1MAE
The Active Site Structure of Methylamine Dehydrogenase: Hydrazines Identify C6 as the Reactive Site of the Tryptophan Derived Quinone Cofactor
1MAE の概要
| エントリーDOI | 10.2210/pdb1mae/pdb |
| 分子名称 | METHYLAMINE DEHYDROGENASE (LIGHT SUBUNIT), METHYLAMINE DEHYDROGENASE (HEAVY SUBUNIT), NITROGEN MOLECULE, ... (4 entities in total) |
| 機能のキーワード | oxidoreductase(chnh2(d)-deaminating) |
| 由来する生物種 | Paracoccus versutus 詳細 |
| 細胞内の位置 | Periplasm: P22641 P23006 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 51714.18 |
| 構造登録者 | |
| 主引用文献 | Huizinga, E.G.,van Zanten, B.A.,Duine, J.A.,Jongejan, J.A.,Huitema, F.,Wilson, K.S.,Hol, W.G. Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor. Biochemistry, 31:9789-9795, 1992 Cited by PubMed Abstract: To identify the reactive part of the orthoquinone function of the tryptophan-derived cofactor found in methylamine dehydrogenase (MADH), we have determined the crystal structures of MADH from Thiobacillus versutus inhibited by methylhydrazine and (2,2,2-trifluoroethyl)hydrazine. Extra electron density attached to C6 of the tryptophyl tryptophanquinone cofactor shows that this atom and not C7 is the reactive part of the ortho-quinone moiety. The density retained after hydrazine inhibition is much less extensive than expected, however, suggesting that partial breakdown of the inhibitors after reaction with the cofactor may take place. A detailed description is presented of the cofactor environment in an improved model of MADH which now includes information from the recently determined gene sequence of the cofactor-containing subunit [Ubbink, M., van Kleef, M.A.G., Kleinjan, D., Hoitink, C.W.G., Huitema, F., Beintema, J.J., Duine, J.A., & Canters, G.W. (1991) Eur. J. Biochem. 202, 1003-1012]. We hypothesize that Asp76 is responsible for proton abstraction from the alpha-carbon of the substrate during catalysis. PubMed: 1390754DOI: 10.1021/bi00155a036 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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