Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.1 extracted from

  • Ishibashi, M.; Oda, K.; Arakawa, T.; Tokunaga, M.
    Cloning, expression, purification and activation by Na ion of halophilic alkaline phosphatase from moderate halophile Halomonas sp. 593 (2011), Protein Expr. Purif., 76, 97-102.
    View publication on PubMed
Search for more literature for 3.1.3.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Halomonas sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Na+ gel filtration fraction is converted to the native structure by Na2SO4 suggesting the importance of Na ion Halomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
108000
-
 native PAGE Halomonas sp.

Organism

Organism UniProt Comment Textmining
Halomonas sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purified recombinant HaALP is separated into four fractions by gel filtration. Dialyzed against 50 mM Tris-HCl (pH 8.0)/2 mM MgCl2 buffer containing 3 M NaCl, one of these four fractions is activated to almost full activity Halomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Halomonas sp. 4-nitrophenol + phosphate
-
 ?

Subunits

Subunits Comment Organism
dimer native PAGE Halomonas sp.

Synonyms

Synonyms Comment Organism
alkaline phosphatase
-
 Halomonas sp.
HaALP
-
 Halomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Halomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10.25
-
 assay at Halomonas sp.