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1YAS

HYDROXYNITRILE LYASE COMPLEXED WITH HISTIDINE

1YAS の概要
エントリーDOI10.2210/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
Wagner, U.G.,Kratky, C. (登録日: 1996-05-15, 公開日: 1997-06-16, 最終更新日: 2024-02-14)
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: 8805565
DOI: 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)
構造検証レポート
Validation report summary of 1yas
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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