3,4-dihydroxyphenylacetate 2,3-dioxygenase
In enzymology, a 3,4-dihydroxyphenylacetate 2,3-dioxygenase (EC 1.13.11.15) is an enzyme that catalyzes the chemical reaction
- 3,4-dihydroxyphenylacetate + O2 2-hydroxy-5-carboxymethylmuconate semialdehyde
| 3,4-dihydroxyphenylacetate 2,3-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.15 | ||||||||
| CAS no. | 37256-56-7 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are 3,4-dihydroxyphenylacetate and O2, whereas its product is 2-hydroxy-5-carboxymethylmuconate semialdehyde.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing). Other names in common use include 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase, HPC dioxygenase, and homoprotocatechuate 2,3-dioxygenase. This enzyme participates in tyrosine metabolism. It employs one cofactor, iron.
Structural studies
As of late 2007, eight structures have been solved for this class of enzymes, with PDB accession codes 1F1R, 1F1U, 1F1V, 1F1X, 1Q0C, 1Q0O, 2IG9, and 2IGA.
References
- Adachi K, Takeda Y, Senoh S, Kita H (December 1964). "Metabolism of P-Hydroxyphenylacetic Acid In Pseudomonas ovalis". Biochimica et Biophysica Acta (BBA) - General Subjects. 93 (3): 483–93. doi:10.1016/0304-4165(64)90332-0. PMID 14263147.
- Barbour MG, Bayly RC (September 1981). "Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida". Journal of Bacteriology. 147 (3): 844–50. doi:10.1128/JB.147.3.844-850.1981. PMC 216120. PMID 6895079.
- Kutty RK, Devi NA, Veeraswamy M, Ramesh S, Rao PV (October 1977). "Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde". The Biochemical Journal. 167 (1): 163–70. doi:10.1042/bj1670163. PMC 1183633. PMID 588248.