Open AccessInvolvement of a corrinoid enzyme in methanogenesis from acetate in Methanosarcina barkeri
Author(s) -
Wijngaard W.M.H.,
Drift C.,
Vogels G.D.
Publication year - 1988
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.1574-6968.1988.tb02589.x
Subject(s) - methanogenesis , corrinoid , methanosarcina barkeri , methanosarcina , biochemistry , cofactor , methanomicrobiales , enzyme , chemistry , acetate kinase , methane , organic chemistry , escherichia coli , methylation , methyltransferase , gene
Abstract Extracts of acetate‐grown Methanosarcina barkeri strain Fusaro formed methane from acetate plus ATP and form acetyl phosphate under H 2 . Coenzyme A (CoA) is stimulatory. Inhibitors of methanogenesis are cyanide, propyliodide and bromoethanesulfonic acid. In cofactor‐free extracts methanogenic activity from acetate was restored by addition of ATP, CoA, coenzyme M and 7‐mercaptoheptanoylthreonine phosphate. An enzyme‐bound corrinoid was found to be involved in methanogenesis from acetate.