Inozitol-tetrakisfosfat 1-kinaza
Inozitol-tetrakisfosfat 1-kinaza (EC 2.7.1.134, 1D-mio-inozitol-tetrakisfosfat 1-kinaza, inozitol-trisfosfat 6-kinaza, 1D-mio-inozitol-trisfosfat 6-kinaza, ATP:1D-mio-inozitol-1,3,4-trisfosfat 6-fosfotransferaza, inozitol-trisfosfat 5-kinaza, 1D-mio-inozitol-trisfosfat 5-kinaza, ATP:1D-mio-inozitol-1,3,4-trisfosfat 5-fosfotransferaza) je enzim sa sistematskim imenom ATP:1D-mio-inozitol-3,4,5,6-tetrakisfosfat 1-fosfotransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
Inozitol-tetrakisfosfat 1-kinaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.7.1.134 | ||||||||
CAS broj | 187175-98-0 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Ovaj enzim takođe fosforiliše Ins(1,3,4)P3 na pozicijama O-5 i O-6.
Reference uredi
- ↑ Stephens, L.R., Hawkins, P.T., Morris, A.J. and Downes, P.C. (1988). „L-myo-Inositol 1,4,5,6-tetrakisphosphate (3-hydroxy)kinase”. Biochem. J. 249: 283-292. PMID 2829850.
- ↑ Balla, T., Guillemette, G., Baukal, A.J. and Catt, K. (1987). „Metabolism of inositol 1,3,4-trisphosphate to a new tetrakisphosphate isomer in angiotensin-stimulated adrenal glomerulosa cells”. J. Biol. Chem. 262: 9952-9955. PMID 3497156.
- ↑ Shears, S.B., Parry, J.B., Tang, E.K.Y., Irvine, R.F., Michell, R.H. and Kirk, C.J. (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: 139-147. PMID 2823793.
- ↑ Shears, S.B. (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: 19879-19886. PMID 2584198.
- ↑ Yang, X. and Shears, S.B. (2000). „Multitasking in signal transduction by a promiscuous human Ins(3,4,5,6)P4 1-kinase/Ins(1,3,4)P3 5/6-kinase”. Biochem. J. 351: 551-555. PMID 11042108.
- ↑ Ho, M.W., Yang, X., Carew, M.A., Zhang, T., Hua, L., Kwon, Y.U., Chung, S.K., Adelt, S., Vogel, G., Riley, A.M., Potter, B.V. and Shears, S.B. (2002). „Regulation of Ins(3,4,5,6)P4 signaling by a reversible kinase/phosphatase”. Curr. Biol. 12: 477-482. PMID 11909533.
Literatura uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.