Literature summary 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.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.1.17 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.2.1.17 |
acetoacetyl-CoA |
- |
Rattus norvegicus |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
4.2.1.17 |
mitochondrion |
- |
Rattus norvegicus |
5739 |
- |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
4.2.1.17 |
161000 |
- |
6 * 161000, the hexamer is a dimer of trimers |
Rattus norvegicus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.1.17 |
Rattus norvegicus |
P14604 |
the classification is ambiguous because the stereochemistry is not exactly determined |
- |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
4.2.1.17 |
liver |
- |
Rattus norvegicus |
- |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.2.1.17 |
hexamer |
6 * 161000, the hexamer is a dimer of trimers |
Rattus norvegicus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.1.17 |
mitochondrial enoyl coenzyme A hydratase |
the classification is ambiguous because the stereochemistry is not exactly determined |
Rattus norvegicus |