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.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Sakai S,Inokuma K,Nakashimada Y,Nishio Ndoi
10.1128/AEM.01421-07subject
Has Abstractpub_date
2008-03-01 00:00:00pages
1447-52issue
5eissn
0099-2240issn
1098-5336pii
AEM.01421-07journal_volume
74pub_type
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