Open AccessDegradation of Glyoxylate and Glycolate with ATP Synthesis by a Thermophilic Anaerobic Bacterium, Moorella sp. Strain HUC22-1
Author(s) -
Shinsuke Sakai,
Kentaro Inokuma,
Yutaka Nakashimada,
Naomichi Nishio
Publication year - 2008
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01421-07
Subject(s) - glyoxylate cycle , biochemistry , malate synthase , bacteria , substrate (aquarium) , strain (injury) , enzyme , thermophile , chemistry , biology , isocitrate lyase , ecology , anatomy , genetics
The thermophilic homoacetogenic bacteriumMoorella sp. strain HUC22-1 ferments glyoxylate to acetate roughly according to the reaction 2 glyoxylate → acetate + 2 CO2 . 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 H2 plus CO2 . Crude extracts of glyoxylate-grown cells catalyzed the ADP- and NADP-dependent condensation of glyoxylate and acetyl coenzyme A (acetyl-CoA) to pyruvate and CO2 and converted pyruvate to acetyl-CoA and CO2 , 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 consumedl -malate, an intermediate in the malyl-CoA pathway, and produced acetate. These findings suggest thatMoorella sp. strain HUC22-1 can generate ATP by substrate-level phosphorylation during glyoxylate catabolism through the malyl-CoA pathway.