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Fersht, A. (1999) Structure and mechanism in protein science: A guide to enzyme catalysis and protein folding. W. H. Freeman and Company, New York.

has been cited by the following article:

• TITLE: How can aprotic ionic liquids affect enzymatic enantioselectivity?

  AUTHORS: Hidetaka Noritomi, Hideki Chiba, Manabu Kikuta, Satoru Kato

  KEYWORDS: α-Chymotrypsin; Enantioselectivity; Esterification; Aprotic Ionic Liquid

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.6 No.10, October 8, 2013

  ABSTRACT: The enantioselectivity of α-chymotrypsin in the esterification of N-acetyl-tryptophan with ethanol was examined in aprotic ionic liquids. The enantioselectivity was found to be strongly affected by a kind of solvent, water content, and reaction temperature. The (kcatKM)L/(kcat/KM)D ratio in 1-ethyl-3-methylimidazolium bis(fluorosulfonyl)imide ([C2mim][FSI]) containing 1.0% (v/v) water at 25°C exhibits 32,000, while that in 1-ethyl-3-methylimidazolium tetrafluoroborate ([C2mim][BF4]) containing 1.0% (v/v) water at 25°C shows 190. The (kcat/KM)L/(kcat/KM)D ratio in [C2mim] [BF4] at 25°C varies from 190 at 1.0% (v/v) water to 65000 at 5.0% (v/v) water. Moreover, the (kcat/KM)L/ (kcat/KM)