Transmethylation reactions during methanogenesis from acetate in Methanosarcina barkeri. [Annual report], August 1, 1991--April 1, 1993

Technical Report · Thu Jul 01 04:00:00 EDT 1993

DOI:https://doi.org/10.2172/10165770· OSTI ID:10165770

Krzycki, J A

Methanosarcina possesses an abundance corrinoid, which acts as enzyme prosthetic group and functions in methyl transfer reactions. When this work was initiated only two corrinoid proteins had been described from Methanosarcina: methyltransferase I, which catalyses the first step m methanogenesis from methanol; and the corrinoid/iron sulfur protein, which is the primary methyl accepting group in the cleavage of acetyl-CoA during methanogenesis from acetate. Using our technique of in vitro methylation of corrinoid proteins by radioactive methanogenic substrates we have found several novel corrinoid proteins are present in this organism which can function as methytransferases, which are methylated by growth substrate, and are apparently regulated by growth substrate.

• Research Organization: Ohio State Univ., Columbus, OH (United States). Dept. of Microbiology
• Sponsoring Organization: USDOE, Washington, DC (United States)
• DOE Contract Number: FG02-91ER20042
• OSTI ID: 10165770
• Report Number(s): DOE/ER/20042--1; ON: DE93017203
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
090900
550201
59 BASIC BIOLOGICAL SCIENCES
AUTORADIOGRAPHY
BIOLOGICAL PATHWAYS
CARBON 14 COMPOUNDS
ELECTROPHORESIS
FRACTIONATION
GEL PERMEATION CHROMATOGRAPHY
METHANOGENIC BACTERIA
METHYL TRANSFERASES
PROCESSING
PROGRESS REPORT
TRACER TECHNIQUES