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Literature summary for 1.3.8.6 extracted from

  • Rao, K.S.; Vander Velde, D.; Dwyer, T.M.; Goodman, S.I.; Frerman, F.E.
    Alternate substrates of human glutaryl-CoA dehydrogenase: Structure and reactivity of substrates, and identification of a novel 2-enoyl-CoA product (2002), Biochemistry, 41, 1274-1284.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003 0.005 glutaryl-CoA
-
Homo sapiens
0.0066
-
glutaramyl-CoA
-
Homo sapiens
0.014
-
4-nitrobutyryl-CoA
-
Homo sapiens
0.02
-
methyl-glutaryl-CoA
-
Homo sapiens
0.024
-
pentanoyl-CoA
-
Homo sapiens
0.085
-
hexanoyl-CoA
-
Homo sapiens
0.105
-
5-hexenoyl-CoA
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
recombinant enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrobutyryl-CoA + acceptor
-
Homo sapiens 4-nitro-but-2-enoyl-CoA + reduced acceptor
-
?
5-hexenoyl-CoA + acceptor
-
Homo sapiens ? + reduced acceptor
-
?
glutaramyl-CoA + acceptor
-
Homo sapiens ? + reduced acceptor
-
?
glutaryl-CoA + acceptor acceptor: ferrocenium hexafluorophosphate Homo sapiens crotonyl-CoA + CO2 + reduced acceptor
-
?
hexanoyl-CoA + acceptor
-
Homo sapiens ? + reduced acceptor
-
?
methyl-glutaryl-CoA + acceptor
-
Homo sapiens methyl-crotonyl-CoA + reduced acceptor
-
?
pentanoyl-CoA + acceptor
-
Homo sapiens ? + reduced acceptor
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.023
-
glutaryl-CoA oxidase activity Homo sapiens
0.033
-
4-nitrobutyryl-CoA oxidase activity Homo sapiens