Open Access[Acetyl-CoA cleavage and synthesis in methanogens]. Progress report, September 1994--August 1997
Publication year - 1998
Language(s) - English
Resource type - Reports
DOI - 10.2172/666267
Subject(s) - ferredoxin , cleavage (geology) , enzyme , corrinoid , chemistry , sulfur , spectroscopy , stereochemistry , biochemistry , biology , methyltransferase , dna , methylation , organic chemistry , physics , paleontology , fracture (geology) , quantum mechanics
The acetyl-CoA decarbonylase synthase (ACDS) complex has been detected in a variety of methanogens including species of Methanosarcina, Methanothrix (i.e., Methanosaeta), and Methanococcus. The multienzyme complex from Methanosarcina barkeri is composed of five different subunits, possibly arranged in an {alpha}{sub 6}{beta}{sub 6}{gamma}{sub 6}{delta}{sub 6}{var_epsilon}{sub 6} structure with the individual subunits of molecular masses (kDa) of 89, 60, 50, 48, and 20, respectively. This progress report summarizes the work from the past 21 months on studies directed toward understanding how the ACDS complex functions in the physiology of acetate-cleaving, and acetate-synthesizing methanogens