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Literature summary extracted from

  • Hamed, R.B.; Batchelar, E.T.; Clifton, I.J.; Schofield, C.J.
    Mechanisms and structures of crotonase superfamily enzymes - how nature controls enolate and oxyanion reactivity (2008), Cell. Mol. Life Sci., 65, 2507-2527.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.17 CoA the enzyme is dependent on CoA Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.17 E144A site-directed mutagenesis, the mutant shows a 1000fold reduced activity compared to the wild-type enzyme Rattus norvegicus
4.2.1.17 E164A site-directed mutagenesis, the mutant shows a 1000fold reduced activity compared to the wild-type enzyme Rattus norvegicus

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.17 additional information Rattus norvegicus ECH catalyzes the reversible syn-addition of a water molecule across the double bond of a trans-2-enoyl-CoA, e.g. crotonyl-CoA, thioester to give a beta-hydroxyacyl-CoA thioester. The enzyme binds the substrates at the interface between monomers within the same trimer ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.17 Rattus norvegicus P14604
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.17 crotonyl-CoA + H2O stereoselective reaction mechanism, Glu144 and Glu164 are essential for ECH catalysis, overview Rattus norvegicus (3S)-3-hydroxybutanoyl-CoA
-
 ?
4.2.1.17 additional information ECH catalyzes the reversible syn-addition of a water molecule across the double bond of a trans-2-enoyl-CoA, e.g. crotonyl-CoA, thioester to give a beta-hydroxyacyl-CoA thioester. The enzyme binds the substrates at the interface between monomers within the same trimer Rattus norvegicus ?
-
 ?
4.2.1.17 additional information ECH (XI) also has enoyl-CoA isomerase activity at approximately 1/5000 the level of its hydratase activity, overview Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.17 More the enzyme binds the substrates at the interface between monomers within the same trimer, monomer structure, modelling in comparison to other crotonase superfamily enzymes, overview Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
4.2.1.17 ECH
-
 Rattus norvegicus
4.2.1.17 More crotonase superfamily enzyme Rattus norvegicus