Genome analysis and heterologous expression of acetate-activating enzymes in the anammox bacterium Kuenenia stuttgartiensis

Russ, L; Harhangi, HR; Schellekens, J; Verdellen, B; Kartal, B; Op den Camp, HJ; Jetten, MS

HERO ID

1454828

Reference Type

Journal Article

Year

2012

Language

English

PMID

22752113

HERO ID 1454828
In Press No
Year 2012
Title Genome analysis and heterologous expression of acetate-activating enzymes in the anammox bacterium Kuenenia stuttgartiensis
Authors Russ, L; Harhangi, HR; Schellekens, J; Verdellen, B; Kartal, B; Op den Camp, HJ; Jetten, MS
Journal Archives of Microbiology
Volume 194
Issue 11
Page Numbers 943-948
Abstract Anaerobic ammonium-oxidizing bacteria were recently shown to use short-chain organic acids as additional energy source. The AMP-forming acetyl-CoA synthetase gene (acs) of Kuenenia stuttgartiensis, encoding an important enzyme involved in the conversion of these organic acids, was identified and heterologously expressed in Escherichia coli to investigate the activation of several substrates, that is, acetate, propionate and butyrate. The heterologously expressed ACS enzyme could complement an E. coli triple mutant deficient in all pathways of acetate activation. Activity was observed toward several short-chain organic acids, but was highest with acetate. These properties are in line with a mixotrophic growth of anammox bacteria. In addition to acs, the genome of K. stuttgartiensis contained the essential genes of an acetyl-CoA synthase/CO dehydrogenase complex and genes putatively encoding two isoenzymes of archaeal-like ADP-forming acetyl-CoA synthetase underlining the importance of acetyl-CoA as intermediate in the carbon assimilation metabolism of anammox bacteria.
Doi 10.1007/s00203-012-0829-7
Pmid 22752113
Wosid WOS:000310219500007
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English
Keyword Acetate; Propionate; Acetyl-coenzyme A; Anammox; AMP