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Literature summary for 3.6.1.9 extracted from

  • Zalatan, J.G.; Fenn, T.D.; Brunger, A.T.; Herschlag, D.
    Structural and functional comparisons of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implications for mechanism and evolution (2006), Biochemistry, 45, 9788-9803.
    View publication on PubMed
Search for more literature for 3.6.1.9

Crystallization (Commentary)

Crystallization (Comment) Organism
in absence of ligands and in complex with vanadate or AMP. Comparison of bimetallo active site with Escherichia coli alkaline phosphatase Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information substrate methyl 4-nitrophenyl phosphate, KM-value greater than 2 mM, substrate bis-4-nitrophenyl phosphate, KM-value greater than 1 mM Mus musculus
0.11
-
 p-nitrophenyl 5'-thymidine monophosphate 25°C, pH 8.0 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate dianion + H2O
-
 Mus musculus 4-nitrophenol + phosphate
-
 ?
4-nitrophenyl phosphate monoanion + H2O 72fold higher activity than with 4-nitrophenyl phosphate dianion Mus musculus 4-nitrophenol + phosphate
-
 ?
bis-4-nitrophenyl phosphate + H2O 2000fold higher activity than with 4-nitrophenyl phosphate dianion Mus musculus 4-nitrophenol + phosphate
-
 ?
methyl 4-nitrophenyl phosphate + H2O 200fold higher activity than with 4-nitrophenyl phosphate dianion Mus musculus 4-nitrophenol + methyl phosphate
-
 ?
p-nitrophenyl 5'-thymidine monophosphate + H2O 1500000fold higher activity than with 4-nitrophenyl phosphate dianion Mus musculus 4-nitrophenol + TMP
-
 ?