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Identification of catalytically active groups of wheat (Triticum aestivum) germ lipase

Identification of catalytically active groups of wheat (Triticum aestivum) germ lipase The active site of wheat germ lipase was studied by the Dixon method and chemical modification. The profile of curve log V = f(pH), pK and ionization heat values, lipase photoinactivation, and lipase inactivation with diethylpyrocarbonate and dicyclohexylcarbodiimide led us to assume that the active site of the enzyme comprises the carboxylic group of aspartic or glutamic acid and the imidazole group of histidine. Apparently, the OH-group of serine plays a key role in catalysis: as a result of incubation for 1 h in the presence of phenylmethylsulfonyl fluoride, the enzyme activity decreased by more than 70%. It is shown that ethylenediamine tetraacetate is a noncompetitive inhibitor of lipase. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Identification of catalytically active groups of wheat (Triticum aestivum) germ lipase

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References (14)

Publisher
Springer Journals
Copyright
Copyright © 2008 by MAIK Nauka
Subject
Life Sciences; Medical Microbiology ; Microbiology ; Biochemistry, general
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683808040029
Publisher site
See Article on Publisher Site

Abstract

The active site of wheat germ lipase was studied by the Dixon method and chemical modification. The profile of curve log V = f(pH), pK and ionization heat values, lipase photoinactivation, and lipase inactivation with diethylpyrocarbonate and dicyclohexylcarbodiimide led us to assume that the active site of the enzyme comprises the carboxylic group of aspartic or glutamic acid and the imidazole group of histidine. Apparently, the OH-group of serine plays a key role in catalysis: as a result of incubation for 1 h in the presence of phenylmethylsulfonyl fluoride, the enzyme activity decreased by more than 70%. It is shown that ethylenediamine tetraacetate is a noncompetitive inhibitor of lipase.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Jul 12, 2008

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