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. 1986 Dec;168(3):1372–1377. doi: 10.1128/jb.168.3.1372-1377.1986

Purification and properties of the 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanobacterium thermoautotrophicum.

A A DiMarco, M I Donnelly, R S Wolfe
PMCID: PMC213648  PMID: 3782039

Abstract

The 5,10-methenyltetrahydromethanopterin cyclohydrolase of Methanobacterium thermoautotrophicum was purified 128-fold to homogeneity. The enzyme had a subunit Mr of 41,000 as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. From high-performance size exclusion chromatography of the native protein, an Mr of 82,000 was determined, suggesting a dimer of identical subunits. The enzyme was inhibited by 10-formyltetrahydromethanopterin and stimulated by Mg2+. Evaluation of the reaction equilibrium indicated that the methenyl derivative was favored over 5-formyltetrahydromethanopterin, with a much higher equilibrium constant than for the analogous reaction of tetrahydrofolate derivatives. Folate derivatives did not serve as substrates for this enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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