Productive and nonproductive substrate binding in enzyme mimics

Lele, B. S. ; Kulkarni, M. G. ; Mashelkar, R. A. (1999) Productive and nonproductive substrate binding in enzyme mimics Polymer, 40 (14). pp. 4063-4070. ISSN 0032-3861

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Hydrolytic activity of molecularly imprinted polymeric mimics of chymotrypsin was evaluated against N-acetyl tyrosyl para nitrophenyl ester and N-benzoyl tyrosyl para nitrophenyl ester, respectively. The mimic grafted on hydrophilic support exhibited high kcat and high Km values for N-acetyl tyrosyl para nitrophenyl ester. But, for N-benzoyl tyrosyl para nitrophenyl ester, the mimic exhibited low kcat as well as low Km values, consistent with the nonproductive binding exhibited by natural chymotrypsin for hydrophobic substrate. The same mimic when grafted on hydrophobic support exhibited trends consistent with Michaelis-Menten kinetics and also higher catalytic activity than that exhibited by the mimic on hydrophilic support. Thus in the case of mimics nonproductive substrate binding could be eliminated by the choice of appropriate support. This helped to enhance the mimic activity towards a specific substrate. This discretion is not available in the case of native enzyme.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Chymotrypsin Mimic; Substrate Binding; Hydrophobic Support
ID Code:17071
Deposited On:16 Nov 2010 08:34
Last Modified:04 Jun 2011 08:22

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