Glicerol-3-fosfat dehidrogenaza (NAD+)
Glicerol-3-fosfat dehidrogenaza (NAD+) | |||||||||
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Identifikatori | |||||||||
EC broj | 1.1.1.8 | ||||||||
CAS broj | 9075-65-4 | ||||||||
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 (NAD+) (EC 1.1.1.8, glicerol-3-fosfatna dehidrogenaza (NAD+), alfa-glicerol fosfat dehidrogenaza (NAD+), alfa-glicerofosfat dehidrogenaza (NAD+), glicerol 1-fosfat dehidrogenaza, glicerol fosfat dehidrogenaza (NAD+), glicerofosfat dehidrogenaza (NAD+), hidroglicerofosfat dehidrogenaza, L-alfa-glicerol fosfat dehidrogenaza, L-alfa-glicerofosfat dehidrogenaza, L-glicerol fosfat dehidrogenaza, L-glicerofosfat dehidrogenaza, NAD+-alfa-glicerofosfat dehidrogenaza, NAD+-zavisna glicerol fosfat dehidrogenaza, NAD+-zavisna glicerol-3-fosfat dehidrogenaza, NAD+-L-glicerol-3-fosfat dehidrogenaza, NAD+-vezani glicerol 3-fosfat dehidrogenaza, NADH-dihidroksiaceton fosfat reduktaza, L-glicerol-3-fosfat dehidrogenaza) je enzim sa sistematskim imenom sn-glicerol-3-fosfat:NAD+ 2-oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- sn-glicerol 3-fosfat + NAD+ gliceron fosfat + NADH + H+
Ovaj enzim takođe deluje na propan-1,2-diol fosfat and gliceron sulfat (mada sa znatno manjim afinitetom).
Reference
- ↑ Baranowski, T. (1963). „α-Glycerophosphate dehydrogenase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York: Academic Press. str. 85-96.
- ↑ Brosemer, R.W. and Kuhn, R.W. (1969). „Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenases”. Biochemistry 8: 2095-2105. PMID 4307630.
- ↑ O'Brien, S.J. and MacIntyre, R.J. (1972). „The α-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects”. Biochem. Genet. 7: 141-161. PMID 4340553.
- ↑ Warkentin, K.L. and Fondy, T.P. (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: 97-109. PMID 4200180.
- ↑ Albertyn, J., van Tonder, A. and Prior, B.A. (1992). „Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae”. FEBS Lett. 308: 130-132. PMID 1499720.
- ↑ Koekemoer, T.C., Litthauer, D. and Oelofsen, W. (1995). „Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase”. Int. J. Biochem. Cell Biol. 27: 625-632. PMID 7671141.
Literatura
- 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.
Spoljašnje veze
- MeSH Glycerol-3-phosphate+dehydrogenase+(NAD+)
- p
- r
- u