Purification and Cloning of a Soluble ATP-Diphosphohydrolase (Apyrase) from Potato Tubers (Solanum tuberosum)

A soluble ATP-diphosphohydrolase (apyrase, EC 3.6.1.5) has been purified from potato tubers,Solanum tuberosum,to a specific activity of 10,000 μmol Pi/mg/min. The cDNA corresponding to the potato apyrase has been isolated and termed RROP1. The deduced amino acid sequence contains a putative signal s...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1996-01, Vol.218 (3), p.916-923
Main Authors: Handa, Masahisa, Guidotti, Guido
Format: Article
Language:English
Subjects:
ADN
Amino Acid Sequence
Animals
Apyrase - genetics
Apyrase - isolation & purification
Base Sequence
CLONACION
CLONAGE
Cloning, Molecular
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
DNA, Complementary - genetics
EVOLUCION
EVOLUTION
HIDROLASAS
Humans
HYDROLASE
Mice
Molecular Sequence Data
PURIFICACION
PURIFICATION
SECUENCIA NUCLEICA
Sequence Alignment
Sequence Homology, Amino Acid
SEQUENCE NUCLEIQUE
SOLANUM TUBEROSUM
Solanum tuberosum - enzymology
TUBERCULE
TUBERCULO
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Description
Summary:A soluble ATP-diphosphohydrolase (apyrase, EC 3.6.1.5) has been purified from potato tubers,Solanum tuberosum,to a specific activity of 10,000 μmol Pi/mg/min. The cDNA corresponding to the potato apyrase has been isolated and termed RROP1. The deduced amino acid sequence contains a putative signal sequence, two hydrophobic regions at the carboxy terminus, two potential Asn-linked glycosylation sites, and four regions in the amino-terminal half that we term ACR (apyrase conserved regions) 1–4 that are highly conserved in known apyrases and related enzymes: garden pea nucleoside triphosphatase,Toxoplasma gondiinucleoside triphosphate hydrolases, andSaccharomyces cerevisiaegolgi guanosine diphosphatase. A yeast 71.9-kDa hypothetical protein on chromosome V, aCaenorhabditis eleganshypothetical 61.3-kDa protein on chromosome III, and human CD39, a lymphoid cell activation antigen, also share the conserved ACR regions, but their ability to hydrolyze nucleotides has not been assessed.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.0162