Structure and function of SirC from Bacillus megaterium: a metal-binding precorrin-2 dehydrogenase

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Structure and function of SirC from Bacillus megaterium: a metal-binding precorrin-2 dehydrogenase.

In Bacillus megaterium, the synthesis of vitamin B(12) (cobalamin) and sirohaem diverges at sirohydrochlorin along the branched modified tetrapyrrole biosynthetic pathway. This key intermediate is made by the action of SirC, a precorrin-2 dehydrogenase that requires NAD(+) as a cofactor. The structure of SirC has now been solved by X-ray crystallography to 2.8 A (1 A = 0.1 nm) resolution. The p...

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Production of cobalamin and sirohaem in Bacillus megaterium: an investigation into the role of the branchpoint chelatases sirohydrochlorin ferrochelatase (SirB) and sirohydrochlorin cobalt chelatase (CbiX)

One of the four operons required for cobalamin biosynthesis in Bacillus megaterium is also associated with sirohaem synthesis, and contains three genes, sirA, sirB and sirC. By undertaking functional complementation experiments and in nitro assays using recombinantly produced enzymes, we have been able to demonstrate that (1) SirA acts as a uroporphyrinogen I I1 methyltransferase, transforming ...

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Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium.

In Bacillus megaterium, the hemAXBCDL genes were isolated and were found to be highly similar to the genes from Bacillus subtilis that are required for the conversion of glutamyl-tRNA into uroporphyrinogen III. Overproduction and purification of HemC (porphobilinogen deaminase) and -D (uroporphyrinogen III synthase) allowed these enzymes to be used for the in vitro synthesis of uroporphyrinogen...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2008

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj20080785