| Literature DB >> 7928975 |
D L Roberts1, S Zhao, T Doukov, S W Ragsdale.
Abstract
The methyltransferase (MeTr) from Clostridium thermoaceticum transfers the N5-methyl group of (6S)-methyltetrahydrofolate to the cobalt center of a corrinoid/iron-sulfur protein in the acetyl coenzyme A pathway. MeTr was purified to homogeneity and shown to lack metals. The acsE gene encoding MeTr was sequenced and actively expressed in Escherichia coli at a level of 9% of cell protein. Regions in the sequence of MeTr and the E. coli cobalamin-dependent methionine synthase were found to share significant homology, suggesting that they may represent tetrahydrofolate-binding domains.Entities:
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Year: 1994 PMID: 7928975 PMCID: PMC196833 DOI: 10.1128/jb.176.19.6127-6130.1994
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490