The catalytic role of aspartate in a short strong hydrogen bond of the Asp274-His32 catalytic dyad in phosphatidylinositol- specific phospholipase C can be substituted by a chloride ion

Journal of Biological Chemistry

Volumn 279, Issue 31, 2004, Pages 31995-32000

  Zhao, Li ^a   Liao, Hua ^a,c   Tsai, Ming Daw ^a,b  

^a OHIO STATE UNIVERSITY   (United States)

^b GENOMICS RESEARCH CENTER   (Taiwan)

^c MILLENNIUM PHARMACEUTICALS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLATION; CATALYSIS; ENZYMES; HYDROGEN BONDS; OXYGEN; PHOSPHORUS;

CARBOXYLATE SIDE CHAIN; CLEAVAGE;

AMINO ACIDS;

ANION; ASPARTIC ACID; CHLORIDE ION; HISTIDINE; OXYGEN; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE C; PHOSPHORUS;

ARTICLE; BACILLUS THURINGIENSIS; CATALYSIS; CATALYST; CHEMICAL BOND; HYDROGEN BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL;

ANIONS; ASPARTIC ACID; BACILLUS THURINGIENSIS; BINDING SITES; CATALYSIS; CHLORIDES; DOSE-RESPONSE RELATIONSHIP, DRUG; HISTIDINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; IONS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MODELS, MOLECULAR; MONTE CARLO METHOD; MUTATION; NORMAL DISTRIBUTION; PHOSPHATIDYLINOSITOL DIACYLGLYCEROL-LYASE; STRUCTURE-ACTIVITY RELATIONSHIP;

BACILLUS THURINGIENSIS; BACTERIA (MICROORGANISMS);

EID: 3543039982     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M404184200     Document Type: Article

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