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Literature summary for 1.1.1.36 extracted from

  • Hiltunen, J.K.; Wenzel, B.; Beyer, A.; Erdmann, R.; Fossa, A.; Kunau, W.H.
    Peroxisomal multifunctional beta-oxidation protein of Saccharomyces cerevisiae. Molecular analysis of the fox2 gene and gene product (1992), J. Biol. Chem., 267, 6646-6653.
    View publication on PubMed
Search for more literature for 1.1.1.36

Protein Variants

Protein Variants Comment Organism
truncated version truncated version (lacking the carboxyl-terminal 271 amino acids). The truncated form contains only the D-3-hydroxyacyl-CoA dehydrogenase activity Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-3-hydroxyacyl-CoA + NAD+ Saccharomyces cerevisiae
-
 3-ketoacyl-CoA + NADH + H+
-
 ?
D-3-hydroxyacyl-CoA + NAD+ Saccharomyces cerevisiae fox2
-
 3-ketoacyl-CoA + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 fox2 mutant strain
-
Saccharomyces cerevisiae fox2
-
 fox2 mutant strain
-

Purification (Commentary)

Purification (Comment) Organism
the FOX2 gene is overexpressed from a multicopy vector (YEp352) in Saccharomyces cerevisiae and the gene product purified to apparent homogenity. A truncated version of MFP lacking 271 carboxyl-terminal amino acids is also overexpressed and purified Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-3-hydroxyacyl-CoA + NAD+
-
 Saccharomyces cerevisiae 3-ketoacyl-CoA + NADH + H+
-
 ?
D-3-hydroxyacyl-CoA + NAD+
-
 Saccharomyces cerevisiae fox2 3-ketoacyl-CoA + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
D-3-hydroxyacyl-CoA dehydrogenase part of the multifunctional protein (MFP) containing crotonase, L-3-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and 3-hydroxyacyl-CoA epimerase Saccharomyces cerevisiae