Ala160 and His116 residues are involved in activity and specificity of apyrase, an ATP-hydrolysing enzyme produced by enteroinvasive Escherichia coli.

scientific article

Ala160 and His116 residues are involved in activity and specificity of apyrase, an ATP-hydrolysing enzyme produced by enteroinvasive Escherichia coli. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1099/MIC.0.28142-0
P698PubMed publication ID16151198
P5875ResearchGate publication ID7611318

P50authorFederica Del ChiericoQ56479761
Serena SchippaQ58423099
P2093author name stringMauro Nicoletti
Piera Valenti
Francesca Berlutti
Daniela Santapaola
Serena Sarli
P433issuePt 9
P921main subjectEscherichia coliQ25419
P304page(s)2853-2860
P577publication date2005-09-01
P1433published inMicrobiologyQ11339587
P1476titleAla160 and His116 residues are involved in activity and specificity of apyrase, an ATP-hydrolysing enzyme produced by enteroinvasive Escherichia coli
P478volume151

Reverse relations

cites work (P2860)
Q50457351Analysis on the interaction domain of VirG and apyrase by pull-down assay.
Q42069451Apyrase, the product of the virulence plasmid-encoded phoN2 (apy) gene of Shigella flexneri, is necessary for proper unipolar IcsA localization and for efficient intercellular spread.
Q40611568Novel Nucleoside Diphosphatase Contributes to Staphylococcus aureus Virulence
Q35108869Polar localization of PhoN2, a periplasmic virulence-associated factor of Shigella flexneri, is required for proper IcsA exposition at the old bacterial pole

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