Incorporation of an unnatural amino acid in the active site of porcine pancreatic phospholipase A2. Substitution of histidine by 1, 2, 4-triazole-3-alanine yields an enzyme with high activity at acidic pH

Protein Engineering

Volumn 9, Issue 4, 1996, Pages 345-352

  Beiboer, Sigrid H W ^a   Van Den Berg, Bert ^b   Dekker, Niek ^a   Cox, Ruud C ^a   Verheij, Hubertus M ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Enzyme mechanism; Phospholipase A2; Site directed mutagenesis; Unnatural amino acids

Indexed keywords

3 (1,2,4 TRIAZOL 3 YL)ALANINE; ALANINE DERIVATIVE; ASPARAGINE; HISTIDINE; MUTANT PROTEIN; PANCREAS ENZYME; PHOSPHOLIPASE A2; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; COMPETITIVE INHIBITION; CONTROLLED STUDY; COVALENT BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PH; PRIORITY JOURNAL;

ACIDS; ALANINE; ANIMALS; BASE SEQUENCE; BINDING SITES; CALCIUM; ESCHERICHIA COLI; HISTIDINE; HYDROGEN-ION CONCENTRATION; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PANCREAS; PHOSPHOLIPASES A; RECOMBINANT PROTEINS; SWINE;

EID: 0029982453     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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