ExplorEnz: EC 2.1.1.132

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2.1.1.132

Accepted name:

precorrin-6B C5,15-methyltransferase (decarboxylating)

Reaction:

2 S-adenosyl-L-methionine + precorrin-6B = 2 S-adenosyl-L-homocysteine + precorrin-8X + CO₂ (overall reaction)
(1a) S-adenosyl-L-methionine + precorrin-6B = S-adenosyl-L-homocysteine + precorrin-7 + CO₂
(1b) S-adenosyl-L-methionine + precorrin-7 = S-adenosyl-L-homocysteine + precorrin-8X

For diagram of corrin biosynthesis (part 4), click here

Glossary:

precorrin-6B = precorrin-6Y

Other name(s):

precorrin-6 methyltransferase; precorrin-6Y methylase; precorrin-6Y C^5,15-methyltransferase (decarboxylating); cobL (gene name)

Systematic name:

S-adenosyl-L-methionine:1-precorrin-6B C^5,15-methyltransferase (C-12-decarboxylating)

Comments:

The enzyme participates in the aerobic (late cobalt insertion) adenosylcobalamin biosynthesis pathway. The enzyme from the bacterium Pseudomonas denitrificans is a fusion protein with two active sites; one catalyses the methylation at C-15 followed by decarboxylation of the C-12 acetate side chain, while the other catalyses the methylation at C-5. The corresponding activities in the anaerobic adenosylcobalamin biosynthesis pathway are catalysed by EC 2.1.1.196, cobalt-precorrin-6B (C15)-methyltransferase [decarboxylating], and EC 2.1.1.289, cobalt-precorrin-7 (C5)-methyltransferase, respectively.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 162995-22-4

References:

1.	Blanche, F., Famechon, A., Thibaut, D., Debussche, L., Cameron, B., Crouzet, J. Biosynthesis of vitamin B₁₂ in Pseudomonas denitrificans: the biosynthetic sequence from precorrin-6Y to precorrin-8X is catalyzed by the cobL gene product. J. Bacteriol. 174 (1992) 1050–1052. [DOI] [PMID: 1732195]
2.	Deery, E., Schroeder, S., Lawrence, A.D., Taylor, S.L., Seyedarabi, A., Waterman, J., Wilson, K.S., Brown, D., Geeves, M.A., Howard, M.J., Pickersgill, R.W. and Warren, M.J. An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. Nat. Chem. Biol. 8 (2012) 933–940. [DOI] [PMID: 23042036]

[EC 2.1.1.132 created 1999, modified 2013]