The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad

Biochemistry

Volumn 42, Issue 22, 2003, Pages 6696-6708

  Rydel, Timothy J ^a   Williams, Jennifer M ^a   Krieger, Elysia ^a   Moshiri, Farhad ^a   Stallings, William C ^b   Brown, Sherri M ^a   Pershing, Jay C ^a   Purcell, John P ^a   Alibhai, Murtaza F ^a  

^a MONSANTO COMPANY   (United States)

^b PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CRYSTAL STRUCTURE; DISPERSIONS; X RAY ANALYSIS;

MULTIWAVELENGTH ANOMALOUS DISPERSIONS (MAD);

LIPIDS;

ALANINE; ASPARTIC ACID; HYDROLASE; LIPID ACYL HYDROLASE; PATATIN; PHOSPHOLIPASE A2; SERINE; UNCLASSIFIED DRUG; WATER;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; CYTOSOL; DISPERSION; DRUG ACTIVITY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; INSECTICIDAL ACTIVITY; MUTAGENESIS; POTATO; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

ALANINE; AMINO ACID SUBSTITUTION; ANIMALS; ASPARTIC ACID; BEETLES; CARBOXYLIC ESTER HYDROLASES; CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; HUMANS; ISOENZYMES; LARVA; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHOLIPASES A; PICHIA; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY; SERINE;

SOLANUM TUBEROSUM; ZEA MAYS;

EID: 0037984885     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027156r     Document Type: Article

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