Glicerol-3-fosfat dehidrogenaza (hinon)
| Glicerol-3-fosfat dehidrogenaza | |||||||||
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| Glicerol-3-fosfat dehidrogenaza monomer + FAD, E.Coli | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.1.5.3 | ||||||||
| CAS broj | 9001-49-4 | ||||||||
| 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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Glicerol-3-fosfat dehidrogenaza (EC 1.1.5.3, alfa-glicerofosfatna dehidrogenaza, alfa-glicerofosfatna dehidrogenaza (akceptor), anaerobna glicerol-3-fosfatna dehidrogenaza, DL-glicerol 3-fosfatna oksidaza, FAD-zavisna glicerol-3-fosfatna dehidrogenaza, FAD-zavisna sn-glicerol-3-fosfatna dehidrogenaza, FAD-GPDH, FAD-vezana glicerol 3-fosfatna dehidrogenaza, FAD-vezana L-glicerol-3-fosfatna dehidrogenaza, flavin-vezana glicerol-3-fosfatna dehidrogenaza, flavoprotein-vezana L-glicerol 3-fosfatna dehidrogenaza, glicerol 3-fosfatna citohrom c reduktaza, glicerol fosfatna dehidrogenaza, glicerol fosfatna dehidrogenaza (akceptor), glicerol fosfatna dehidrogenaza (FAD), glicerol-3-fosfatna CoQ reduktaza, glicerol-3-fosfatna dehidrogenaza (flavin-vezana), glicerol-3-fosfat:CoQ reduktaza, glicerofosfatna dehidrogenaza, L-3-glicerofosfat-ubihinonska oksidoreduktaza, L-glicerol-3-fosfatna dehidrogenaza, L-glicerofosfatna dehidrogenaza, mGPD, mitochondrial glicerol fosfatna dehidrogenaza, NAD+-inzavisni glicerol fosfatna dehidrogenaza, od piridin nukleotida nezavisni L-glicerol 3-fosfatna dehidrogenaza, sn-glicerol 3-fosfatna oksidaza, sn-glicerol-3-fosfatna dehidrogenaza, sn-glicerol-3-fosfat:(akceptor) 2-oksidoreduktaza, sn-glicerol-3-fosfat:akceptor 2-oksidoreduktaza) je enzim sa sistematskim imenom sn-glicerol 3-fosfat:hinon oksidoreduktaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- sn-glicerol 3-fosfat + hinon gliceron fosfat + hinol
Ova od flavina zavisna dehidrogenaza je esencijalni membranski enzim, koji funkcioniše u okviru glikolize, respiracije i fosfolipidne biosinteze. Kod bakterija se ovaj enzim nalazi na citoplazmičnoj membrani, dok je kod eukariota vezan za spoljašnju stranu unurašnje mitohondrijske membrane. .
Reference[uredi | uredi kod]
- ↑ Ringler, R.L. (1961). „Studies on the mitochondrial α-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain”. J. Biol. Chem. 236: 1192-1198. PMID 13741763.
- ↑ Schryvers, A., Lohmeier, E. and Weiner, J.H. (1978). „Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli”. J. Biol. Chem. 253: 783-788. PMID 340460.
- ↑ MacDonald, M.J. and Brown, L.J. (1996). „Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied”. Arch. Biochem. Biophys. 326: 79-84. PMID 8579375.
- ↑ Rauchová, H., Fato, R., Drahota, Z. and Lenaz, G. (1997). „Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria”. Arch. Biochem. Biophys. 344: 235-241. PMID 9244403.
- ↑ Shen, W., Wei, Y., Dauk, M., Zheng, Z. and Zou, J. (2003). „Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants”. FEBS Lett. 536: 92-96. PMID 12586344.
- ↑ Walz, A.C., Demel, R.A., de Kruijff, B. and Mutzel, R. (2002). „Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic α-helix”. Biochem. J. 365: 471-479. PMID 11955283.
- ↑ Ansell, R., Granath, K., Hohmann, S., Thevelein, J.M. and Adler, L. (1997). „The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation”. EMBO J. 16: 2179-2187. PMID 9171333.
- ↑ Larsson, C., Påhlman, I.L., Ansell, R., Rigoulet, M., Adler, L. and Gustafsson, L. (1998). „The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae”. Yeast 14: 347-357. PMID 9559543.
Literatura[uredi | uredi kod]
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- 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.
- Baranowski T (1963). „α-Glycerophosphate dehydrogenase”. u: Boyer PD, Lardy H, Myrbäck K. The Enzymes (2nd izd.). New York: Academic Press. str. 85–96.
- Brosemer RW, Kuhn RW (May 1969). „Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenases”. Biochemistry 8 (5): 2095–105. DOI:10.1021/bi00833a047. PMID 4307630.
- O'Brien SJ, MacIntyre RJ (October 1972). „The -glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects”. Biochem. Genet. 7 (2): 141–61. DOI:10.1007/BF00486085. PMID 4340553.
- Warkentin DL, Fondy TP (July 1973). „Isolation and characterization of cytoplasmic L-glycerol-3-phosphate dehydrogenase from rabbit-renal-adipose tissue and its comparison with the skeletal-muscle enzyme”. Eur. J. Biochem. 36 (1): 97–109. DOI:10.1111/j.1432-1033.1973.tb02889.x. PMID 4200180.
- Albertyn J, van Tonder A, Prior BA (August 1992). „Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae”. FEBS Lett. 308 (2): 130–2. DOI:10.1016/0014-5793(92)81259-O. PMID 1499720.
- Koekemoer TC, Litthauer D, Oelofsen W (June 1995). „Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase”. Int. J. Biochem. Cell Biol. 27 (6): 625–32. DOI:10.1016/1357-2725(95)00012-E. PMID 7671141.
- Pahlman, Inga-lill; Larsson, Christer; Averet, Nicole; Bunoust, Odile; Boubekeur, Samira; Gustafsson, Lena and Rigoulet, Michel (August 2002). „Kinetic Regulation of the Mitochondrial Glycerol-3-phosphate Dehydrogenase by the External NADH Dehydrogenase in Saccharomyces cerevisiae”. The Journal of Biological Chemistry 277 (31): 27991–27995. DOI:10.1074/jbc.M204079200. PMID 12032156.
- Overkamp, Karin M.; Bakker, Barbara M.; Kotter, Peter; van Tuijl, Arjen; de Vries, Simon; van Dijken, Johannes P. and Pronk, Jack T. (May 2000). „In Vivo Analysis of the Mechanisms for Oxidation of Cytosolic NADH by Saccharomyces cerevisiae Mitochondria”. Journal of Bacteriology 182 (10): 2823–2830. DOI:10.1128/JB.182.10.2823-2830.2000. PMC 101991. PMID 10781551. Pristupljeno 2011-05-16.
- Dawson, Anthony G.; Cooney, Gregory J. (July 1978). „RECONSTRUCTION OF THE wGLYCEROLPHOSPHATE SHUTTLE USING RAT KIDNEY MITOCHONDRIA”. Febs Letters 91 (2): 169–172. DOI:10.1016/0014-5793(78)81164-8. PMID 210038.
- Opperdoes, Fred R.; Borst, Piet; Bakker, Suzanne and Leene, Wolter (October 1976). „Localization of Glycerol-3-Phosphate Oxidase in the Mitochondrion and Particulate NAD+-Linked Glycerol-3-Phosphate Dehydrogenase in the Microbodies of the Bloodstream Form of Trypanosoma brucei”. European Journal of Biochemistry 76 (1): 29–39. DOI:10.1111/j.1432-1033.1977.tb11567.x. PMID 142010.
- Eswaramoorthy, Subramaniam; Bonanno, Jeffrey B.; Burley, Stephen K. and Swaminathan, Subramanyam (June 2006). „Mechanism of action of a flavin-containing monooxygenase”. Proceedings of the National Academy of Sciences of the United States of America 103 (26): 9832–9837. DOI:10.1073/pnas.0602398103. PMC 1502539. PMID 16777962. Pristupljeno 2011-05-16.