The antibacterial properties of secreted phospholipases A2: A major physiological role for the group IIA enzyme that depends on the very high pI of the enzyme to allow penetration of the bacterial cell wall

Journal of Biological Chemistry

Volumn 277, Issue 3, 2002, Pages 1788-1793

  Beers, Stephen A ^a   Buckland, Andrew G ^b   Koduri, Rao S ^a   Cho, Wonhwa ^a   Gelb, Michael H ^b   Wilton, David C ^a,c  

^a UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

^b UNIVERSITY OF WASHINGTON   (United States)

^c UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLOGICAL MEMBRANES; CELLS; HYDROLYSIS; MUTAGENESIS;

CATIONIC RESIDUES;

ENZYMES;

PHOSPHOLIPASE A2;

ANTIBACTERIAL ACTIVITY; ARTICLE; BACTERIAL CELL WALL; BACTERICIDAL ACTIVITY; BACTERIUM MUTANT; CELL MEMBRANE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME RELEASE; ENZYME SPECIFICITY; GRAM POSITIVE BACTERIUM; HYDROLYSIS; LISTERIA INNOCUA; MICROCOCCUS LUTEUS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN TRANSPORT; STAPHYLOCOCCUS AUREUS;

ANTI-BACTERIAL AGENTS; CELL WALL; GRAM-POSITIVE BACTERIA; HUMANS; HYDROLYSIS; ISOELECTRIC POINT; PHOSPHOLIPASES A; PROTEIN TRANSPORT;

BACTERIA (MICROORGANISMS); LISTERIA; LISTERIA INNOCUA; MICROCOCCUS; MICROCOCCUS LUTEUS; POSIBACTERIA; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS;

EID: 0037127316     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M109777200     Document Type: Article

References (34)