Inositol-tetrakisphosphate 1-kinase

inositol tetrakisphosphate 1-kinase
Identifiers
EC no.	2.7.1.134
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an inositol-tetrakisphosphate 1-kinase (EC 2.7.1.134) is an enzyme that catalyzes the chemical reaction

ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate ${\displaystyle \rightleftharpoons }$ ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

Thus, the two substrates of this enzyme are ATP and 1D-myo-inositol 3,4,5,6-tetrakisphosphate, whereas its two products are ADP and 1D-myo-inositol 1,3,4,5,6-pentakisphosphate.

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:1D-myo-inositol-3,4,5,6-tetrakisphosphate 1-phosphotransferase. Other names in common use include 1D-myo-inositol-tetrakisphosphate 1-kinase, inositol-trisphosphate 6-kinase, 1D-myo-inositol-trisphosphate 6-kinase, ATP:1D-myo-inositol-1,3,4-trisphosphate 6-phosphotransferase, inositol-trisphosphate 5-kinase, 1D-myo-inositol-trisphosphate 5-kinase, and ATP:1D-myo-inositol-1,3,4-trisphosphate 5-phosphotransferase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2ODT, 2Q7D, and 2QB5.

References

• Stephens LR, Hawkins PT, Morris AJ, Downes PC (1988). "L-myo-inositol 1,4,5,6-tetrakisphosphate (3-hydroxy)kinase". Biochem. J. 249 (1): 283–92. doi:10.1042/bj2490283. PMC   1148695 . PMID   2829850.
• Balla T, Guillemette G, Baukal AJ, Catt KJ (1987). "Metabolism of inositol 1,3,4-trisphosphate to a new tetrakisphosphate isomer in angiotensin-stimulated adrenal glomerulosa cells". J. Biol. Chem. 262 (21): 9952–5. doi: 10.1016/S0021-9258(18)61058-0 . PMID   3497156.
• Shears SB, Parry JB, Tang EK, Irvine RF, Michell RH, Kirk CJ (1987). "Metabolism of D-myo-inositol 1,3,4,5-tetrakisphosphate by rat liver, including the synthesis of a novel isomer of myo-inositol tetrakisphosphate". Biochem. J. 246 (1): 139–47. doi:10.1042/bj2460139. PMC   1148250 . PMID   2823793.
• Shears SB (1989). "The pathway of myo-inositol 1,3,4-trisphosphate phosphorylation in liver. Identification of myo-inositol 1,3,4-trisphosphate 6-kinase, myo-inositol 1,3,4-trisphosphate 5-kinase, and myo-inositol 1,3,4,6-tetrakisphosphate 5-kinase". J. Biol. Chem. 264 (33): 19879–86. doi: 10.1016/S0021-9258(19)47192-5 . PMID   2584198.
• Yang X, Shears SB (2000). "Multitasking in signal transduction by a promiscuous human Ins(3,4,5,6)P(4) 1-kinase/Ins(1,3,4)P(3) 5/6-kinase". Biochem. J. 351 (Pt 3): 551–5. doi:10.1042/0264-6021:3510551. PMC   1221393 . PMID   11042108.
• Vogel G, Riley AM, Potter BV, Shears SB (2002). "Regulation of Ins(3,4,5,6)P(4) signaling by a reversible kinase/phosphatase". Curr. Biol. 12 (6): 477–82. doi: 10.1016/S0960-9822(02)00713-3 . PMID   11909533. S2CID   14548016.