1YAS
HYDROXYNITRILE LYASE COMPLEXED WITH HISTIDINE
1YAS の概要
| エントリーDOI | 10.2210/pdb1yas/pdb |
| 分子名称 | HYDROXYNITRILE LYASE, SULFATE ION, HISTIDINE, ... (4 entities in total) |
| 機能のキーワード | oxynitrilase, cyanogenesis, cyanhydrin formation, lyase, complex (lyase-peptide), complex (lyase-peptide) complex, complex (lyase/peptide) |
| 由来する生物種 | Hevea brasiliensis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 29514.82 |
| 構造登録者 | |
| 主引用文献 | Wagner, U.G.,Hasslacher, M.,Griengl, H.,Schwab, H.,Kratky, C. Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure, 4:811-822, 1996 Cited by PubMed Abstract: Over three thousand species of plants, including important food crops such as cassava, use cyanogenesis, the liberation of HCN upon tissue damage, as a defense against predation. Detoxification of cyanogenic food crops requires disruption of the cyanogenic pathway. Hydroxynitrile lyase is one of the key enzymes in cyanogenesis, catalyzing the decomposition of an alpha-cyanohydrin to form HCN plus the corresponding aldehyde or ketone. These enzymes are also of potential utility for industrial syntheses of optically pure chiral cyanohydrins, being used to catalyze the reverse reaction. We set out to gain insight into the catalytic mechanism of this important class of enzymes by determining the three-dimensional structure of hydroxynitrile lyase from the rubber tree, Hevea brasiliensis. PubMed: 8805565DOI: 10.1016/S0969-2126(96)00088-3 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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