Piridoksamin-fosfat oksidaza
Piridoksamin-fosfat oksidaza (EC 1.4.3.5, piridoksamin 5'-fosfat oksidaza, piridoksamin fosfatna oksidaza, piridoksin (piridoksamin) fosfat oksidaza, piridoksin (piridoksamin) 5'-fosfat oksidaza, piridoksaminfosfatna oksidaza (EC 1.4.3.5: deaminacija), PMP oksidaza, piridoksol-5'-fosfat:kiseonik oksidoreduktaza (deaminacija), piridoksamin-fosfatna oksidaza, PdxH) je enzim sa sistematskim imenom piridoksamin-5'-fosfat:kiseonik oksidoreduktaza (deaminacija).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju:
Piridoksamin-fosfat oksidaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.4.3.5 | ||||||||
CAS broj | 9029-21-4 | ||||||||
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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- (1) piridoksamin 5'-fosfat + H2O + O2 piridoksal 5'-fosfat + NH3 + H2O2
- (2) piridoksin 5'-fosfat + O2 piridoksal 5'-fosfat +H2O2
Ovaj enzim je flavoprotein (FMN). Kod Escherichia coli, koenzim piridoksal 5'-fosfat se sintetiše de novo putem u kome učestvuje EC 1.2.1.72 (eritroza-4-fosfat dehidrogenaza), EC 1.1.1.290 (4-fosfoeritronat dehidrogenaza), EC 2.6.1.52 (fosfoserin transaminaza), EC 1.1.1.262 (4-hidroksitreonin-4-fosfat dehidrogenaza), EC 2.6.99.2 (piridoksin 5'-fosfat sintaza) i EC 1.4.3.5 (sa piridoksin 5'-fosfatom kao supstratom).
Reference
uredi- ↑ Choi, J.-D., Bowers-Komro, D.M., Davis, M.D., Edmondson, D.E. and McCormick, D.B. (1983). „Kinetic properties of pyridoxamine (pyridoxine)-5′-phosphate oxidase from rabbit liver”. J. Biol. Chem. 258: 840-845. PMID 6822512.
- ↑ Wada, H. and Snell, E.E. (1961). „The enzymatic oxidation of pyridoxine and pyridoxamine phosphates”. J. Biol. Chem. 236: 2089-2095. PMID 13782387.
- ↑ Notheis, C., Drewke, C. and Leistner, E. (1995). „Purification and characterization of the pyridoxol-5′-phosphate:oxygen oxidoreductase (deaminating) from Escherichia coli”. Biochim. Biophys. Acta 1247: 265-271. PMID 7696318.
- ↑ Laber, B., Maurer, W., Scharf, S., Stepusin, K. and Schmidt, F.S. (1999). „Vitamin B6 biosynthesis: formation of pyridoxine 5′-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein”. FEBS Lett. 449: 45-48. PMID 10225425.
- ↑ Musayev, F.N., Di Salvo, M.L., Ko, T.P., Schirch, V. and Safo, M.K. (2003). „Structure and properties of recombinant human pyridoxine 5′-phosphate oxidase”. Protein Sci. 12: 1455-1463. PMID 12824491.
- ↑ Safo, M.K., Musayev, F.N. and Schirch, V. (2005). „Structure of Escherichia coli pyridoxine 5′-phosphate oxidase in a tetragonal crystal form: insights into the mechanistic pathway of the enzyme”. Acta Crystallogr. D Biol. Crystallogr. 61: 599-604. PMID 15858270.
- ↑ Zhang, Z. and McCormick, D.B. (1992). „Uptake and metabolism of N-(4′-pyridoxyl)amines by isolated rat liver cells”. Arch. Biochem. Biophys. 294: 394-397. PMID 1567194.
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.