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