3-oxoadipate enol-lactonase
| 3-oxoadipate enol-lactonase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 3-Oxoadipate enol-lactonase homodimer, Paraburkholderia xenovorans | |||||||||
| Identifiers | |||||||||
| EC no. | 3.1.1.24 | ||||||||
| CAS no. | 9031-04-3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
3-oxoadipate enol-lactonase (EC 3.1.1.24) is an enzyme that catalyzes the reaction
β-ketoadipate enol lactone
H2O
β-ketoadipic acid
The enzyme characterised from Pseudomonas putida hydrolyses the enol lactone, 5-oxo-4,5-dihydro-2-furylacetic acid, to β-ketoadipic acid.The reaction is part of a pathway that breaks down the antioxidant, protocatechuic acid,[1][2] and other aromatic compounds.[3][4]
This enzyme is a hydrolase, specifically one acting on carboxylic ester bonds. The systematic name is 4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase. Other names in common use include carboxymethylbutenolide lactonase, β-ketoadipic enol-lactone hydrolase, 3-ketoadipate enol-lactonase, 3-oxoadipic enol-lactone hydrolase, and β-ketoadipate enol-lactone hydrolase.[5]
References
- ↑ Ornston LN (August 1966). "The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. II. Enzymes of the protocatechuate pathway". The Journal of Biological Chemistry. 241 (16): 3787–94. doi:10.1016/S0021-9258(18)99840-6. PMID 5916392.
- ↑ Ornston LN (1970). "Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida)". Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida). Methods Enzymol. Vol. 17A. pp. 529–549. doi:10.1016/0076-6879(71)17237-0. ISBN 978-0-12-181874-6.
- ↑ Bains, Jasleen; Kaufman, Laura; Farnell, Benjamin; Boulanger, Martin J. (2011). "A Product Analog Bound Form of 3-Oxoadipate-enol-Lactonase (PcaD) Reveals a Multifunctional Role for the Divergent Cap Domain". Journal of Molecular Biology. 406 (5): 649–658. doi:10.1016/j.jmb.2011.01.007. PMID 21237173.
- ↑ Diaz Ortiz, Laura L.; Botero-Rozo, David; Vargas, Natalia; Ortiz, Sandra; Restrepo, Silvia; Vives, Martha J. (2025). "Deciphering the phenol degradation metabolic pathway in Scedosporium apiospermum HDO1". Applied and Environmental Microbiology. 91 (8) e01038-25. doi:10.1128/aem.01038-25. PMC 12366324. PMID 40637408.
- ↑ Enzyme 3.1.1.24 at KEGG Pathway Database.
Categories: