Ala 160 and His116 residues are involved in activity and specificity of apyrase, an ATP-hydrolysing enzyme produced by enteroinvasive Escherichia coli

Microbiology

Volumn 151, Issue 9, 2005, Pages 2853-2860

  Sarli, Serena ^a   Nicoletti, Mauro ^b   Schippa, Serena ^a   Del Chierico, Federica ^a   Santapaola, Daniela ^b   Valenti, Piera ^c   Berlutti, Francesca ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b UNIVERSITY OF CHIETI   (Italy)

^c SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL PHOSPHATE; ACID PHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; APYRASE; ARGININE; HISTIDINE; SERINE; THREONINE; VIRULENCE FACTOR;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL VIRULENCE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PLASMID; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; SHIGELLA; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; PATHOGENICITY;

ESCHERICHIA COLI; SHIGELLA;

ADENOSINE TRIPHOSPHATE; ALANINE; APYRASE; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; HISTIDINE; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; SUBSTRATE SPECIFICITY; VIRULENCE FACTORS;

EID: 24944458212     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.28142-0     Document Type: Article

References (23)

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