Substrate efflux propensity plays a key role in the specificity of secretory A-type phospholipases

Journal of Biological Chemistry

Volumn 285, Issue 1, 2010, Pages 751-760

  Haimi, Perttu ^a   Hermansson, Martin ^a   Batchu, Krishna Chaithanya ^a   Virtanen, Jorma A ^a   Somerharju, Pentti ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACYL CHAIN; BI-LAYER; DOUBLE BOND POSITIONS; HIGH THROUGHPUT; KEY ATTRIBUTES; LIPID EFFLUX; PHOSPHOLIPASES; PHOSPHOLIPID SUBSTRATE; POSITIONAL ISOMERS; RATE LIMITING; SUBSTRATE SPECIFICITY; SUBSTRATE-BINDING SITES;

BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; CHAIN LENGTH; ENZYMES; HYDROLYSIS; ISOMERS; MICELLES; PHOSPHOLIPIDS;

SUBSTRATES;

PHOSPHOLIPASE A;

ARTICLE; BILAYER MEMBRANE; BINDING SITE; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HOMEOSTASIS; HYDROLYSIS; MASS SPECTROMETRY; MEMBRANE VESICLE; MICELLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN TRANSPORT;

ANIMALS; GLUCOSIDES; HIGH-THROUGHPUT SCREENING ASSAYS; HYDROLYSIS; LIPID BILAYERS; MASS SPECTROMETRY; MICELLES; PHOSPHATIDYLCHOLINES; PHOSPHOLIPASES A; SUBSTRATE SPECIFICITY; SUS SCROFA; UNILAMELLAR LIPOSOMES;

EID: 73649118839     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.061218     Document Type: Article

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