Properties of the membrane-bound 5'-nucleotidase and utilization of extracellular ATP in Vibrio parahaemolyticus.
Vibrio parahaemolyticus utilized ATP, ADP or AMP as the sole source of carbon. About three times higher activity of membrane-bound 5'-nucleotidase was observed in cells grown in the presence of these nucleotides than in their absence: and therefore the enzyme seems to be inducible. Since the 5'-nucleotidase activity could be measured with whole cells, the active site of this enzyme appears to be outwardly oriented. Both Mg2+ and Cl- were required for activity. Among the divalent cations tested, Mn2+ and Co2+ could replace Mg2+ to some extent, whereas Zn2+ strongly inhibited activity. Among the anions tested, Br-, I- and NO3- could replace Cl-, but SO4(2-) and CH3COO- could not. When cells were grown with ATP, Cl- was indispensable and Zn2+ strongly inhibited growth. Therefore, it is concluded that extracellular ATP and other 5'-nucleotides are cleaved by the membrane-bound 5'-nucleotidase outside the cells and that the adenosine produced is then utilized.
Sakai
Y
Y
Department of Microbiology, Okayama University, Japan.
Toda
K
K
Mitani
Y
Y
Tsuda
M
M
Shinoda
S
S
Tsuchiya
T
T
D015720:5'-Nucleotidase; D000244:Adenosine Diphosphate / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D002712:Chlorides / Q000494:pharmacology; D004790:Enzyme Induction; D008274:Magnesium / Q000494:pharmacology; D009708:Nucleotidases / Q000037:antagonists & inhibitors / Q000096:biosynthesis*; D013379:Substrate Specificity; D014733:Vibrio / Q000201:enzymology* / Q000254:growth & development; D015032:Zinc / Q000494:pharmacology
D002712:Chlorides; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D009708:Nucleotidases; D015720:5'-Nucleotidase; D008274:Magnesium; D015032:Zinc