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

BRENDA support

Literature summary for 3.1.3.56 extracted from

  • Chi, Y.; Zhou, B.; Wang, W.Q.; Chung, S.K.; Kwon, Y.U.; Ahn, Y.H.; Chang, Y.T.; Tsujishita, Y.; Hurley, J.H.; Zhang, Z.Y.
    Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2 (2004), J. Biol. Chem., 279, 44987-44995.
    View publication on PubMed
Search for more literature for 3.1.3.56

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged full length enzyme in Escherichia coli strain BL21(DE3) Schizosaccharomyces pombe
expression of His-tagged isolated catalytic domain in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
E597Q site-directed mutagenesis, the mutant enzyme shows an over 140fold increased catalytic efficiency and a 2.4fold reduced affinity for Mg2+ compared to the wild-type enzyme Schizosaccharomyces pombe

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ competitive to Mg2+ Schizosaccharomyces pombe
Cu2+
-
 Schizosaccharomyces pombe

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics, substrate specificity, overview Homo sapiens
additional information
-
 additional information kinetics, substrate specificity, overview Schizosaccharomyces pombe
0.056
-
 7-methyl-6-thioguanosine pH 7.0, 30°C, recombinant enzyme Schizosaccharomyces pombe

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates, competitive binding to other metal ions, KM 0.0145 mM and turnover number 7.28 s-1 at pH 7.0, 30°C, recombinant enzyme Schizosaccharomyces pombe
Mg2+
-
 Homo sapiens
Mg2+ required, optimal at 2 mM, existence of a second inhibitory metal binding site, competitive binding to other metal ions, KM 0.53 mM and turnover number 9.64 s-1 at pH 7.0, 30°C, recombinant enzyme Schizosaccharomyces pombe
Mn2+ activates, competitive binding to other metal ions, KM 0.012 mM and turnover number 7.48 s-1 at pH 7.0, 30°C, recombinant enzyme Schizosaccharomyces pombe
Ni2+ activates, competitive binding to other metal ions, KM 0.0064 mM and turnover number 5.48 s-1 at pH 7.0, 30°C, recombinant enzyme Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the enzyme has multiple roles in cellular signalling and may regulate distinct pathways ?
-
 ?
additional information Schizosaccharomyces pombe the enzyme has multiple roles in cellular signalling and may regulate distinct pathways ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Schizosaccharomyces pombe
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged catalytic domain from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off Homo sapiens
recombinant His-tagged full length enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Schizosaccharomyces pombe

Reaction

Reaction Comment Organism Reaction ID
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate catalytic and kinetic reaction mechanism, substrate binding, overview Homo sapiens
a
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate catalytic and kinetic reaction mechanism, substrate binding, overview Schizosaccharomyces pombe
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
-
 Homo sapiens 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
 ?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
-
 Schizosaccharomyces pombe 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
 ?
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
-
 Homo sapiens 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate
-
 ?
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
-
 Schizosaccharomyces pombe 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate
-
 ?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
-
 Schizosaccharomyces pombe 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
 ?
1D-myo-inositol 1,2,3,4,5-pentakisphosphate + H2O preferred substrate Homo sapiens 1D-myo-inositol 1,2,3,4-tetrakisphosphate + phosphate
-
 ?
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O
-
 Schizosaccharomyces pombe 1D-myo-inositol 1,2,4,6-tetrakisphosphate + phosphate
-
 ?
1D-myo-inositol 1,2,4,5-tetrakisphosphate + H2O
-
 Schizosaccharomyces pombe 1D-myo-inositol 1,2,4-trisphosphate + phosphate
-
 ?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
-
 Homo sapiens 1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
 ?
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
-
 Schizosaccharomyces pombe 1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
 ?
1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O
-
 Homo sapiens 1D-myo-inositol 1,4,6-trisphosphate + phosphate
-
 ?
1D-myo-inositol 1,4,5-trisphosphate + H2O
-
 Schizosaccharomyces pombe 1D-myo-inositol 1,4-bisphosphate + phosphate
-
 ?
1D-myo-inositol 2,4,5,6-tetrakisphosphate + H2O
-
 Schizosaccharomyces pombe 1D-myo-inositol 2,4,6-trisphosphate + phosphate
-
 ?
1D-myo-inositol 2,4,5,6-tetrakisphosphate + H2O low activity Homo sapiens 1D-myo-inositol 2,4,6-trisphosphate + phosphate
-
 ?
1D-myo-inositol 2,4,5-trisphosphate + H2O preferred substrate Schizosaccharomyces pombe 1D-myo-inositol 2,4-bisphosphate + phosphate
-
 ?
1D-myo-inositol 4,5,6-trisphosphate + H2O
-
 Schizosaccharomyces pombe 1D-myo-inositol 4,6-bisphosphate + phosphate
-
 ?
3-O-methylfluorescein phosphate + H2O
-
 Schizosaccharomyces pombe 3-O-methylfluorescein + phosphate
-
 ?
4-nitrophenyl phosphate + H2O
-
 Schizosaccharomyces pombe 4-nitrophenol + phosphate
-
 ?
7-methyl-6-thioguanosine + H2O spectrophotometric continous coupled enzyme assay substrate Schizosaccharomyces pombe 7-methyl-6-thioguanine + ribose 1-phosphate
-
 ?
additional information the enzyme has multiple roles in cellular signalling and may regulate distinct pathways Homo sapiens ?
-
 ?
additional information the enzyme has multiple roles in cellular signalling and may regulate distinct pathways Schizosaccharomyces pombe ?
-
 ?
additional information substrate specificity, no activity with 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1D-myo-inositol 1,5-bisphosphate, 1D-myo-inositol 1,3,5-trisphosphate, and with alpha-D-glucose 1-phosphate, D-glucose 6-phosphate, and alpha-D,L-glycerophosphate, overview Schizosaccharomyces pombe ?
-
 ?
additional information substrate specificity, no activity with 1D-myo-inositol 1,4,5-trisphosphate, 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1D-myo-inositol 1,5-bisphosphate, and 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, overview Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More three-dimensional structure analysis of enzyme with active site-bound substrate, analysis of crystal structure Schizosaccharomyces pombe

Synonyms

Synonyms Comment Organism
inositol polyphosphate 5-phosphatase
-
 Homo sapiens
inositol polyphosphate 5-phosphatase
-
 Schizosaccharomyces pombe
More cf. EC 3.1.3.36, phosphoinositide 5-phosphatase Schizosaccharomyces pombe
SHIP2
-
 Homo sapiens
SPsynaptojanin
-
 Schizosaccharomyces pombe
Synaptojanin
-
 Schizosaccharomyces pombe

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Homo sapiens
30
-
 assay at Schizosaccharomyces pombe

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11
-
 7-methyl-6-thioguanosine pH 7.0, 30°C, recombinant enzyme Schizosaccharomyces pombe

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.4 assay at Homo sapiens
7 7.4 assay at Schizosaccharomyces pombe

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 pH profile Schizosaccharomyces pombe

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information
-
 Schizosaccharomyces pombe