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Literature summary for 3.1.3.1 extracted from

  • Goldman S, Hecht K, Eisenberg H, Mevarech M.
    Extracellular Ca2(+)-dependent inducible alkaline phosphatase from extremely halophilic archaebacterium Haloarcula marismortui (1990), J. Bacteriol., 172, 7065-7070.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.1

General Stability

General Stability Organism
at 3.5 mM Ca2+, the enzyme is unstable at low NaCl concentrations but its stability increases with the salt concentration. At 32 mM Ca2+ , the enzyme is rather stable even at low NaCl concentrations. Even at 4 M NaCl, the stability of the enzyme depends on the Ca2+ concentration Haloarcula marismortui
both calcium ions (in the millimolar range) and NaCl (in the molar range) are required for the stability of the enzyme Haloarcula marismortui

Inhibitors

Inhibitors Comment Organism Structure
phosphate
-
 Haloarcula marismortui

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted during phosphate starvation Haloarcula marismortui
-
-
membrane the enzyme is secreted during phosphate starvation Haloarcula marismortui 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ requires Ca2+ and not Zn2+ ions for its activity.Optimal Ca2+ concentration for enzymatic activity is 3.4 mM Haloarcula marismortui
KCl the enzyme is more active in NaCl than with KCl Haloarcula marismortui
NaCl required, the enzyme is more active in NaCl than with KCl Haloarcula marismortui

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 the enzyme appears as a broad peak at a location corresponding to molecules having molecular masses of 650 to 850 kDa. The native form of the enzyme is heterogeneous and composed of multiple oligomeric forms Haloarcula marismortui
160000
-
 x * 160000, SDS-PAGE, the native form of the enzyme is heterogeneous and composed of multiple oligomeric forms Haloarcula marismortui

Organism

Organism UniProt Comment Textmining
Haloarcula marismortui
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Haloarcula marismortui

Source Tissue

Source Tissue Comment Organism Textmining
culture medium the enzyme is secreted during phosphate starvation Haloarcula marismortui
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 160000, SDS-PAGE, the native form of the enzyme is heterogeneous and composed of multiple oligomeric forms Haloarcula marismortui

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Haloarcula marismortui

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Haloarcula marismortui
9
-
 assay at Haloarcula marismortui

pH Range

pH Minimum pH Maximum Comment Organism
8 9.5 pH 8.0: about 60% of maximal activity, pH 9.5: about 75% of maximal activity Haloarcula marismortui

Expression

Organism Comment Expression
Haloarcula marismortui the enzyme is produced only when the cells are starved of phosphate. No activity can be detected when the phosphate concentration is higher than 0.1 mM, and the highest specific activity is obtained when the minimal medium is completely devoid of phosphate. When the cells are starved of phosphate, the production of the enzyme starts immediately and continues at a constant rate for at least 48 h up