The nucleotidase of Boophilus microplus and its relationship to enzymes from the rat and Escherichia coli.
Boophilus microplus contains a nucleotidase-like enzyme which is able to hydrolyze a range of nucleoside 5'-mono-, di- and triphosphates to the nucleoside. Its relationship to several other nucleotide hydrolyzing enzymes has been explored. Limited peptide sequencing shows similarities to both mammalian nucleotidases and the Escherichia coli uridine diphosphate sugar hydrolase. The tick enzyme also hydrolyzes UDP-glucose, though by a mechanism different to that of the bacterial enzyme. On the other hand, it resembles the mammalian nucleotidases in that there is evidence that it is attached to the cell membrane by a glycosyl-phosphatidylinositol (GPI) anchor.
CSIRO Division of Tropical Animal Production, Indooroopilly, Queensland, Australia.
P
P
Willadsen
G A
GA
Riding
J
J
Jarmey
A
A
Atkins
D015720:5'-Nucleotidase / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005260:Female; D006868:Hydrolysis; D008969:Molecular Sequence Data; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010727:Phosphoric Diester Hydrolases / Q000494:pharmacology; D051381:Rats; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013379:Substrate Specificity; D013987:Ticks / Q000201:enzymology* / Q000235:genetics*; D014532:Uridine Diphosphate Glucose / Q000378:metabolism
D015720:5'-Nucleotidase; D010727:Phosphoric Diester Hydrolases; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D014532:Uridine Diphosphate Glucose