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Literature summary for 3.1.3.1 extracted from

  • Zappa, S.; Rolland, J.L.; Flament, D.; Gueguen, Y.; Boudrant, J.; Dietrich, J.
    Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon Pyrococcus abyssi (2001), Appl. Environ. Microbiol., 67, 4504-4511.
    View publication on PubMed
Search for more literature for 3.1.3.1

Activating Compound

Activating Compound Comment Organism Structure
Co2+ 2fold activation at 1 mM Pyrococcus abyssi
Mg2+ 2fold activation at 1 mM Pyrococcus abyssi
Zn2+ 2fold activation at 1 mM Pyrococcus abyssi

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, expression in Escherichia coli HMS174 (DE3) Pyrococcus abyssi

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol 68% inhibition at 1 mM, 86% inhibition at 10 mM Pyrococcus abyssi
Ca2+ 17% inhibition at 1 mM Pyrococcus abyssi
Cu2+ 28% inhibition at 1 mM Pyrococcus abyssi
DTT nearly complete inhibition at 2 mM Pyrococcus abyssi
EDTA 90% inhibition at 1 mM Pyrococcus abyssi
EGTA 82% inhibition at 1 mM Pyrococcus abyssi
KCl 90% remaining activity Pyrococcus abyssi
molybdate slight inhibition at 10 mM Pyrococcus abyssi
additional information no inhibition by molybdate and vanadate Pyrococcus abyssi
NaCl 2 M, 60% remaining activity Pyrococcus abyssi
Ni2+ 56% inhibition at 1 mM Pyrococcus abyssi
phosphate
-
 Pyrococcus abyssi
vanadate
-
 Pyrococcus abyssi

Metals/Ions

Metals/Ions Comment Organism Structure
additional information highly dependent on divalent cations Pyrococcus abyssi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
 1 * 54000, SDS-PAGE Pyrococcus abyssi
54000
-
 2 * 54000, SDS-PAGE Pyrococcus abyssi

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi Q9UZV2 euryarchaeon, strain Orsay, highly thermostable enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from Escherichia coli, 450fold, to 95% purity Pyrococcus abyssi

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Pyrococcus abyssi 4-nitrophenol + phosphate
-
 ?
additional information the enzyme also dephosphorylizes cohesive and blunt ends of DNA fragments, cohesive ends are slightly preferred Pyrococcus abyssi ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 54000, SDS-PAGE Pyrococcus abyssi
monomer 1 * 54000, SDS-PAGE Pyrococcus abyssi
additional information both monomeric and dimeric enzyme forms exist, no cysteine residues are involved in intramolecular disulfide bonds Pyrococcus abyssi

Synonyms

Synonyms Comment Organism
alkaline phosphatase
-
 Pyrococcus abyssi
AP
-
 Pyrococcus abyssi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
 Pyrococcus abyssi

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 80 25% of maximal activity at 37°C, 80% of maximal activity at 60-80°C Pyrococcus abyssi

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
 80% remaining activity after 36 h Pyrococcus abyssi
100
-
 half-life 18 h Pyrococcus abyssi
105
-
 half-life 5 h Pyrococcus abyssi
115
-
 inactivation within 30 min Pyrococcus abyssi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
11
-
-
 Pyrococcus abyssi

pH Range

pH Minimum pH Maximum Comment Organism
9 12
-
 Pyrococcus abyssi

pI Value

Organism Comment pI Value Maximum pI Value
Pyrococcus abyssi calculation from amino acid sequence
-
 4.9