@inbook{c9a56333ddc54422a420a5616f9a4b72,
title = "Acetate kinase and phosphotransacetylase",
abstract = "Most of the methane produced in nature derives from the methyl group of acetate, the major end product of anaerobes decomposing complex plant material. The acetate is derived from the metabolic intermediate acetyl-CoA via the combined activities of phosphotransacetylase and acetate kinase. In Methanosarcina species, the enzymes function in the reverse direction to activate acetate to acetyl-CoA prior to cleavage into a methyl and carbonyl group of which the latter is oxidized providing electrons for reduction of the former to methane. Thus, phosphotransacetylase and acetate kinase have a central role in the conversion of complex organic matter to methane by anaerobic microbial food chains. Both enzymes have been purified from Methanosarcina thermophila and characterized. Both enzymes from M. thermophila have also been produced in Escherichia coli permitting crystal structures and amino acid variants, the kinetic and biochemical studies of which have lead to proposals for catalytic mechanisms. The high identity of both enzymes to paralogs in the domain Bacteria suggests ancient origins and common mechanisms.",
author = "Ferry, {James G.}",
note = "Funding Information: Research in the author's laboratory was supported by the National Institutes of Health, National Science Foundation, and the Department of Energy.",
year = "2011",
doi = "10.1016/B978-0-12-385112-3.00011-1",
language = "English (US)",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "219--231",
booktitle = "Methods in Enzymology",
address = "United States",
}