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Mutation Report for: K492E_ratno-Ces1d

Mode of mutation|Site directed mutagenesis
Amino Acid change|K492E
Torpedo number|467
Comment|No effect on the hydrolysis of PNPC or PNPA, no activity on cholesteryl oleate; when associated with R-186, or with R-186 and T-491. Increases activity on PNPC compared to activity on PNPA; when associated with R-186; I-423 and T- 491.
Kinetic parameters|none

    Title: Mutation of residues 423 (Met/Ile), 444 (Thr/Met), and 506 (Asn/Ser) confer cholesteryl esterase activity on rat lung carboxylesterase. Ser-506 is required for activation by cAMP-dependent protein kinase
    Wallace TJ, Kodsi EM, Langston TB, Gergis MR, Grogan WM
    Ref: Journal of Biological Chemistry, 276:33165, 2001 : PubMed


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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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