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Literature summary extracted from

  • Kozakiewicz, A.; Neumann, P.; Banach, M.; Komoszy?ski, M.; Wojtczak, A.
    Modeling studies of potato nucleoside triphosphate diphosphohydrolase NTPDase1: an insight into the catalytic mechanism (2008), Acta Biochim. Pol., 55, 141-150.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.5 additional information mutational analysis of residues involved in catalysis, overview Solanum tuberosum

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.5 Solanum tuberosum
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.5 additional information identification of the amino acids interacting with the nucleoside triphosphate substrate and probably involved in the catalyzed hydrolysis. The mixed two-step catalytic mechanism of hydrolysis involves Thr127 and Thr55 as potential nucleophilic factors responsible for the cleavage of the Pgamma and Pbeta anhydride bonds, respectively. Their is assisted by Glu170 and Glu78 residues, respectively, detailed overview Solanum tuberosum ?
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 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.5 More identification of ACR regions in residues 40-454 possibly involved in metal binding, sequence comparison, and structure analysis and modeling, overview Solanum tuberosum

Synonyms

EC Number Synonyms Comment Organism
3.6.1.5 Apyrase
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 Solanum tuberosum
3.6.1.5 More apyrase belongs to the actin superfamily of proteins and is a member of the NTPDase family Solanum tuberosum
3.6.1.5 NTPDase1
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 Solanum tuberosum
3.6.1.5 nucleoside triphosphate diphosphohydrolase
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 Solanum tuberosum