Open AccessRoseovarius sp. strain 217: aerobic taurine dissimilation via acetate kinase and acetate‐CoA ligase
Author(s) -
Baldock Marijke I.,
Denger Karin,
Smits Theo H.M.,
Cook Alasdair M.
Publication year - 2007
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2007.00719.x
Subject(s) - acetate kinase , biochemistry , taurine , acetyltransferase , chemistry , enzyme , biology , gene , acetylation , amino acid , escherichia coli
The genome sequence of Roseovarius sp. strain 217 indicated that many pathway enzymes found in other organisms for the degradation of taurine are represented, but that a novel, apparently energy‐dependent pathway is involved in the conversion of acetyl phosphate to acetyl CoA. Thus, an ABC transporter for taurine could be postulated, while inducible taurine: pyruvate aminotransferase, alanine dehydrogenase, sulfoacetaldehyde acetyltransferase and sulfite dehydrogenase could be assayed. Whereas phosphate acetyltransferase has been found in other organisms, none was indicated in the genome sequence and no activity was found in cell‐free extracts. Instead, acetate kinase was active as was acetate‐CoA ligase.