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Escherichia coli K-12 substr. MG1655 Reaction: 1.1.5.3

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Composite Reactions Electron-Transfer-Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.1.5.3

Enzymes and Genes:
glycerol-3-phosphate dehydrogenase, aerobic Inferred from experiment : glpD

In Pathway: glycerol degradation I , glycerophosphodiester degradation , glycerol-3-phosphate to cytochrome bo oxidase electron transfer

Supersedes EC numbers: 1.1.99.5, 1.1.2.1

Note that this reaction equation differs from the official Enzyme Commission reaction equations for this EC number.

Reaction Locations: inner membrane (sensu Gram-negative Bacteria)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: glycerol-3-phosphate dehydrogenase

Enzyme Commission Synonyms: α-glycerophosphate dehydrogenase, α-glycerophosphate dehydrogenase (acceptor), anaerobic glycerol-3-phosphate dehydrogenase, DL-glycerol 3-phosphate oxidase (misleading), FAD-dependent glycerol-3-phosphate dehydrogenase, FAD-dependent sn-glycerol-3-phosphate dehydrogenase, FAD-GPDH, FAD-linked glycerol 3-phosphate dehydrogenase, FAD-linked L-glycerol-3-phosphate dehydrogenase, flavin-linked glycerol-3-phosphate dehydrogenase, flavoprotein-linked L-glycerol 3-phosphate dehydrogenase, glycerol 3-phosphate cytochrome c reductase (misleading), glycerol phosphate dehydrogenase, glycerol phosphate dehydrogenase (acceptor), glycerol phosphate dehydrogenase (FAD), glycerol-3-phosphate CoQ reductase, glycerol-3-phosphate dehydrogenase (flavin-linked), glycerol-3-phosphate:CoQ reductase, glycerophosphate dehydrogenase, L-3-glycerophosphate-ubiquinone oxidoreductase, L-glycerol-3-phosphate dehydrogenase (ambiguous), L-glycerophosphate dehydrogenase, mGPD, mitochondrial glycerol phosphate dehydrogenase, NAD+-independent glycerol phosphate dehydrogenase, pyridine nucleotide-independent L-glycerol 3-phosphate dehydrogenase, sn-glycerol 3-phosphate oxidase (misleading), sn-glycerol-3-phosphate dehydrogenase, sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase, sn-glycerol-3-phosphate:acceptor 2-oxidoreductase

Enzyme Commission Summary:
This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane [Walz02], while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane [Schryvers78]. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain [MacDonald96]. This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix [Ansell97, Larsson98]. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9 [Rauchova97]. The enzyme is activated by calcium [MacDonald96].

Citations: [Shen03, Ringler61]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.1.5.3 , ENZYME:EC:1.1.5.3 , IUBMB-ExplorEnz:EC:1.1.5.3


References

Ansell97: Ansell R, Granath K, Hohmann S, Thevelein JM, 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(9);2179-87. PMID: 9171333

Larsson98: Larsson C, Pahlman IL, Ansell R, Rigoulet M, Adler L, Gustafsson L (1998). "The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae." Yeast 14(4);347-57. PMID: 9559543

MacDonald96: MacDonald MJ, Brown LJ (1996). "Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied." Arch Biochem Biophys 326(1);79-84. PMID: 8579375

Rauchova97: Rauchova H, Fato R, Drahota Z, 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(1);235-41. PMID: 9244403

Ringler61: Ringler RL (1961). "Studies on the mitochondrial alpha-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain." J Biol Chem 236;1192-8. PMID: 13741763

Schryvers78: Schryvers A, Lohmeier E, Weiner JH (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(3);783-8. PMID: 340460

Shen03: Shen W, Wei Y, Dauk M, Zheng Z, 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(1-3);92-6. PMID: 12586344

Walz02: Walz AC, Demel RA, de Kruijff B, Mutzel R (2002). "Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic alpha-helix." Biochem J 365(Pt 2);471-9. PMID: 11955283


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, biocyc12.