Download Food Enzymes: Structure and Mechanism by Dominic W.S. Wong PDF
By Dominic W.S. Wong
Food Enzymes: constitution and Mechanism is the 1st quantity to collect present details at the buildings and mechanisms of vital nutrients enzymes. It offers an in-depth dialogue of the dynamic facets of enzyme buildings and their courting to the chemistry of catalysis. The booklet emphasizes features of the chemistry of enzyme constitution and mechanism seldom lined within the nutrition technological know-how literature. It incorporates a thorough dialogue of the genetic amendment of enzyme buildings and features just about particular foodstuff enzymes. greater than a hundred illustrations improve the readability of significant recommendations. entire references mirror the present kingdom of information on enzyme actions.
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Extra resources for Food Enzymes: Structure and Mechanism
Sample text
Thiolsubtilisin exhibits a large reduction in activity towards nonnal amide and especially ester substrates mainly because of a decreased rate in the acylation step (Neet and Koshland 1966). Interestingly enough, it has been demonstrated recently that thiolsubtilisin exhibits a shift in the preference for ammonolysis over hydrolysis of the acyl-enzyme intennediate (Abrahmsen et al. 1991; Nakatsuka et al. 1987). This unique property has been utilized in the synthesis of peptides in which the enzyme is acylated by a peptide segment of activated ester to fonn an acyl-enzyme intennediate that is then deacylated by the nucleophilic attack of the amino group of another peptide (Nakatsuka et al.
111,9261-9262. IVERSON, B. , and LERNER, R. A. 1989. Sequence-specific peptide cleavage catalyzed by an antibody. Science 243, 1184--1188. JACKSON, D. ; JACOBS, J. ; REICH, S. ; BARLETT, P. ; and SCHULTZ, P. G. 1988. An antibody-catalyzed Claisen rearrangement. J. Am. Chem. Soc. 110,4841-4842. JANDA, K. D. 1994. Tagged versus untagged libraries: Methods for the generation and screening of combinatorial chemical libraries. Proc. Nat!. Acad. Sci. USA 91, 10779-10785. JANDA, K. ; BENKOVIC, S. ; and LERNER, R.
1991). Phospholipase A2 of porcine pancreas consists of an interface recognition (binding) site around the entrance of an active site cleft that is composed of the N-terminal helix and loop 62-72. The snake venom enzyme, lacking several residues in the loop, shows a higher activity and affinity for phospholipid micelles. Deletion of residues 62-66 in the porcine phospholipase A2 and mutation of Asp56->Ser, Ser60->Gly, and Asn67->Tyr in the same loop, results in a snake venom enzyme-like surface loop.