Purification and characterization of a methanol-induced cobamide-containing protein from Sporomusa ovata.

Abstract:

:The major cobamide-containing protein from methanol-utilizing Sporomusa ovata was 8-fold enriched to apparent homogeneity. The protein exhibited a molecular mass of 40 kDa and of 38 kDa determined by gel filtration and by SDS-polyacrylamide gel electrophoresis, respectively. This finding indicates a monomeric protein structure. Monospecific polyclonal antisera raised against the protein did not cross react with another cobamide-containing protein from Sporomusa cells. Only the 40 kDa cobamide-containing protein was induced by methanol, since proteins from cells grown on 3,4-dimethoxybenzoate, betaine H2/CO2, or fructose showed faint or no cross reaction. Hence, the 40 kDa cobamide-containing protein is presumably involved in the methyl-transfer reaction of the methanol metabolism. The purified enzyme revealed 1.1 mol of p-cresolyl cobamide per mol of protein, but it lacked of iron-sulfur centers. Remarkably, the cofactor was firmly bound to its protein.

journal_name

Arch Microbiol

journal_title

Archives of microbiology

authors

Stupperich E,Aulkemeyer P,Eckerskorn C

doi

10.1007/BF00245367

keywords:

subject

Has Abstract

pub_date

1992-01-01 00:00:00

pages

370-3

issue

5

eissn

0302-8933

issn

1432-072X

journal_volume

158

pub_type

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