Affiliation:
1. Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Kagamiyama 1-3-1, Higashi-Hiroshima 739-8530, Japan
Abstract
ABSTRACT
The thermophilic homoacetogenic bacterium
Moorella
sp. strain HUC22-1 ferments glyoxylate to acetate roughly according to the reaction 2 glyoxylate → acetate + 2 CO
2
. A batch culture with glyoxylate and yeast extract yielded 11.7 g per mol of cells per substrate, which was much higher than that obtained with H
2
plus CO
2
. Crude extracts of glyoxylate-grown cells catalyzed the ADP- and NADP-dependent condensation of glyoxylate and acetyl coenzyme A (acetyl-CoA) to pyruvate and CO
2
and converted pyruvate to acetyl-CoA and CO
2
, which are the key reactions of the malyl-CoA pathway. ATP generation was also detected during the key enzyme reactions of this pathway. Furthermore, this bacterium consumed
l
-malate, an intermediate in the malyl-CoA pathway, and produced acetate. These findings suggest that
Moorella
sp. strain HUC22-1 can generate ATP by substrate-level phosphorylation during glyoxylate catabolism through the malyl-CoA pathway.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
12 articles.
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