1-phosphatidylinositol 4-kinase

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1-phosphatidylinositol 4-kinase
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Phosphatidylinositol 4-kinase homo16mer, Human
Identifiers
EC no. 2.7.1.67
CAS no. 37205-54-2
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In enzymology, a 1-phosphatidylinositol 4-kinase (EC 2.7.1.67) is an enzyme that catalyzes the chemical reaction

ATP + 1-phosphatidyl-1D-myo-inositol ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate

Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 4-phosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol 4-phosphotransferase. Other names in common use include phosphatidylinositol kinase (phosphorylating), phosphatidylinositol 4-kinase, phosphatidylinositol kinase, type II phosphatidylinositol kinase, PI kinase, and PI 4-kinase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.

Structural studies

As of late 2007, the structure has only been solved for this enzyme. Part of the enzyme was crystallized with its activating partner frequenin. [1]

Related Research Articles

<span class="mw-page-title-main">Phosphoinositide phospholipase C</span>

Phosphoinositide phospholipase C is a family of eukaryotic intracellular enzymes that play an important role in signal transduction processes. These enzymes belong to a larger superfamily of Phospholipase C. Other families of phospholipase C enzymes have been identified in bacteria and trypanosomes. Phospholipases C are phosphodiesterases.

The enzyme glycosylphosphatidylinositol diacylglycerol-lyase catalyzes the reaction

The enzyme phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase (EC 3.1.3.67) catalyzes the chemical reaction

The enzyme phosphatidylinositol-3,4-bisphosphate 4-phosphatase (EC 3.1.3.66) that catalyzes the reaction

The enzyme phosphatidylinositol-3-phosphatase (EC 3.1.3.64) catalyzes the reaction

In enzymology, a N-acetylglucosaminylphosphatidylinositol deacetylase (EC 3.5.1.89) is an enzyme that catalyzes the chemical reaction

In enzymology, a 1-phosphatidylinositol-3-phosphate 5-kinase is an enzyme that catalyzes the chemical reaction

In enzymology, 1-phosphatidylinositol-4-phosphate 5-kinase is an enzyme that catalyzes the chemical reaction

In enzymology, a 1-phosphatidylinositol-5-phosphate 4-kinase is an enzyme that catalyzes the chemical reaction

In enzymology, a diphosphoinositol-pentakisphosphate kinase is an enzyme that catalyzes the chemical reaction

In enzymology, an inositol 3-kinase is an enzyme that catalyzes the chemical reaction

In enzymology, an inositol-pentakisphosphate 2-kinase is an enzyme that catalyzes the chemical reaction

In enzymology, an inositol-tetrakisphosphate 1-kinase is an enzyme that catalyzes the chemical reaction

In enzymology, an inositol-tetrakisphosphate 5-kinase is an enzyme that catalyzes the chemical reaction

In enzymology, a phosphatidylinositol-4,5-bisphosphate 3-kinase is an enzyme that catalyzes the chemical reaction:

In enzymology, a phosphatidylinositol-4-phosphate 3-kinase is an enzyme that catalyzes the chemical reaction

Bisphosphate may refer to:

Inositol-polyphosphate multikinase is an enzyme with systematic name ATP:1D-myo-inositol-1,4,5-trisphosphate 6-phosphotransferase. This enzyme catalyses the following chemical reaction

inositol-1,3,4-trisphosphate 5/6-kinase is an enzyme with systematic name ATP:1D-myo-inositol 1,3,4-trisphosphate 5-phosphotransferase. This enzyme catalyses the following chemical reaction

Inositol-hexakisphosphate kinase is an enzyme with systematic name ATP:1D-myo-inositol-hexakisphosphate 5-phosphotransferase. This enzyme catalyses the following chemical reaction

References

  1. Strahl T, Huttner IG, Lusin JD, et al. (October 2007). "Structural insights into activation of phosphatidylinositol 4-kinase (Pik1) by yeast frequenin (Frq1)". J. Biol. Chem. 282 (42): 30949–59. doi: 10.1074/jbc.M705499200 . PMID   17720810.