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Titolo:
Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae
Autore:
Schocke, L; Schink, B;
Indirizzi:
Univ Konstanz, Fak Biol, D-78434 Constance, Germany Univ Konstanz Constance Germany D-78434 Biol, D-78434 Constance, Germany
Titolo Testata:
ARCHIVES OF MICROBIOLOGY
fascicolo: 5, volume: 171, anno: 1999,
pagine: 331 - 337
SICI:
0302-8933(199904)171:5<331:EABOFB>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANAEROBIC AROMATIC METABOLISM; GLUTACONYL-COA DECARBOXYLASE; SULFATE-REDUCING BACTERIA; DECOMPOSE FATTY-ACIDS; ENZYMATIC REDUCTION; ENERGY-CONSERVATION; KEY REACTION; GEN-NOV; PURIFICATION; ENVIRONMENTS;
Keywords:
Syntrophus gentianae; syntrophic benzoate degradation; glutaconyl-CoA decarboxylase; proton-translocating pyrophosphatase; benzoyl-CoA reductase (dearomatizing);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Schink, B Univ Konstanz, Fak Biol, Postfach 5560, D-78434 Constance, Germany Univ Konstanz Postfach 5560 Constance Germany D-78434 , Germany
Citazione:
L. Schocke e B. Schink, "Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae", ARCH MICROB, 171(5), 1999, pp. 331-337

Abstract

The pathway of fermentative benzoate degradation by the syntrophically fermenting bacterium Syntrophus gentianae was studied by measurement of enzymeactivities in cell-free extracts. Benzoate was activated by a benzoate-CoAligase reaction, forming AMP and pyrophosphate, which was subsequently cleaved by a membrane-bound proton-translocating pyrophosphatase. Glutaconyl-CoA (formed from hypothetical pimelyl-CoA and glutaryl-CoA intermediates) was decarboxylated to crotonyl-CoA by a sodium-ion-dependent membrane-bound glutaconyl-CoA decarboxylase, a biotin enzyme that could be inhibited by avidin. The overall energy budget of this fermentation could be balanced only if the dearomatizing reduction of benzoyl-CoA is assumed to produce cyclohexene carboxyl-CoA rather than cyclohexadiene carboxyl-CoA, although experimental evidence of this reaction is still insufficient. With this assumption, benzoate degradation by S. gentianae can be balanced to yield one-third to two-thirds of an ATP unit per benzoate degraded, in accordance with earlier measurements of whole-cell energetics.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 07:32:19