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Literature summary extracted from

  • Wu, L.; Qiao, Y.; Gao, J.; Deng, G.; Yu, W.; Chen, G.; Li, D.
    Functional characterization of rat glutaryl-CoA dehydrogenase and its comparison with straight-chain acyl-CoA dehydrogenase (2011), Bioorg. Med. Chem. Lett., 21, 6667-6673.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.3.8.6 E370A site-directed mutagenesis, inactive mutant Rattus norvegicus
1.3.8.6 E370Q site-directed mutagenesis, the mutant shows highy reduced activity compared to the wild-type enzyme Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.8.6 2-pentynoyl-CoA inactivates GCD Rattus norvegicus
1.3.8.6 oct-2-yn-4-enoyl-CoA irreversible and most likely involved covalent modification of the apoenzyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.8.6 additional information
-
 additional information kinetics with medium chain acyl-CoA substrates, overview Rattus norvegicus
1.3.8.6 0.035
-
 glutaryl-CoA mutant E370Q, pH and temperature not specified in the publication Rattus norvegicus
1.3.8.6 3.8
-
 glutaryl-CoA wild-type enzyme, pH and temperature not specified in the publication Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.8.6 glutaryl-CoA + FAD Rattus norvegicus GCD catalyzes the oxidative decarboxylation of the gamma-carboxylate of the substrate, glutaryl-CoA, to yield crotonyl-CoA and CO2. (E)-but-2-enoyl-CoA + CO2 + FADH2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.6 Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.6 glutaryl-CoA + FAD
-
 Rattus norvegicus (E)-but-2-enoyl-CoA + CO2 + FADH2
-
 ?
1.3.8.6 glutaryl-CoA + FAD GCD catalyzes the oxidative decarboxylation of the gamma-carboxylate of the substrate, glutaryl-CoA, to yield crotonyl-CoA and CO2. Rattus norvegicus (E)-but-2-enoyl-CoA + CO2 + FADH2
-
 ?
1.3.8.6 additional information the enzyme is also active with butyryl-CoA, hexanoyl-CoA, octanoyl-CoA, and decanoyl-CoA, but is inactive with decanoyl-CoA and dodecanoyl-CoA, substrate specificity, overview Rattus norvegicus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.8.6 GCD
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.8.6 0.004
-
 glutaryl-CoA wild-type enzyme, pH and temperature not specified in the publication Rattus norvegicus
1.3.8.6 0.012
-
 glutaryl-CoA mutant E370Q, pH and temperature not specified in the publication Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.8.6 FAD
-
 Rattus norvegicus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.8.6 additional information
-
 additional information inhibition kinetics Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.3.8.6 evolution the enzyme is a member of the acyl-CoA dehydrogenase (ACD) family of flavoproteins Rattus norvegicus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.3.8.6 2.9
-
 glutaryl-CoA mutant E370Q, pH and temperature not specified in the publication Rattus norvegicus
1.3.8.6 950
-
 glutaryl-CoA wild-type enzyme, pH and temperature not specified in the publication Rattus norvegicus