| stizolobate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.13.11.29 | ||||||||
| CAS no. | 65979-39-7 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a stizolobate synthase (EC 1.13.11.29) is an enzyme that catalyzes the chemical reaction
- 3,4-dihydroxy-L-phenylalanine + O2 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
Thus, the two substrates of this enzyme are 3,4-dihydroxy-L-phenylalanine and O2, whereas its product is 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-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-dihydroxy-L-phenylalanine:oxygen 4,5-oxidoreductase (recyclizing). This enzyme participates in tyrosine metabolism. It employs one cofactor, zinc.
References
- Saito K, Komamine A (1976). "Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo". Eur. J. Biochem. 68 (1): 237–43. doi:10.1111/j.1432-1033.1976.tb10783.x. PMID 9285.
- Saito K, Komamine A (1978). "Biosynthesis of stizolobinic acid and stizolobic acid in higher plants". Eur. J. Biochem. 82 (2): 385–92. doi:10.1111/j.1432-1033.1978.tb12033.x. PMID 624278.
This page was last edited on 26 August 2023, at 15:54