Catalytic Properties, Molecular Composition and Sequence Alignments of Pyruvate: Ferredoxin Oxidoreductase from the Methanogenic Archaeon Methanosarcina Barkeri (Strain Fusaro)

• Published in: European journal of biochemistry Vol. 237; no. 1; pp. 35 - 44
• Main Authors: Bock, Anne‐Katrin, Kunow, Jasper, Glasemacher, Jürgen, Schönheit, Peter
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01.04.1996
• Subjects: Amino Acid Sequence; Archaea; Catalysis; Cell Extracts; Chromatography, Gel; Chromatography, Ion Exchange; coenzyme F420; Electrophoresis, Polyacrylamide Gel; ferredoxin; ferredoxin oxidoreductase; Ketone Oxidoreductases - genetics; Ketone Oxidoreductases - isolation & purification; Ketone Oxidoreductases - metabolism; Methanosarcina barkeri; Methanosarcina barkeri - enzymology; Molecular Sequence Data; pyruvate; Pyruvate Synthase; Sequence Homology, Amino Acid

Methanosarcina barkeri (strain Fusaro) was grown on pyruvate as methanogenic substrate [Bock, A. K., Prieger‐Kraft, A. & Schönheit, P. (1994) Arch. Microbiol. 161, 33–46]. The first enzyme of pyruvate catabolism, pyruvate oxidoreductase, which catalyzes oxidation of pyruvate to acetyl‐CoA was pu...