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Titolo:
GENES-CODING FOR THE BENZOYL-COA PATHWAY OF ANAEROBIC AROMATIC METABOLISM IN THE BACTERIUM THAUERA-AROMATICA
Autore:
BREESE K; BOLL M; ALTMORBE J; SCHAGGER H; FUCHS G;
Indirizzi:
UNIV FREIBURG,INST BIOL 2,LEHRSTUHL MIKROBIOL,SCHANZLESTR 1 D-79104 FREIBURG GERMANY UNIV FREIBURG,INST BIOL 2,LEHRSTUHL MIKROBIOL D-79104 FREIBURG GERMANY UNIV FREIBURG,INST BIOL 3 D-7800 FREIBURG GERMANY UNIV FRANKFURT,UNIV KLINIKUM D-6000 FRANKFURT GERMANY
Titolo Testata:
European journal of biochemistry
fascicolo: 1, volume: 256, anno: 1998,
pagine: 148 - 154
SICI:
0014-2956(1998)256:1<148:GFTBPO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACIDAMINOCOCCUS-FERMENTANS; ESCHERICHIA-COLI; (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE; NUCLEOTIDE-SEQUENCE; ENZYMATIC REDUCTION; MOLECULAR-CLONING; KEY REACTION; DEHYDROGENASE; EXPRESSION; BIOSYNTHESIS;
Keywords:
BENZOYL-COA PATHWAY; BENZOYL-COA REDUCTASE; DIENOYL-COA HYDRATASE; 3-HYDROXYPIMELYL-COA; 2-HYDROXYGLUTARYL-COA DEHYDRATASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
K. Breese et al., "GENES-CODING FOR THE BENZOYL-COA PATHWAY OF ANAEROBIC AROMATIC METABOLISM IN THE BACTERIUM THAUERA-AROMATICA", European journal of biochemistry, 256(1), 1998, pp. 148-154

Abstract

Many aromatic compounds are anaerobically oxidized to CO, via benzoyl-CoA as the common aromatic intermediate. In Thauera aromatica, the central benzoyl-CoA pathway comprises the ATP-driven two-electron reduction of the benzene ring, this reaction uses a ferredoxin as electron donor and is catalyzed by benzoyl-CoA reductase. The first intermediate, cyclohex-1,5-diene-1-carboxyl-CoA, is subsequently hydrated by dienoyl-CoA hydratase to 6-hydroxycyclohex-1-ene-1-carboxyl-CoA. Formation of the main product produced by cell extracts, 3-hydroxypimelyl-CoA, requires at least two further steps; the oxidation of a hydroxyl group and the hydrolytic carbon ring cleavage of a CoA-activated beta-oxoacid. In addition, enoyl-CoA hydratase may come into play. A cluster of eight adjacent genes, which are transcribed in the same direction and may form an operon, was found in this bacterium. The cluster codes for proven and postulated enzymes of the benzoyl-CoA pathway. The genes for the enzymes code for ferredoxin, four subunits of benzoyl-CoA reductase, dienoyl-CoA hydratase, 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dt:hydrogenase (NAD(+)), and the ring hydrolyzing enzyme. The deduced amino acid sequences of these proteins were 35-86% similar to the corresponding sequences found in Rhodopseudomonns palustris. Benzoyl-CoA reductase subunits exhibit distinct similarities with 2-hydroxyglutaryl-CoA dehydratase and its ATP-hydrolysing activase protein of Acidaminococcus fermentans as well as with open reading frames of unknown functionin other bacteria. Conversion of benzoyl-CoA to 3-hydroxypimelyl-CoA can be explained by a minimal model of the benzoyl-CoA pathway assuming the four enzymes whose genes were characterized and an additional enoyl-CoA hydratase. In R. palustris the dienoyl-CoA hydratase gene is lacking suggesting the operation of a modified benzoyl-CoA pathway withcyclohex-1-ene-1-carboxyl-CoA as intermediate.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 22:31:58