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Literature summary for 4.2.1.17 extracted from

  • Engel, C.K.; Mathieu, M.; Zeelen, J.P.; Hiltunen, J.K.; Wierenga, R.K.
    Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket (1996), EMBO J., 15, 5135-5145.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method, crystal structure of the enzyme complexed with the potent inhibitor acetoacetyl-CoA, refined at 2.5 A resolution. The active site architecture confirms the importance of Glu164 as the catalytic acid for providing the alpha-proton during the hydratase reaction. It also shows the importance of Glu144 as the catalytic base for the activation of a water molecule in the hydratase reaction Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
acetoacetyl-CoA
-
Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Rattus norvegicus 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
161000
-
6 * 161000, the hexamer is a dimer of trimers Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P14604 the classification is ambiguous because the stereochemistry is not exactly determined
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Subunits

Subunits Comment Organism
hexamer 6 * 161000, the hexamer is a dimer of trimers Rattus norvegicus

Synonyms

Synonyms Comment Organism
mitochondrial enoyl coenzyme A hydratase the classification is ambiguous because the stereochemistry is not exactly determined Rattus norvegicus