1JC4

Crystal Structure of Se-Met Methylmalonyl-CoA Epimerase

1JC4 の概要

• エントリーDOI: 10.2210/pdb1jc4/pdb
• 関連するPDBエントリー: 1JC5
• 分子名称: Methylmalonyl-CoA epimerase, SULFATE ION (3 entities in total)
• 機能のキーワード: vicinal oxygen chelate superfamily, methylmalonyl-coa, isomerase
• 由来する生物種: Propionibacterium freudenreichii subsp. shermanii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68845.06

構造登録者

Mc Carthy, A.A.,Baker, H.M.,Shewry, S.C.,Patchett, M.L.,Baker, E.N. (登録日: 2001-06-07, 公開日: 2001-07-11, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)