Purification and Properties of Methanol:5-hydroxybenzimidazolylcobamide Methyltransferase from Methanosarcina Barkeri

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1984 Nov 1

PMID 6438059

Citations 24

Authors

P van der Meijden

B W te Brommelstroet

C M Poirot

C van der Drift

G D Vogels

Affiliations

Soon will be listed here.

Abstract

Methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri has been purified to approximately 90% homogeneity by ion-exchange chromatography on DEAE-cellulose and QAE-A50 Sephadex columns. The molecular weight, estimated by gel electrophoresis, was found to be 122,000, and the enzyme contained two different subunits with molecular weights of 34,000 and 53,000, which indicates an alpha 2 beta structure. The enzyme contains three or four molecules of 5-hydroxybenzimidazolylcobamide, which could be removed by treatment of the enzyme with 2-mercaptoethanol or sodium dodecyl sulfate. In both cases the enzyme dissociated into its subunits. For stability, the enzyme required the presence of divalent cations such as Mg2+, Mn2+, Sr2+, Ca2+, or Ba2+. ATP, GTP, or CTP was needed in a reductive activation process of the enzyme. This activation was brought about by a mixture of H2, ferredoxin, and hydrogenase, but also by CO, which is thought to reduce the corrinoid chemically. The CO dehydrogenase-like activity of the methyltransferase is discussed.

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