L-lysine 6-monooxygenase (NADPH)
| L-lysine 6-monooxygenase (NADPH) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 L-lysine 6-monooxygenase tetramer + 44 I (l.blue), Pseudomonas syringae | |||||||||
| Identifiers | |||||||||
| EC no. | 1.14.13.59 | ||||||||
| CAS no. | 64295-82-5 | ||||||||
| 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 L-lysine 6-monooxygenase (NADPH) (EC 1.14.13.59) is an enzyme that catalyzes the chemical reaction
- L-lysine + NADPH + H+ + O2 N6-hydroxy-L-lysine + NADP+ + H2O
The 4 substrates of this enzyme are L-lysine, NADPH, H+, and O2, whereas its 3 products are N6-hydroxy-L-lysine, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is L-lysine,NADPH:oxygen oxidoreductase (6-hydroxylating). This enzyme is also called lysine N6-hydroxylase. This enzyme participates in lysine degradation.
References
[edit]- Plattner HJ, Pfefferle P, Romaguera A, Waschutza S, Diekmann H (1989). "Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222". Biol. Met. 2 (1): 1–5. doi:10.1007/BF01116193. PMID 2518519.
- Macheroux P, Plattner HJ, Romaguera A, Diekmann H (1993). "FAD and substrate analogs as probes for lysine N6-hydroxylase from Escherichia coli EN 222". Eur. J. Biochem. 213 (3): 995–1002. doi:10.1111/j.1432-1033.1993.tb17846.x. PMID 8504838.
- Thariath AM, Fatum KL, Valvano MA, Viswanatha T (1993). "Physico-chemical characterization of a recombinant cytoplasmic form of lysine: N6-hydroxylase". Biochim. Biophys. Acta. 1203 (1): 27–35. doi:10.1016/0167-4838(93)90032-M. PMID 8218389.
- de Lorenzo V, Bindereif A, Paw BH, Neilands JB (1986). "Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12". J. Bacteriol. 165 (2): 570–8. doi:10.1128/jb.165.2.570-578.1986. PMC 214457. PMID 2935523.
- Marrone L, Siemann S, Beecroft M, Viswanatha T (1996). "Specificity of lysine:N-6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism". Bioorganic Chemistry. 24 (4): 401–406. doi:10.1006/bioo.1996.0034.
- Goh CJ, Szczepan EW, Menhart N, Viswanatha T (1989). "Studies on lysine:N6-hydroxylation by cell-free systems of Aerobacter aerogenes 62-1". Biochim. Biophys. Acta. 990 (3): 240–5. doi:10.1016/s0304-4165(89)80040-6. PMID 2493814.
