1BE6

TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE

1BE6 の概要

• エントリーDOI: 10.2210/pdb1be6/pdb
• 分子名称: SUBTILISIN CARLSBERG, CALCIUM ION, PHENYLETHYLENECARBOXYLIC ACID, ... (5 entities in total)
• 機能のキーワード: serine protease, organic solvent, acyl-enzyme
• 由来する生物種: Bacillus licheniformis
• 細胞内の位置: Secreted: P00780
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27987.06

構造登録者

Schmitke, J.L.,Stern, L.J.,Klibanov, A.M. (登録日: 1998-05-20, 公開日: 1998-10-14, 最終更新日: 2024-10-16)

主引用文献

Schmitke, J.L.,Stern, L.J.,Klibanov, A.M.
Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water.
Proc.Natl.Acad.Sci.USA, 95:12918-12923, 1998

PubMed Abstract: The x-ray crystal structures of trans-cinnamoyl-subtilisin, an acyl-enzyme covalent intermediate of the serine protease subtilisin Carlsberg, have been determined to 2.2-A resolution in anhydrous acetonitrile and in water. The cinnamoyl-subtilisin structures are virtually identical in the two solvents. In addition, their enzyme portions are nearly indistinguishable from previously determined structures of the free enzyme in acetonitrile and in water; thus, acylation in either aqueous or nonaqueous solvent causes no appreciable conformational changes. However, the locations of bound solvent molecules in the active site of the acyl- and free enzyme forms in acetonitrile and in water are distinct. Such differences in the active site solvation may contribute to the observed variations in enzymatic activities. On prolonged exposure to organic solvent or removal of interstitial solvent from the crystal lattice, the channels within enzyme crystals are shown to collapse, leading to a drop in the number of active sites accessible to the substrate. The mechanistic and preparative implications of our findings for enzymatic catalysis in organic solvents are discussed.

PubMed: 9789015
DOI: 10.1073/pnas.95.22.12918

実験手法

X-RAY DIFFRACTION (2.15 Å)