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Literature summary for 2.7.1.127 extracted from

  • Communi, D.; Dewaste, V.; Erneux, C.
    Calcium-calmodulin-dependent protein kinase II and protein kinase C-mediated phosphorylation and activation of D-myo-inositol 1,4, 5-trisphosphate 3-kinase B in astrocytes (1999), J. Biol. Chem., 274, 14734-14742.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
12-O-tetradecanoylphorbol-13-acetate 2fold activation, isoform B Homo sapiens
12-O-tetradecanoylphorbol-13-acetate 2fold activation, isoform B Rattus norvegicus
CaM kinase II phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, no effect on the sensitivity to the Ca2+/calmodulin complex, CaM kinase II alone activates 35-40fold in the presence of Ca2+ and calmodulin Homo sapiens
CaM kinase II phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, no effect on the sensitivity to the Ca2+/calmodulin complex, CaM kinase II alone activates 35-40fold in the presence of Ca2+ and calmodulin Rattus norvegicus
Carbachol calphostin C, KN-93 or KN-62 partially prevents activation Rattus norvegicus
Carbachol 6-8fold okadaic acid-sensitive activation, maximal at 0.01 mM, isoform B, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction Homo sapiens
Carbachol 6-8fold okadaic acid-sensitive activation, maximal at 0.01 mM, isoform B, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction Rattus norvegicus
additional information isoenzyme B of 1321N1 cells is not activated by UTP Homo sapiens
additional information isoenzymes A and B are not activated by protein kinase A Rattus norvegicus
Protein kinase C phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, but protein kinase C alone inhibits in the presence of Ca2+ and calmodulin, no effect on the sensitivity to the Ca2+/calmodulin complex Homo sapiens
Protein kinase C phosphorylation of isoenzyme B by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, but protein kinase C alone inhibits in the presence of Ca2+ and calmodulin, no effect on the sensitivity to the Ca2+/calmodulin complex Rattus norvegicus
UTP
-
Homo sapiens
UTP 6-8fold okadaic acid-sensitive activation, maximal at 0.01 mM, isoform B, calphostin C, KN-93 or KN-62 partially prevents activation, UTP-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
Protein kinase C
-
Homo sapiens
Protein kinase C protein kinase C alone, without CaM kinase II, inhibits in the presence of Ca2+ and calmodulin Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
1D-myo-inositol 1,4,5-trisphosphate isoform B Homo sapiens
0.0015
-
1D-myo-inositol 1,4,5-trisphosphate isoform B Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
particle-bound not activated isoenzyme B: 65% soluble, 35% particulate fraction, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction, only 10% remain soluble Homo sapiens
-
-
particle-bound not activated isoenzyme B: 65% soluble, 35% particulate fraction, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction, only 10% remain soluble Rattus norvegicus
-
-
soluble unstimulated isoenzyme B: 65% soluble, 35% particulate fraction, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction, only 10% remain soluble Homo sapiens
-
-
soluble unstimulated isoenzyme B: 65% soluble, 35% particulate fraction, carbachol-activated isoenzyme B shows a redistribution of enzyme from soluble to particulate fraction, only 10% remain soluble Rattus norvegicus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ phosphorylation of isoenzyme B has no effect on the sensitivity to the Ca2+/calmodulin complex Rattus norvegicus
Ca2+ activation by Ca2+/calmodulin Homo sapiens
Ca2+ activation by Ca2+/calmodulin Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
88000
-
x * 88000, isoform B, SDS-PAGE, Western blot analysis Homo sapiens
88000
-
x * 88000, isoform B, SDS-PAGE, Western blot analysis Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 1D-myo-inositol 1,4,5-trisphosphate Homo sapiens regulatory mechanism of isoenzyme B involving phosphorylation by both protein kinase C and CaM kinase II ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate Rattus norvegicus regulatory mechanism of isoenzyme B involving phosphorylation by both protein kinase C and CaM kinase II ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate Homo sapiens inositol 1,4,5-trisphosphate is a second messenger ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate Rattus norvegicus inositol 1,4,5-trisphosphate is a second messenger ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isoform B
-
Rattus norvegicus
-
2-3 days old, isoform B
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of enzyme by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, distinct sites are phosphorylated independently by both protein kinases, prevented by the CaM kinase II inhibitors KN-93, KN-62 and the protein kinase C inhibitor calphostin C Homo sapiens
phosphoprotein phosphorylation of enzyme by calmodulin kinase II and protein kinase C added together results in a maximal 60-70fold activation, distinct sites are phosphorylated independently by both protein kinases, prevented by the CaM kinase II inhibitors KN-93, KN-62 and the protein kinase C inhibitor calphostin C Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
isoenzyme B Homo sapiens
isoenzyme B Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
astrocyte cerebral cortex astrocytes, isoform B Rattus norvegicus
-
astrocytoma cell 1321N1 cells, isoform B Homo sapiens
-
brain
-
Homo sapiens
-
brain cortical astrocytes, isoform B Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4
-
isoform B, in absence of the Ca2+/calmodulin complex Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 1D-myo-inositol 1,4,5-trisphosphate regulatory mechanism of isoenzyme B involving phosphorylation by both protein kinase C and CaM kinase II Homo sapiens ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate regulatory mechanism of isoenzyme B involving phosphorylation by both protein kinase C and CaM kinase II Rattus norvegicus ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate inositol 1,4,5-trisphosphate is a second messenger Homo sapiens ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate inositol 1,4,5-trisphosphate is a second messenger Rattus norvegicus ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
?

Subunits

Subunits Comment Organism
? x * 88000, isoform B, SDS-PAGE, Western blot analysis Homo sapiens
? x * 88000, isoform B, SDS-PAGE, Western blot analysis Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens
ATP
-
Rattus norvegicus
Calmodulin activation by Ca2+/calmodulin Homo sapiens
Calmodulin activation by Ca2+/calmodulin Rattus norvegicus
Calmodulin phosphorylation of isoenzyme B has no effect on the sensitivity to the Ca2+/calmodulin complex Rattus norvegicus