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Literature summary for 3.1.3.1 extracted from

  • Polakowski, R.; Craig, D.B.; Skelley, A.; Dovichi, N.J.
    Single molecules of highly purified bacterial alkaline phosphatase have identical activity (2000), J. Am. Chem. Soc., 122, 4853-4855.
No PubMed abstract available

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene phoA, 3 isozymes 1, 2, and 3 differing in the N-terminal sequence
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Escherichia coli
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gene phoA, 3 isozymes 1,2, and 3 differing in the N-terminal sequence
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no glycoprotein
-
Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
3 isozymes Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
a phosphate monoester + H2O = an alcohol + phosphate Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'-[2-benzthiazole]-6'-hydroxybenzthiazole phosphate + H2O weakly fluorescent substrate Escherichia coli 2'-[2-benzthiazole]-6'-hydroxybenzthiazole + phosphate highly fluorescent product ?

Subunits

Subunits Comment Organism
dimer heterodimer, isozyme 2 Escherichia coli
monomer isozymes 1 and 3 Escherichia coli

Synonyms

Synonyms Comment Organism
alkaline phosphatase
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
33
-
2'-[2-benzthiazole]-6'-hydroxybenzthiazole phosphate
-
Escherichia coli