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MetaCyc Enzyme: glutaryl-CoA dehydrogenase

Gene: gcdH Accession Number: G-4001 (MetaCyc)

Synonyms: GCD

Species: Pseudomonas Sp. K172

Subunit composition of glutaryl-CoA dehydrogenase = [GcdH]4
         glutaryl-CoA dehydrogenase subunit = GcdH

Summary:
Glutaryl-CoA dehydrogenase is a key enzyme present in all three kingdoms of life. In humans, it is a mitochondrial protein, and defficiency in its activity results in the disease glutaric aciduria type 1 (GA1), a relatively common cause of acute metabolic brain damage in infants [Goodman01].

Glutaryl-CoA dehydrogenase is a dual function enzyme, which also catalyzes the reaction of glutaconyl-CoA decarboxylase, resulting in crotonyl-CoA. Glutaconyl-CoA is an intermediate in the overall oxidative decarboxylation of glutaryl-CoA [Hartel93].

The enzymes express at high level when cells of Pseudomonas strains KB 740 and K 172 were grown on benzoate or other aromatic compounds under anaerobic conditions. Similar activity was also detected in cell-free extracts of Rhodopseudomonas, Rhodomicrobium and Rhodocyclus after phototrophic growth on benzoate.

Enzymes have been purified from the two Pseudomonas strains, and were found to be very similar. Both were homotetramers with a molecular weight of 170 kDa, and contained 1 mol of FAD per subunit [Hartel93].

The bi-functional glutaryl-CoA dehydrogenases that depend on ETF (electron-transfer flavoprotein) form one class of glutaconyl-CoA decarboxylases. A second class of these enzymes exists which depends on biotin rather than FAD. Enzymes that belong to the other class have been purified from glutamate fermenting bacteria (see glutaconyl-CoA decarboxylase) [Beatrix90].

Molecular Weight of Polypeptide: 41 kD (experimental) [Hartel93 ]

Molecular Weight of Multimer: 170 kD (experimental) [Hartel93]

Relationship Links: Entrez-Nucleotide:PART-OF:AE016774

Gene-Reaction Schematic: ?

MultiFun Terms: metabolism carbon utilization carbon compounds

Credits:
Created 06-Jun-2006 by Caspi R , SRI International


Enzymatic reaction of: glutaconyl-CoA decarboxylase (glutaryl-CoA dehydrogenase)

EC Number: 4.1.1.70

(E)-glutaconyl-CoA + H+ <=> CO2 + crotonyl-CoA

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

In Pathways: glutaryl-CoA degradation

Cofactors or Prosthetic Groups: FAD [Hartel93]


Enzymatic reaction of: glutaryl-CoA dehydrogenase

glutaryl-CoA + an oxidized electron-transfer flavoprotein + H+ <=> (E)-glutaconyl-CoA + a reduced electron-transfer flavoprotein

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

In Pathways: glutaryl-CoA degradation

Cofactors or Prosthetic Groups: FAD [Hartel93]

Kinetic Parameters:

Substrate
Km (μM)
Citations
glutaryl-CoA
3.0
[Hartel93]


Enzymatic reaction of: glutaryl-CoA dehydrogenase

EC Number: 1.3.8.6

glutaryl-CoA + an oxidized electron-transfer flavoprotein <=> crotonyl-CoA + CO2 + a reduced electron-transfer flavoprotein

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

Reversibility of this reaction is unspecified.

Alternative Substrates for glutaryl-CoA: (E)-glutaconyl-CoA [Hartel93 ]

In Pathways: glutaryl-CoA degradation

Cofactors or Prosthetic Groups: FAD [Hartel93]

Kinetic Parameters:

Substrate
Km (μM)
Citations
glutaryl-CoA
3.0
[Hartel93]


References

Beatrix90: Beatrix B, Bendrat K, Rospert S, Buckel W (1990). "The biotin-dependent sodium ion pump glutaconyl-CoA decarboxylase from Fusobacterium nucleatum (subsp. nucleatum). Comparison with the glutaconyl-CoA decarboxylases from gram-positive bacteria." Arch Microbiol 154(4);362-9. PMID: 2244788

Goodman01: Goodman SI (2001). "Prenatal diagnosis of glutaric acidemias." Prenat Diagn 21(13);1167-8. PMID: 11787045

Hartel93: Hartel U, Eckel E, Koch J, Fuchs G, Linder D, Buckel W (1993). "Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate." Arch Microbiol 1993;159(2);174-81. PMID: 8439237


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc14.