Abstract
The O-demethylase of the methylotrophic homoacetogenic bacterium strain MC was purified to apparent homogeneity. The enzyme system consisted of four different components that were designated A, B, C, and D according to their elution sequence from the anionic-exchange chromatography column. All four components were essentially required for catalysis of the transfer of the methyl group from phenyl methyl ethers to tetrahydrofolate. According to gel filtration and SDS-PAGE, components A and B were monomers with apparent molecular masses of approximately 26 kDa (subunit 25 kDa) and 36 (subunit 41 kDa), respectively; component C appeared to be a trimeric protein (195 kDa, subunit 67 kDa); and component D was probably a dimer (64 kDa, subunit 30 kDa). Component A contained one corrinoid per monomer. In crude extracts, component D appeared to be the rate-limiting protein for the complete methyl transfer reaction. Additional requirements for the reaction were ATP and low-potential reducing equivalents supplied by either titanium(III) citrate or H2 plus hydrogenase purified from strain MC.
Similar content being viewed by others
Author information
Authors and Affiliations
Additional information
Received: 5 February 1997 / Accepted: 17 April 1997
Rights and permissions
About this article
Cite this article
Kaufmann, F., Wohlfarth, G. & Diekert, G. Isolation of O-demethylase, an ether-cleaving enzyme system of the homoacetogenic strain MC. Arch Microbiol 168, 136–142 (1997). https://doi.org/10.1007/s002030050479
Issue Date:
DOI: https://doi.org/10.1007/s002030050479