J Bacteriol. 1994 Oct;176(19):6127-30.

The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum.

Roberts DL, Zhao S, Doukov T, Ragsdale SW.

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Department of Biochemistry, University of Nebraska, Lincoln 68583-0718.

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.

PMID:: 7928975; [PubMed - indexed for MEDLINE]
PMCID:: PMC196833

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Mechanism of transfer of the methyl group from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein catalyzed by the methyltransferase from Clostridium thermoaceticum: a key step in the Wood-Ljungdahl pathway of acetyl-CoA synthesis. [Biochemistry. 1999]
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Cited by 4 PubMed Central articles

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Structures reported by this article

Mad Crystal Structure Analysis Of Methyltetrahydrofolate: CorrinoidIRON-Sulfur Protein Methyltransferase (Metr)

PDB: 1F6Y

Source: Moorella thermoacetica ATCC 39073

Method: X-Ray Diffraction

Resolution: 2.2 Å

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The reductive acetyl coenzyme A pathway: sequence and heterologous expression of...
The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum.
J Bacteriol. 1994 Oct ;176(19):6127-30.

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