A molecular orbital study on the effects of substituents on the proton transfer from Ser-195 to His-57 in the hydrolysis of .ALPHA.-chymotrypsin.

• 梅山 秀明

• 今村 詮

• 永田 親義

抄録

From the results of molecular orbital study on the effects of substituents on the proton transfer from Ser-195 to His-57 in the "charge relay system"of α-chymotrypsin, the acylation step is thought to be as follows : (1) the carbonyl carbon of the substrate approaches to the oxygen of Ser-195 in the "charge relay system" ; (2) after the proton of Ser-195 is transferred to N^■2 of His-57 by the trigger of the interaction between the oxygen of Ser-195 and the carbonyl carbon of the substrate, the oxygen of Ser-195 covalent-bonds with the carbonyl carbon of the substrate ; (3) acyl-Ser-195 rotates by 120 degrees around the serine C^α-C^β bond. The rotation of acyl-Ser-195 must be accompanied with the deeper movement of the aromatic part of the substrate in the pocket of α-chymotrypsin. Moreover, it was shown that a significant role in accelerating the proton transfer from Ser-195 to His-57 was played by the interaction between the oxygen of Ser-195 and carbonyl carbon of substrate, not by two hydrogen bonds between the carbonyl oxygen and the backbone-NH-groups of Gly-193 and Ser-195.

収録刊行物

• ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ

  ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ 23 (12), 3045-3055, 1975

  公益社団法人 日本薬学会

キーワード

• Drug Discovery
• General Chemistry
• General Medicine

詳細情報

• CRID: 1390282679150890496
• NII論文ID: 110003621807
• NII書誌ID: AA00602100
• DOI: 10.1248/cpb.23.3045
• COI: 1:CAS:528:DyaE28XntV2ltg%3D%3D
• ISSN: 13475223
• ISSN: 00092363
• PubMed: 1218445
• Web Site: http://www.jstage.jst.go.jp/article/cpb1958/23/12/23_12_3045/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/1977005264
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可