The enzyme 3,4-dihydroxyphenylalanine reductive deaminase (EC 4.3.1.22, reductive deaminase, DOPA-reductive deaminase, DOPARDA; systematic name 3,4-dihydroxy-L-phenylalanine ammonia-lyase (3,4-dihydroxyphenylpropanoate-forming))[1] catalyses the following chemical reaction
| 3,4-dihydroxyphenylalanine reductive deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.22 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- L-dopa 2 NADH 3,4-dihydroxyphenylpropanoate 2 NAD NH3
This enzyme participates in L-phenylalanine catabolism in the anaerobic phototrophic bacterium Rhodobacter sphaeroides OU5.
References
edit- ^ Ranjith NK, Sasikala C, Ramana C (2007). "Catabolism of L-phenylalanine and L-yrosine by Rhodobacter sphaeroides OU5 occurs through 3,4-dihydroxyphenylalanine". Research in Microbiology. 158 (6): 506–11. doi:10.1016/j.resmic.2007.04.008. PMID 17616348.506-11&rft.date=2007&rft_id=info:doi/10.1016/j.resmic.2007.04.008&rft_id=info:pmid/17616348&rft.aulast=Ranjith&rft.aufirst=NK&rft.au=Sasikala, C&rft.au=Ramana, C&rft_id=https://doi.org/10.1016%2Fj.resmic.2007.04.008&rfr_id=info:sid/en.wikipedia.org:3,4-dihydroxyphenylalanine reductive deaminase" class="Z3988">
External links
edit- 3,4-dihydroxyphenylalanine reductive deaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
