Escherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer

Journal of Biological Chemistry

Volumn 272, Issue 39, 1997, Pages 24176-24182

  Badola, Prakash ^a   Sanders II, Charles R ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; DIACYLGLYCEROL KINASE; MEMBRANE ENZYME; PHOSPHATE;

ARTICLE; CATALYST; CELL MEMBRANE; DIFFUSION; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; ESCHERICHIA COLI; EVOLUTION; MICELLE; NONHUMAN; PHOSPHATE TRANSPORT; PRIORITY JOURNAL;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; CATALYSIS; DIACYLGLYCEROL KINASE; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; KINETICS; MOLECULAR SEQUENCE DATA; ORGANOPHOSPHORUS COMPOUNDS; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI; FELIS CATUS;

EID: 0030859453     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.39.24176     Document Type: Article

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