4GCH

STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN

4GCH の概要

• エントリーDOI: 10.2210/pdb4gch/pdb
• 分子名称: GAMMA-CHYMOTRYPSIN A, 3-(4-DIETHYLAMINO-2-HYDROXY-PHENYL)-2-METHYL-PROPIONIC ACID, ... (5 entities in total)
• 機能のキーワード: hydrolase (serine proteinase)
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space: P00766 P00766 P00766
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 25511.87

構造登録者

Stoddard, B.L.,Ringe, D.,Petsko, G.A. (登録日: 1989-09-25, 公開日: 1990-10-15, 最終更新日: 2024-06-05)

主引用文献

Stoddard, B.L.,Bruhnke, J.,Porter, N.,Ringe, D.,Petsko, G.A.
Structure and activity of two photoreversible cinnamates bound to chymotrypsin.
Biochemistry, 29:4871-4879, 1990

PubMed Abstract: The serine protease gamma-chymotrypsin was covalently inhibited with two different photoreversible cinnamate compounds, and the structures of the resulting complexes were determined to 1.9-A resolution. The inhibitors show different kinetics of binding, inhibition, and nonphotochemical deacylation relative to each other in solution activity assays. The crystal structures of the enzyme-cinnamate complexes show that both compounds acylate serine 195 and that the two molecules are bound in similar nonproductive conformations which have drastic effects on their ability to turn over. Substitution of a diethylamino group on the para position of the cinnamate ring causes a 1000-fold increase in the thermal stability of the inhibitor toward hydrolysis and deacylation.

PubMed: 2364065
DOI: 10.1021/bi00472a017

実験手法

X-RAY DIFFRACTION (1.9 Å)