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Glycerol-3-phosphate dehydrogenase

 
Wikipedia: Glycerol-3-phosphate dehydrogenase
Glycerol-3-phosphate dehydrogenase
Identifiers
EC number 1.1.1.8
CAS number 9075-65-4
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures
Gene Ontology AmiGO / EGO
glycerol-3-phosphate dehydrogenase 1 (soluble)
Glycerol-3-phosphate dehydrogenase 1.png
Identifiers
Symbol GPD1
Entrez 2819
HUGO 4455
OMIM 138420
RefSeq NM_005276
UniProt P21695
Other data
EC number 1.1.1.8
Locus Chr. 12 q12-q13
glycerol-3-phosphate dehydrogenase 2 (mitochondrial)
Identifiers
Symbol GPD2
Entrez 2820
HUGO 4456
OMIM 138430
RefSeq NM_000408
UniProt P43304
Other data
EC number 1.1.1.8
Locus Chr. 2 q24.1

Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reduction of dihydroxyacetone phosphate (aka glycerone phosphate, outdated) to sn-glycerol 3-phosphate.

Older terms for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase (alphaGPDH) and glycerolphosphate dehydrogenase (GPDH). However, glycerol-3-phosphate dehydrogenase is not the same as glyceraldehyde 3-phosphate dehydrogenase (GAPDH) whose substrate is an aldehyde not an alcohol.

Contents

Reaction

The reaction catalyzed by cytosolic GPDH is as follows:

Dihydroxyacetone phosphate to glycerol 3-phosphate en.svg

Glycerol-3-phosphate shuttle

The cytosolic together with the mitochondrial glycerol-3-phosphate dehydrogenase work in concert. Oxidation of cytoplasmic NADH by the cytosolic form of the enzyme creates glycerol-3-phosphate from dihydroxyacetone phosphate. Once the Glycerol-3-phosphate has moved through the inner mitochondrial membrane it can then be oxidised by a separate isoform of glycerol-3-phosphate dehydrogenase. This differ as it is instead FADH2 linked. As a result there is a net loss in energy, comparable to 1 ATP. Illustrated here [1].

See also

References

  • Baranowski T (1963). "α-Glycerophosphate dehydrogenase". in Boyer PD, Lardy H, Myrbäck K. The Enzymes (2nd ed.). New York: Academic Press. pp. 85-96. 
  • Brosemer RW, Kuhn RW (May 1969). "Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenases". Biochemistry 8 (5): 2095–105. 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. 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. 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. 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. 

External links


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