A single amino acid substitution in the pleckstrin homology domain of phospholipase C δ1 enhances the rate of substrate hydrolysis

Journal of Biological Chemistry

Volumn 272, Issue 26, 1997, Pages 16240-16246

  Bromann, Paul A ^a   Boetticher, Evan E ^a   Lomasney, Jon W ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C; PLECKSTRIN;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE; HYDROLYSIS; MICELLE; MICHAELIS CONSTANT; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE HOMOLOGY;

BLOOD PROTEINS; ENZYME ACTIVATION; HUMANS; HYDROLYSIS; INOSITOL 1,4,5-TRISPHOSPHATE; KINETICS; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PHOSPHATIDYLINOSITOLS; PHOSPHOLIPASE C; PHOSPHOPROTEINS; POINT MUTATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0030946066     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.26.16240     Document Type: Article

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