1JC5

Crystal Structure of Native Methylmalonyl-CoA Epimerase

Summary for 1JC5

• Entry DOI: 10.2210/pdb1jc5/pdb
• Related: 1JC4
• Descriptor: Methylmalonyl-CoA Epimerase, SULFATE ION (3 entities in total)
• Functional Keywords: epimerisation, methylmalonyl-coa, vicinal oxygen chelate superfamily, metal-assisted catalysis, isomerase
• Biological source: Propionibacterium freudenreichii subsp. shermanii
• Total number of polymer chains: 6
• Total formula weight: 101394.08

Authors

Mc Carthy, A.A.,Baker, H.M.,Shewry, S.C.,Patchett, M.L.,Baker, E.N. (deposition date: 2001-06-07, release date: 2001-07-11, Last modification date: 2024-02-07)

Primary citation

McCarthy, A.A.,Baker, H.M.,Shewry, S.C.,Patchett, M.L.,Baker, E.N.
Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: a novel enzymatic function on an ancient metal binding scaffold.
Structure, 9:637-646, 2001

PubMed Abstract: Methylmalonyl-CoA epimerase (MMCE) is an essential enzyme in the breakdown of odd-numbered fatty acids and of the amino acids valine, isoleucine, and methionine. Present in many bacteria and in animals, it catalyzes the conversion of (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, the substrate for the B12-dependent enzyme, methylmalonyl-CoA mutase. Defects in this pathway can result in severe acidosis and cause damage to the central nervous system in humans.

PubMed: 11470438
DOI: 10.1016/S0969-2126(01)00622-0

Experimental method

X-RAY DIFFRACTION (2.2 Å)