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

Journal of Biological Chemistry

Volumn 276, Issue 35, 2001, Pages 33165-33174

  Wallace, Timothy J ^a   Kodsi, Ehab M ^a   Langston, Timothy B ^a   Gergis, Mervat R ^a   Grogan, William M ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; ENZYMES; MUTAGENESIS; X RAY ANALYSIS;

MUTATIONS;

BIOCHEMISTRY;

ASPARAGINE; CARBOXYLESTERASE; CHOLESTEROL ESTERASE; CYCLIC AMP DEPENDENT PROTEIN KINASE; ISOLEUCINE; METHIONINE; OCTANOIC ACID DERIVATIVE; PHENYLACETIC ACID DERIVATIVE; SERINE; THREONINE; ACETYLCHOLINESTERASE; COMPLEMENTARY DNA; RECOMBINANT PROTEIN;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; GENE MUTATION; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT; SITE DIRECTED MUTAGENESIS; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CYTOSOL; ENZYMOLOGY; HUMAN; LIVER; LUNG; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

ACETYLCHOLINESTERASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ASPARAGINE; CARBOXYLESTERASE; CARBOXYLIC ESTER HYDROLASES; CHOLESTEROL ESTERASE; CLONING, MOLECULAR; CYCLIC AMP-DEPENDENT PROTEIN KINASES; CYTOSOL; DNA, COMPLEMENTARY; ENZYME ACTIVATION; HUMANS; ISOLEUCINE; LIVER; LUNG; METHIONINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN STRUCTURE, SECONDARY; RATS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SERINE; THREONINE;

EID: 0035980020     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M105644200     Document Type: Article

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