Identification of the active site serine of hormone-sensitive lipase by site-directed mutagenesis
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چکیده
منابع مشابه
Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis.
Menaquinol-fumarate oxidoreductase of Escherichia coli is a four-subunit membrane-bound complex that catalyzes the final step in anaerobic respiration when fumarate is the terminal electron acceptor. The enzyme is structurally and catalytically similar to succinate dehydrogenase (succinate-ubiquinone oxidoreductase) from both procaryotes and eucaryotes. Both enzymes have been proposed to contai...
متن کاملIdentification of the active site serine in pancreatic cholesterol esterase by chemical modification and site-specific mutagenesis.
Chemical modification and site-specific mutagenesis approaches were used in this study to identify the active site serine residue of pancreatic cholesterol esterase. In the first approach, purified porcine pancreatic cholesterol esterase was covalently modified by incubation with [3H]diisopropylfluorophosphate (DFP). The radiolabeled cholesterol esterase was digested with CNBr, and the peptides...
متن کاملIdentification of the enzymatic active site of tobacco caffeoyl-coenzyme A O-methyltransferase by site-directed mutagenesis.
Animal catechol O-methyltransferases and plant caffeoyl-coenzyme A O-methyltransferases share about 20% sequence identity and display common structural features. The crystallographic structure of rat liver catechol O-methyltransferase was used as a template to construct a homology model for tobacco caffeoyl-coenzyme A O-methyltransferase. Integrating substrate specificity data, the three-dimens...
متن کاملIdentification of the amino acid residues involved in an active site of Escherichia coli ribonuclease H by site-directed mutagenesis.
The amino acid residues essential for the catalytic activity of ribonuclease H (RNase H) from Escherichia coli (E. coli) were identified by site-directed mutagenesis. It has been proposed by computer analysis that E. coli RNase H has homologous amino acid sequence with the RNase H domains of various retroviral reverse transcriptases (RTs) (Johnson, M. S., McClure, M. A., Feng, D. F., Gray, J., ...
متن کاملThe active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis.
Strictly conserved charged residues among polygalacturonases (Asp-180, Asp-201, Asp-202, His-223, Arg-256, and Lys-258) were subjected to site-directed mutagenesis in Aspergillus niger endopolygalacturonase II. Specific activity, product progression, and kinetic parameters (K(m) and V(max)) were determined on polygalacturonic acid for the purified mutated enzymes, and bond cleavage frequencies ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1994
ISSN: 0014-5793
DOI: 10.1016/0014-5793(94)00403-x