1REQ

METHYLMALONYL-COA MUTASE

Summary for 1REQ

• Entry DOI: 10.2210/pdb1req/pdb
• Descriptor: METHYLMALONYL-COA MUTASE, COBALAMIN, DESULFO-COENZYME A, ... (6 entities in total)
• Functional Keywords: isomerase, mutase, intramolecular transferase
• Biological source: Propionibacterium freudenreichii subsp. shermanii; More
• Total number of polymer chains: 4
• Total formula weight: 304096.58

Authors

Evans, P.R.,Mancia, F. (deposition date: 1996-01-19, release date: 1997-01-27, Last modification date: 2024-02-14)

Primary citation

Mancia, F.,Keep, N.H.,Nakagawa, A.,Leadlay, P.F.,McSweeney, S.,Rasmussen, B.,Bosecke, P.,Diat, O.,Evans, P.R.
How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution.
Structure, 4:339-350, 1996

PubMed Abstract: The enzyme methylmalonyl-coenzyme A (CoA) mutase, an alphabeta heterodimer of 150 kDa, is a member of a class of enzymes that uses coenzyme B12 (adenosylcobalamin) as a cofactor. The enzyme induces the formation of an adenosyl radical from the cofactor. This radical then initiates a free-radical rearrangement of its substrate, succinyl-CoA, to methylmalonyl-CoA.

PubMed: 8805541
DOI: 10.1016/S0969-2126(96)00037-8

Experimental method

X-RAY DIFFRACTION (2 Å)