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Literature summary for 1.3.8.6 extracted from

  • Rao, K.S.; Albro, M.; Dwyer, T.M.; Frerman, F.E.
    Kinetic mechanism of glutaryl-CoA dehydrogenase (2006), Biochemistry, 45, 15853-15861.
    View publication on PubMed
Search for more literature for 1.3.8.6

Protein Variants

Protein Variants Comment Organism
E370Q the dienolate intermediate observed upon decarboxylation of glutaconyl-CoA can be detected with E370Q GCD but not with wild-type, because the crotonyl-CoA dienolate forms a charge-transfer complex with the oxidized FAD and the substitution of a glutamine residue for Glu370 prevents rapid protonation of the dienolate Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0047
-
 glutaryl-CoA at pH 6.5 Homo sapiens
0.0081
-
 glutaryl-CoA at pH 7.6 Homo sapiens
0.034
-
 glutaryl-CoA at pH 8.5 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q92947
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutaconyl-CoA + acceptor
-
 Homo sapiens crotonyl-CoA + CO2 + reduced acceptor
-
 ?
glutaryl-CoA + acceptor
-
 Homo sapiens crotonoyl-CoA + CO2 + reduced acceptor
-
 ?

Synonyms

Synonyms Comment Organism
GCD
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.5
-
 glutaconyl-CoA
-
 Homo sapiens
5.6
-
 glutaryl-CoA at pH 6.5 Homo sapiens
11.3
-
 glutaryl-CoA at pH 7.6 Homo sapiens
13.2
-
 glutaryl-CoA at pH 8.5 Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD oxidation of reduced FAD is much faster than the chemical steps that occur in the active site of the enzyme Homo sapiens