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Literature summary for 3.1.3.16 extracted from

  • Mai, B.; Frey, G.; Swanson, R.V.; Mathur, E.J.; Stetter, K.O.
    Molecular cloning and functional expression of a protein-serine/threonine phosphatase from the hyperthermophilic archaeon Pyrodictium abyssi TAG11 (1998), J. Bacteriol., 180, 4030-4035.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.16

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrodictium abyssi

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Pyrodictium abyssi
diethyldicarbonate 0.5%. No inhibition at 0.05% and 0.1% Pyrodictium abyssi
EDTA
-
 Pyrodictium abyssi
Fe2+
-
 Pyrodictium abyssi
NaF
-
 Pyrodictium abyssi
okadaic acid inhibition is greater at 40°C than at 90°C Pyrodictium abyssi
sodium potassium tartrate
-
 Pyrodictium abyssi
Zn2+
-
 Pyrodictium abyssi

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activity is dependent on the presence of divalent ions such as Mn2+, Co2+, Ni2+, or Mg2+. Mn2+, Co2+, Ni2+ are much more effective than Mg2+. Maximal activation is induced at concentrations in the range of 0.5 to 1 mM Pyrodictium abyssi
Mg2+ activity is dependent on the presence of divalent ions such as Mn2+, Co2+, Ni2+, or Mg2+. Mn2+, Co2+, Ni2+ are much more effective than Mg2+. Maximal activation with Mg2+ is induced between 5 and 10 mM Pyrodictium abyssi
Mn2+ activity is dependent on the presence of divalent ions such as Mn2+, Co2+, Ni2+, or Mg2+. Mn2+ is the most effective divalent metal ion. Maximal activation is induced at concentrations in the range of 0.5 to 1 mM Pyrodictium abyssi
Ni2+ activity is dependent on the presence of divalent ions such as Mn2+, Co2+, Ni2+, or Mg2+. Mn2+, Co2+, Ni2+ are much more effective than Mg2+. Maximal activation is induced at concentrations in the range of 0.5 to 1 mM Pyrodictium abyssi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33340
-
 x * 33340, calculation from sequence Pyrodictium abyssi

Organism

Organism UniProt Comment Textmining
Pyrodictium abyssi O08367
-
-
Pyrodictium abyssi TAG11 O08367
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrodictium abyssi

Renatured (Commentary)

Renatured (Comment) Organism
the protein denatured by 6 M guanidinium chloride is refolded by dilution (100fold) into a buffer containing 0.5 M L-arginine Pyrodictium abyssi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[a peptide]-serine/threonine phosphate + H2O
-
 Pyrodictium abyssi [a peptide]-serine/threonine + phosphate
-
 ?
[a peptide]-serine/threonine phosphate + H2O
-
 Pyrodictium abyssi TAG11 [a peptide]-serine/threonine + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 33340, calculation from sequence Pyrodictium abyssi

Synonyms

Synonyms Comment Organism
protein-serine/threonine phosphatase
-
 Pyrodictium abyssi
Py-PP1
-
 Pyrodictium abyssi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
-
 Pyrodictium abyssi

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 110 the enzyme is active in the range from 40 to 110°C Pyrodictium abyssi

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
 half-life: 180 min Pyrodictium abyssi
100
-
 half-life: 7 min Pyrodictium abyssi
105
-
 half-life: 3 min Pyrodictium abyssi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Pyrodictium abyssi

pH Range

pH Minimum pH Maximum Comment Organism
4.5 8 pH changes (pH 4.5 to 8.0) have no significant effect on enzyme activity. No activity is observed below pH 4.0 or above 8.5 Pyrodictium abyssi

pI Value

Organism Comment pI Value Maximum pI Value
Pyrodictium abyssi calculation from sequence
-
 6.15