A reversed genetic approach reveals the coenzyme specificity and other catalytic properties of three enzymes putatively involved in anaerobic oxidation of methane with sulfate
Author:
Affiliation:
1. The Institute of Low Temperature Science; Hokkaido University; Sapporo Japan
2. Department of Biochemistry; Max Planck Institute for Terrestrial Microbiology; Marburg Germany
3. PRESTO; Japan Science and Technology Agency (JST); Saitama Japan
Funder
Japan Science and Technology agency
Japan Society for the Promotion of Science
Max Planck Society
Publisher
Wiley
Subject
Ecology, Evolution, Behavior and Systematics,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/1462-2920.12475/fullpdf
Reference40 articles.
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2. N5,N10-Methenyltetrahydromethanopterin cyclohydrolase from the extreme thermophile Methanopyrus kandleri: increase of catalytic efficiency (Kcat/KM) and thermostability in the presence of salts;Breitung;Archiv Microbiol,1991
3. Salt dependence, kinetic-properties and catalytic mechanism of N-formylmethanofuran-tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri;Breitung;Eur J Biochem,1992
4. Unusual coenzymes of methanogenesis;Dimarco;Annu Rev Biochem,1990
5. Coenzyme F420 dependent N5, N10-methylenetetrahydromethanopterin dehydrogenase in methanol grown Methanosarcina barkeri;Enßle;Arch Microbiol,1991
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