1VGR
Formyl-CoA transferase mutant Asp169 to Glu
1VGR の概要
| エントリーDOI | 10.2210/pdb1vgr/pdb |
| 関連するPDBエントリー | 1p5h 1p5r 1t3z 1vgq |
| 分子名称 | Formyl-coenzyme A transferase, COENZYME A (3 entities in total) |
| 機能のキーワード | coa transferase, oxalate, oxalate degradation, intertwined, knotted fold, caib-baif family, coa complex, transferase |
| 由来する生物種 | Oxalobacter formigenes |
| 細胞内の位置 | Cytoplasm: O06644 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 96026.45 |
| 構造登録者 | Ricagno, S.,Jonsson, S.,Richards, N.G.,Lindqvist, Y. (登録日: 2004-04-28, 公開日: 2004-08-03, 最終更新日: 2023-10-25) |
| 主引用文献 | Jonsson, S.,Ricagno, S.,Lindqvist, Y.,Richards, N.G. Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes J.Biol.Chem., 279:36003-36012, 2004 Cited by PubMed Abstract: Oxalobacter formigenes is an obligate anaerobe that colonizes the human gastrointestinal tract and employs oxalate breakdown to generate ATP in a novel process involving the interplay of two coupled enzymes and a membrane-bound oxalate:formate antiporter. Formyl-CoA transferase is a critical enzyme in oxalate-dependent ATP synthesis and is the first Class III CoA-transferase for which a high resolution, three-dimensional structure has been determined (Ricagno, S., Jonsson, S., Richards, N., and Lindqvist, Y. (2003) EMBO J. 22, 3210-3219). We now report the first detailed kinetic characterizations of recombinant, wild type formyl-CoA transferase and a number of site-specific mutants, which suggest that catalysis proceeds via a series of anhydride intermediates. Further evidence for this mechanistic proposal is provided by the x-ray crystallographic observation of an acylenzyme intermediate that is formed when formyl-CoA transferase is incubated with oxalyl-CoA. The catalytic mechanism of formyl-CoA transferase is therefore established and is almost certainly employed by all other members of the Class III CoA-transferase family. PubMed: 15213226DOI: 10.1074/jbc.M404873200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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