Both acidic and basic amino acids in an amphitropic enzyme, CTP:phosphocholine cytidylyltransferase, dictate its selectivity for anionic membranes

Journal of Biological Chemistry

Volumn 278, Issue 1, 2003, Pages 514-522

  Johnson, Joanne E ^a   Xie, Mingtang ^a   Singh, Laila M R ^a   Edge, Robert ^b   Cornell, Rosemary B ^a  

^a SIMON FRASER UNIVERSITY   (Canada)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ELECTROSTATICS; LIPIDS; MEMBRANES; PROTEINS; SYNTHESIS (CHEMICAL);

INTERFACIAL STRIPS;

ENZYMES;

AMINO ACID; AMPHOLYTE; CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE; CYTIDINE TRIPHOSPHATE; GLUTAMIC ACID; GLUTAMINE; LIPID; LYSINE; PHOSPHATIDYLCHOLINE;

ARTICLE; CELL MEMBRANE; CONTROLLED STUDY; ELECTRICITY; HYDROPHOBICITY; MEMBRANE BINDING; PH; PKA; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; AMINO ACIDS, ACIDIC; AMINO ACIDS, BASIC; ANIMALS; CHOLINE-PHOSPHATE CYTIDYLYLTRANSFERASE; CIRCULAR DICHROISM; COS CELLS; HYDROGEN-ION CONCENTRATION; ISOENZYMES; MEMBRANE LIPIDS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTATION; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; PROTONS; RATS;

INSERTION SEQUENCES;

EID: 0037414807     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M206072200     Document Type: Article

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