1JC4

Crystal Structure of Se-Met Methylmalonyl-CoA Epimerase

Summary for 1JC4

• Entry DOI: 10.2210/pdb1jc4/pdb
• Related: 1JC5
• Descriptor: Methylmalonyl-CoA epimerase, SULFATE ION (3 entities in total)
• Functional Keywords: vicinal oxygen chelate superfamily, methylmalonyl-coa, isomerase
• Biological source: Propionibacterium freudenreichii subsp. shermanii
• Total number of polymer chains: 4
• Total formula weight: 68845.06

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: 2024-10-30)

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 Å)