1LLO

HEVAMINE A (A PLANT ENDOCHITINASE/LYSOZYME) COMPLEXED WITH ALLOSAMIDIN

1LLO の概要

• エントリーDOI: 10.2210/pdb1llo/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000468
• 分子名称: Hevamine-A, 2-acetamido-2-deoxy-beta-D-allopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-allopyranose, ALLOSAMIZOLINE, ... (4 entities in total)
• 機能のキーワード: chitinase, lysozyme, hydrolase
• 由来する生物種: Hevea brasiliensis (rubber tree)
• 細胞内の位置: Vacuole: P23472
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30213.82

構造登録者

Terwisscha Van Scheltinga, A.C.,Armand, S.,Kalk, K.H.,Isogai, A.,Henrissat, B.,Dijkstra, B.W. (登録日: 1995-11-08, 公開日: 1996-03-08, 最終更新日: 2024-10-30)

主引用文献

Terwisscha van Scheltinga, A.C.,Armand, S.,Kalk, K.H.,Isogai, A.,Henrissat, B.,Dijkstra, B.W.
Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis.
Biochemistry, 34:15619-15623, 1995

PubMed Abstract: The plant enzyme hevamine has both chitinase and lysozyme activity. HPLC analysis of the products of the hydrolysis of chitopentaose shows that hevamine acts with retention of the configuration, despite the absence of a nucleophilic or stabilizing carboxylate. To analyze the stabilization of a putative oxocarbonium ion intermediate, the X-ray structure of hevamine complexed with the inhibitor allosamidin was determined at 1.85 A resolution. This structure supports the role of Glu127 as a proton donor. The allosamizoline group binds in the center of the active site, mimicking a reaction intermediate in which a positive charge at C1 is stabilized intramolecularly by the carbonyl oxygen of the N-acetyl group at C2.

PubMed: 7495789
DOI: 10.1021/bi00048a003

実験手法

X-RAY DIFFRACTION (1.85 Å)