Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.17 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
Search for more literature for 4.2.1.17

Activating Compound

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

Protein Variants

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Rattus norvegicus P14604
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotonyl-CoA + H2O stereoselective reaction mechanism, Glu144 and Glu164 are essential for ECH catalysis, overview Rattus norvegicus (3S)-3-hydroxybutanoyl-CoA
-
 ?
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 ?
-
 ?
additional information ECH (XI) also has enoyl-CoA isomerase activity at approximately 1/5000 the level of its hydratase activity, overview Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
ECH
-
 Rattus norvegicus
More crotonase superfamily enzyme Rattus norvegicus