CMP-N-acetylneuraminic acid synthetase from Escherichia coli K1 is a bifunctional enzyme: Identification of minimal catalytic domain for synthetase activity and novel functional domain for platelet-activating factor acetylhydrolase activity

Journal of Biological Chemistry

Volumn 279, Issue 17, 2004, Pages 17738-17749

  Liu, Guangchao ^a   Jin, Chunsheng ^a   Jin, Cheng ^a  

^a INSTITUTE OF MICROBIOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BRAIN; CATALYSTS; ENZYMES; ESCHERICHIA COLI; FUNCTIONS;

BOVINE BRAIN; CATALYTIC DOMAINS; SECONDARY STRUCTURES; TERTIARY STRUCTURES;

BIOCHEMISTRY;

1 ALKYL 2 ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE; ACYLNEURAMINATE CYTIDYLYLTRANSFERASE; AMINO ACID;

ALPHA CHAIN; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BLOOD BRAIN BARRIER; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; ESCHERICHIA COLI K 12; GENE DELETION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

1-ALKYL-2-ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BLOOD-BRAIN BARRIER; BRAIN; CATALYTIC DOMAIN; CATTLE; CHROMATOGRAPHY, THIN LAYER; CLONING, MOLECULAR; CONSERVED SEQUENCE; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GENE DELETION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; N-ACYLNEURAMINATE CYTIDYLYLTRANSFERASE; PLASMIDS; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; SERINE; SOFTWARE; SUBSTRATE SPECIFICITY; TEMPERATURE; TIME FACTORS; TRYPSIN;

BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI; ESCHERICHIA COLI K12; NEGIBACTERIA;

EID: 2342441924     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M400143200     Document Type: Article

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