyme A were observed. The enzyme was quite oxygen-insensitive and was inactivated by low concentrations of cyanide. Enzyme activity was induced under denitrifying conditions with phenylalanine and phenylacetate, it was low in cells grown with phenylglyoxylate, and it was virtually absent in cells grown with benzoate and nitrate or after aerobic growth with phenylacetate. << Less
Arch Microbiol 169:509-516(1998) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.