Precorrin-4 C11-methyltransferase

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precorrin-4 C11-methyltransferase
Identifiers
EC no. 2.1.1.133
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In enzymology, a precorrin-4 C11-methyltransferase (EC 2.1.1.133) is an enzyme that catalyzes the chemical reaction

Contents

S-adenosyl-L-methionine + precorrin-4 S-adenosyl-L-homocysteine + precorrin-5

The two substrates of this enzyme are S-adenosyl methionine and precorrin 4; its two products are S-adenosylhomocysteine and precorrin 5.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-4 C11 methyltransferase. Other names in common use include precorrin-3 methylase, and CobM. It is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.

See also

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1CBF and 2CBF.

Related Research Articles

Pseudomonas denitrificans is a Gram-negative aerobic bacterium that performs denitrification. It was first isolated from garden soil in Vienna, Austria. It overproduces cobalamin (vitamin B12), which it uses for methionine synthesis and it has been used for manufacture of the vitamin. Scientists at Rhône-Poulenc Rorer took a genetically engineered strain of the bacteria, in which eight of the cob genes involved in the biosynthesis of the vitamin had been overexpressed, to establish the complete sequence of methylation and other steps in the cobalamin pathway.

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References