Stizolobate synthase (EC 1.13.11.29) is an enzyme that catalyzes the chemical reaction

Stizolobate synthase
Identifiers
EC no.1.13.11.29
CAS no.65979-39-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins

The two substrates of this enzyme are L-DOPA and oxygen. Its initial product is 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde.[1]

The intermediate readily cyclises and further oxidises, forming a 2-pyrone ring; this stizolobic acid, which is the product that is isolated and after which this enzyme is named.[2][3]

2D representation of the chemical structure of Q27098379.
intermediate
 
 
 
 
Rightward reaction arrow
 
 
 
 

The oxidation step uses oxidised nicotinamide adenine dinucleotide as a cofactor and the enzyme also requires zinc. It 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). It participates in tyrosine metabolism.[1]

Stizolobinic acid

A separate enzyme, stizolobinate synthase also present in higher plants cleaves L-DOPA in a way which produces the isomeric compound, stizolobinic acid.[3]

References

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  1. 1 2 Enzyme 1.13.11.29 at KEGG Pathway Database.
  2. 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.
  3. 1 2 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.