Structure function relationships in milk-clotting enzymes: pepsin: a model

Numerous studies examining functionality on a mechanistic level of food-related proteins have recently been undertaken using genetic engineering techniques. Research in our laboratory has concentrated on the genetic engineering of pepsin, a milk-clotting enzyme which belongs to aspartic proteinases,...

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Bibliographic Details
Main Authors Yada, R.Y. (University of Guelph, Guleph, Ontario, Canada), Tanaka, T
Format Book
LanguageEnglish
Published Washington, DC (USA) American Chemical Society 1998
Subjects
GENETIC ENGINEERING
GENIE GENETIQUE
INGENIERIA GENETICA
PEPSIN
PEPSINA
PEPSINE
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Summary:Numerous studies examining functionality on a mechanistic level of food-related proteins have recently been undertaken using genetic engineering techniques. Research in our laboratory has concentrated on the genetic engineering of pepsin, a milk-clotting enzyme which belongs to aspartic proteinases, in order to determine the role of specific amino acids/regions of pepsin, and its zymogen, pepsinogen, on structure and catalytic activity. Results from these studies indicated that site-directed mutagenesis of regions both adjacent (e.g., flap loop region) and remote (e.g., prosegment of the zymogen, surface of the enzyme) to the active site were critical to catalytic parameters and were reflected in structural changes as determined by circular dichroism and molecular modelling. Information gleaned from such studies may allow us to redesign enzymes, as well as other food-related proteins, for a particular function and/or environment in a predictable manner
Bibliography:Q02
1997091633
ISBN:9780841235847
0841235848