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Literature summary for 1.1.1.35 extracted from

  • Qin, Y.M.; Poutanen, M.H.; Helander, H.M.; Kvist, A.P.; Siivari, K.M.; Schmitz, W.; Conzelmann, E.; Hellman, U.; Hiltunen, J.K.
    Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization (1997), Biochem. J., 321, 21-28.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
Wistar rat
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.17
-
(S)-3-hydroxydecanoyl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I Rattus norvegicus
4.22
-
(S)-3-hydroxybutyryl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-3-hydroxybutyryl-CoA + NAD+
-
Rattus norvegicus 3-oxobutyryl-CoA + NADH + H+
-
?
(S)-3-hydroxydecanoyl-CoA + ?
-
Rattus norvegicus 3-oxodecanoyl-CoA + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
L-specific 3-hydroxyacyl-CoA dehydrogenase
-
Rattus norvegicus