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Titolo:
Autotrophic CO2 fixation by Chloroflexus aurantiacus: Study of glyoxylate formation and assimilation via the 3-hydroxypropionate cycle
Autore:
Herter, S; Farfsing, J; Gadon, N; Rieder, C; Eisenreich, W; Bacher, A; Fuchs, G;
Indirizzi:
Univ Freiburg, Inst Biol 2, D-79104 Freiburg, Germany Univ Freiburg Freiburg Germany D-79104 Biol 2, D-79104 Freiburg, Germany Tech Univ Munich, D-8000 Munich, Germany Tech Univ Munich Munich GermanyD-8000 iv Munich, D-8000 Munich, Germany
Titolo Testata:
JOURNAL OF BACTERIOLOGY
fascicolo: 14, volume: 183, anno: 2001,
pagine: 4305 - 4316
SICI:
0021-9193(200107)183:14<4305:ACFBCA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACETYL-COENZYME-A; FILAMENTOUS BACTERIUM; CARBON FIXATION; METABOLISM; PATHWAY; CARBOXYLASE; C-13-NMR; ACETATE; GROWTH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Fuchs, G Univ Freiburg, Inst Biol 2, Schanzlestr 1, D-79104 Freiburg, Germany Univ Freiburg Schanzlestr 1 Freiburg Germany D-79104 rg, Germany
Citazione:
S. Herter et al., "Autotrophic CO2 fixation by Chloroflexus aurantiacus: Study of glyoxylate formation and assimilation via the 3-hydroxypropionate cycle", J BACT, 183(14), 2001, pp. 4305-4316

Abstract

In the facultative autotrophic organism Chloroflexus aurantiacus, a phototrophic green nonsulfur bacterium, the Calvin cycle does not appear to be operative in autotrophic carbon assimilation. An alternative cyclic pathway, the 3-hydroxypropionate cycle, has been proposed. In this pathway, acetyl coenzyme A (acetyl-CoA) is assumed to be converted to malate, and two CO2 molecules are thereby fixed. Malyl-CoA is supposed to be cleaved to acetyl-CoA, the starting molecule, and glyoxylate, the carbon fixation product. Malyl-CoA cleavage is shown here to be catalyzed by malyl-CoA lyase; this enzyme activity is induced severalfold in autotrophically grown cells. Malate isconverted to malyl-CoA via an inducible CoA transferase with succinyl-CoA as a CoA donor. Some enzyme activities involved in the conversion of malonyl-CoA via 3-hydroxypropionate to propionyl-CoA are also induced under autotrophic growth conditions. So far, no clue as to the first step in glyoxylate assimilation has been obtained. One possibility for the assimilation of glyoxylate involves the conversion of glyoxylate to glycine and the subsequent assimilation of glycine. However, such a pathway does not occur, as shown by labeling of whole cells with [1,2-C-13(2)]glycine, Glycine carbon was incorporated only into glycine, serine, and compounds that contained C-1 units derived therefrom and not into other cell compounds.

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Documento generato il 24/11/20 alle ore 14:20:06