Literature summary for 3.1.3.1 extracted from

de Backer, M.; McSweeney, S.; Rasmussen, H.B.; Riise, B.W.; Lindley, P.; Hough, E.
The 1.9 A crystal structure of heat-labile shrimp alkaline phosphatase (2002), J. Mol. Biol., 318, 1265-1274.

Search for more literature for 3.1.3.1

Application

Application	Comment	Organism
molecular biology	widely used in vitro, e.g. to dephosphorylate DNA or dNTPs, since the enzyme can be inactivated by a short rise in temperature	shrimp

Crystallization (Commentary)

Crystallization (Comment)	Organism
11 mg/ml purified protein, in presence 0.1 mM Zn2+ and 1.0 mM Mg2+, hanging drop vapour diffusion method, crystallization buffer: 42.5% w/v ammoniums sulfate, 10% v/v glycero, 100 mM Tris-maleate, pH 5.6, X-ray diffraction structure determination and analysis at 1.9 A resolution, structure modeling	shrimp

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	metalloenzyme, 1 magnesium ion per monomer, binding structure	shrimp
Zn2+	metalloenzyme, 2 zinc ions per monomer, binding structure	shrimp

Organism

Organism	UniProt	Comment	Textmining
shrimp	-	cold-adapted enzyme	-

Reaction

Reaction	Comment	Organism	Reaction ID
a phosphate monoester + H2O = an alcohol + phosphate	Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, mechanism	shrimp	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	tissue-nonspecific enzyme	shrimp	-

Subunits

Subunits	Comment	Organism
dimer	homodimer, crystal structure	shrimp

Synonyms

Synonyms	Comment	Organism
alkaline phosphatase	-	shrimp
AP	-	shrimp
SAP	-	shrimp

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	heat-labile, the enzyme is inactivated by a short rise in temperature	shrimp

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)