3ptd: Difference between revisions
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PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D274S
OverviewOverview
The role of amino acid residues located in the active site pocket of, phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus, cereus[Heinz, D. W., Ryan, M., Bullock, T., & Griffith, O. H. (1995) EMBO, J. 14, 3855-3863] was investigated by site-directed mutagenesis, kinetics, and crystal structure analysis. Twelve residues involved in catalysis and, substrate binding (His32, Arg69, His82, Gly83, Lys115, Glu117, Arg163, Trp178, Asp180, Asp198, Tyr200, and Asp274) were individually replaced by, 1-3 other amino acids, resulting in a total number of 21 mutants., Replacements in the mutants H32A, H32L, R69A, R69E, R69K, H82A, H82L, E117K, R163I, D198A, D198E, D198S, Y200S, and D274S caused essentially, complete inactivation of the enzyme. The remaining mutants (G83S, K115E, ... [(full description)]
About this StructureAbout this Structure
3PTD is a [Single protein] structure of sequence from [Bacillus cereus]. Active as [Transferred entry: 4.6.1.13], with EC number [3.1.4.10]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis., Gassler CS, Ryan M, Liu T, Griffith OH, Heinz DW, Biochemistry. 1997 Oct 21;36(42):12802-13. PMID:9335537
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