PROFILPELAJAR.COM

Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

Glicerol-3-fosfat dehidrogenaza
Glicerol-3-fosfat dehidrogenaza
Identifikatori
EC broj	1.1.5.3
CAS broj	9001-49-4
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
Pretraga
PMC	članci
PubMed	članci
NCBI	proteini

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

\rightleftharpoons

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

^ 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.; 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. & Brown, L.J. (1996). „Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied”. Arch. Biochem. Biophys. 326: 79—84. PMID 8579375.
^ Rauchová et al. (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.; et al. (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.; et al. (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.; et al. (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.; et al. (1998). „The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae”. Yeast. 14: 347—357. PMID 9559543.

Literatura

Baranowski T (1963). „α-Glycerophosphate dehydrogenase”. Ур.: Boyer PD, Lardy H, Myrbäck K. The Enzymes (2nd изд.). New York: Academic Press. стр. 85—96.
Brosemer RW, Kuhn RW (1969). „Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenases”. Biochemistry. 8 (5): 2095—105. PMID 4307630. doi:10.1021/bi00833a047.
O'Brien SJ, MacIntyre RJ (1972). „The -glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects”. Biochem. Genet. 7 (2): 141—61. PMID 4340553. doi:10.1007/BF00486085.
Warkentin DL, Fondy TP (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. PMID 4200180. doi:10.1111/j.1432-1033.1973.tb02889.x.
Albertyn J, van Tonder A, Prior BA (1992). „Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae”. FEBS Lett. 308 (2): 130—2. PMID 1499720. doi:10.1016/0014-5793(92)81259-O.
Koekemoer TC, Litthauer D, Oelofsen W (1995). „Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase”. Int. J. Biochem. Cell Biol. 27 (6): 625—32. PMID 7671141. doi:10.1016/1357-2725(95)00012-E.
Pahlman, Inga-lill; Larsson, Christer; et al. (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. PMID 12032156. doi:10.1074/jbc.M204079200. Архивирано из оригинала 05. 12. 2017. г. Приступљено 09. 01. 2013.
Overkamp, Karin M.; Bakker, Barbara M.; et al. (2000). „In Vivo Analysis of the Mechanisms for Oxidation of Cytosolic NADH by Saccharomyces cerevisiae Mitochondria”. Journal of Bacteriology. 182 (10): 2823—2830. PMC 101991 . PMID 10781551. doi:10.1128/JB.182.10.2823-2830.2000.
Dawson, Anthony G.; Cooney, Gregory J. (1978). „RECONSTRUCTION OF THE wGLYCEROLPHOSPHATE SHUTTLE USING RAT KIDNEY MITOCHONDRIA”. Febs Letters. 91 (2): 169—172. PMID 210038. doi:10.1016/0014-5793(78)81164-8.
Opperdoes, Fred R.; Borst, Piet; et al. (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. PMID 142010. doi:10.1111/j.1432-1033.1977.tb11567.x.
Eswaramoorthy, Subramaniam; Bonanno, Jeffrey B.; et al. (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. PMC 1502539 . PMID 16777962. doi:10.1073/pnas.0602398103. Приступљено 16. 5. 2011.
Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.