Acetoacetate decarboxylase
| Acetoacetate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Acetoacetate decarboxylase dodecamer structure with bound 2-Pentanone bound in its active sites. | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.1.4 | ||||||||
| CAS no. | 9025-03-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Acetoacetate decarboxylase (AAD or ADC) is an enzyme (EC 4.1.1.4) involved in both the ketone body production pathway in humans and other mammals, and solventogenesis in bacteria. Acetoacetate decarboxylase plays a key role in solvent production by catalyzing the decarboxylation of acetoacetate, yielding acetone and carbon dioxide.
This enzyme has been of particular interest because it is a classic example of how pKa values of ionizable groups in the enzyme active site can be significantly perturbed. Specifically, the pKa value of lysine 115 in the active site is unusually low, allowing for the formation of a Schiff base intermediate and catalysis.
| acetoacetic acid | Acetoacetate decarboxylase | acetone | |
| CO2 | |||
