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Literature summary for 4.2.1.74 extracted from

  • Fong, J.C.; Schulz, H.
    Short-chain and long-chain enoyl-CoA hydratases from pig heart muscle (1981), Methods Enzymol., 71, 390-398.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by acetoacetyl-CoA Sus scrofa
N-Methylmaleimide
-
Sus scrofa
p-chloromercuribenzoate
-
Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
trans-2-decenoyl-CoA
-
Sus scrofa
0.024
-
trans-2-dodecenoyl-CoA
-
Sus scrofa
0.024
-
trans-2-octenoyl-CoA
-
Sus scrofa
0.024
-
trans-2-tetradecenoyl-CoA
-
Sus scrofa
0.045
-
trans-2-hexenoyl-CoA
-
Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Sus scrofa
-

Storage Stability

Storage Stability Organism
-20°C, purified enzyme is stable for several months Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with crotonyl-CoA Sus scrofa ?
-
?
trans-2-decenoyl-CoA + H2O 74% of the activity with trans-2-octenoyl-CoA Sus scrofa (3S)-3-hydroxydecanoyl-CoA
-
?
trans-2-dodecenoyl-CoA + H2O 42% of the activity with trans-2-octenoyl-CoA Sus scrofa (3S)-3-hydroxydodecanoyl-CoA
-
?
trans-2-hexenoyl-CoA + H2O 78% of the activity with trans-2-octenoyl-CoA Sus scrofa (3S)-3-hydroxyhexanoyl-CoA
-
?
trans-2-octenoyl-CoA + H2O best substrate Sus scrofa (3S)-3-hydroxyoctanoyl-CoA
-
?
trans-2-tetradecenoyl-CoA + H2O 34% of the activity with trans-2-octenoyl-CoA Sus scrofa (3S)-3-hydroxytetradecanoyl-CoA
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Sus scrofa