Literature summary for 3.1.3.1 extracted from

Ji, C.N.; Jiang, T.; Chen, M.Q.; Sheng, X.Y.; Mao, Y.M.
Purification, crystallization and preliminary X-ray studies of thermostable alkaline phosphatase from Thermus sp. 3041 (2001), Acta Crystallogr. Sect. D, 57, 614-615.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli TG1	Thermus sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
10 mg/ml, purified recombinant enzyme, hanging-drop vapour-diffusion method, equal volumes of protein and precipitant solution, precipitant solution: 140 mM MgCl2, 100 mM HEPES, pH 7.5, 28.5% PEG 400, X-ray diffraction sturcture determinationand analysis at 2.16 A	Thermus sp.

Organism

Organism	UniProt	Comment	Textmining
Thermus sp.	-	-	-
Thermus sp. 314	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant from Escherichia coli	Thermus sp.

Reaction

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

Synonyms

Synonyms	Comment	Organism
alkaline phosphatase	-	Thermus sp.
AP	-	Thermus sp.

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Release 2023.1 (January 2023)