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Literature summary extracted from

  • Hartmann, D.; Philipp, R.; Schmadel, K.; Birktoft, J.J.; Banaszak, L.J.; Trommer, W.E.
    Spatial arrangement of coenzyme and substrates bound to L-3-hydroxyacyl-CoA dehydrogenase as studied by spin-labeled analogues of NAD+ and CoA (1991), Biochemistry, 30, 2782-2790.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.35 0.08
-
acetoacetyl-pantetheine
-
Sus scrofa
1.1.1.35 1.4
-
acetoacetyl-N-beta-alanylcysteamine
-
Sus scrofa
1.1.1.35 10
-
acetoacetyl-N-acetylcysteamine
-
Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.35 (S)-3-hydroxybutyryl-CoA + NAD+ Sus scrofa
-
acetoacetyl-CoA + NADH
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.35 Sus scrofa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.35 (S)-3-hydroxybutyryl-CoA + NAD+
-
Sus scrofa acetoacetyl-CoA + NADH
-
r
1.1.1.35 acetoacetyl-cysteamine-2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid amide + NADH
-
Sus scrofa (S)-3-hydroxybutyryl-cysteamine-2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid amide + NAD+
-
r
1.1.1.35 acetoacetyl-N-acetylcysteamine + NADH
-
Sus scrofa (S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
r
1.1.1.35 acetoacetyl-N-beta-alanylcysteamine + NADH
-
Sus scrofa (S)-3-hydroxybutyryl-N-beta-alanylcysteamine + NAD+
-
r
1.1.1.35 acetoacetyl-pantetheine + NADH
-
Sus scrofa (S)-3-hydroxybutyryl-pantetheine
-
r
1.1.1.35 acetoacetyl-pantetheine-4'-(2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid ester) + NADH
-
Sus scrofa (S)-3-hydroxybutyryl-pantetheine-4'-(2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid ester) + NAD+
-
r

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.35 NAD+
-
Sus scrofa