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Literature summary extracted from

  • Haapalainen, A.M.; Koski, M.K.; Qin, Y.M.; Hiltunen, J.K.; Glumoff, T.
    Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution (2003), Structure, 11, 87-97.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.36 expression of a truncated enzyme, comprising residues Met1-Asp319 of the dehydrogenase region, lacking the hydratase-2 region, in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.36 selenomethionine-labeled recombinant truncated enzyme, X-ray diffraction structure determination and analysis at 2.38 A resolution Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.36 peroxisome enzyme contains a C-terminal peroxisomal targeting signal sequence Rattus norvegicus 5777
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.36 (R)-3-hydroxybutyryl-CoA Rattus norvegicus dehydration, multifunctional type 2 enzyme trans-2-butenoyl-CoA + H2O
-
 ?
1.1.1.36 (R)-3-hydroxybutyryl-CoA + NAD+ Rattus norvegicus oxidation, multifunctional type 2 enzyme acetoacetyl-CoA + NADH
-
 ?
1.1.1.36 additional information Rattus norvegicus a point mutation in the dehydrogenase region of the enzyme causes peroxisomal disease leading to severe abnormalities and an early death ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.36 Rattus norvegicus
-
 multifunctional enzyme type 2, i.e. MFE-2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.36 recombinant truncated enzyme from Escherichia coli, to homogeneity Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.36 (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+ catalytic site structure and catalytic triad Ser151, Tyr164, and Lys168 Rattus norvegicus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.36 (R)-3-hydroxybutyryl-CoA dehydration, multifunctional type 2 enzyme Rattus norvegicus trans-2-butenoyl-CoA + H2O
-
 ?
1.1.1.36 (R)-3-hydroxybutyryl-CoA + NAD+ oxidation, multifunctional type 2 enzyme Rattus norvegicus acetoacetyl-CoA + NADH
-
 ?
1.1.1.36 additional information a point mutation in the dehydrogenase region of the enzyme causes peroxisomal disease leading to severe abnormalities and an early death Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.36 dimer crystal structure, enzyme shows a alpha/beta short chain alcohol dehydrogenase/reductase, i.e. SDR, fold Rattus norvegicus
1.1.1.36 More the recombinant truncated and selenomethionine-labeled enzyme has a molecular weight of 34602 Da as determined by mass spectrometry Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.36 (3R)-hydroxyacyl-CoA dehydrogenase
-
 Rattus norvegicus
1.1.1.36 MFE-2
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.36 NAD+ binding mode and conformation of NAD+ bound to the enzyme derived from the crystal structure, overview Rattus norvegicus