1PJC
L-ALANINE DEHYDROGENASE COMPLEXED WITH NAD
1PJC の概要
エントリーDOI | 10.2210/pdb1pjc/pdb |
分子名称 | PROTEIN (L-ALANINE DEHYDROGENASE), NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
機能のキーワード | oxidoreductase, nad |
由来する生物種 | Phormidium lapideum |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 39255.69 |
構造登録者 | Baker, P.J.,Sawa, Y.,Shibata, H.,Sedelnikova, S.E.,Rice, D.W. (登録日: 1998-06-05, 公開日: 1999-07-15, 最終更新日: 2023-12-27) |
主引用文献 | Baker, P.J.,Sawa, Y.,Shibata, H.,Sedelnikova, S.E.,Rice, D.W. Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. Nat.Struct.Biol., 5:561-567, 1998 Cited by PubMed Abstract: The structure of the hexameric L-alanine dehydrogenase from Phormidium lapideum reveals that the subunit is constructed from two domains, each having the common dinucleotide binding fold. Despite there being no sequence similarity, the fold of alanine dehydrogenase is closely related to that of the family of D-2-hydroxyacid dehydrogenases, with a similar location of the active site, suggesting that these enzymes are related by divergent evolution. L-alanine dehydrogenase and the 2-hydroxyacid dehydrogenases also use equivalent functional groups to promote substrate recognition and catalysis. However, they are arranged differently on the enzyme surface, which has the effect of directing opposite faces of the keto acid to the dinucleotide in each case, forcing a change in absolute configuration of the product. PubMed: 9665169DOI: 10.1038/817 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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