Structural highlights
Function
PVDA_PSEAE Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as pyoverdin. Pyoverdin is a hydroxamate siderophore composed of a 6,7-dihydroxyquinoline-containing fluorescent chromophore joined to the N-terminus of a partly cyclic octapeptide (D-Ser-L-Arg-D-Ser-L-N(5)-OH-Orn-L-Lys-L-N(5)-OH-Orn-L-Thr-L-Thr in strain PAO1). Specific for NADPH, which plays a role in stabilization of the C4a-hydroperoxyflavin intermediate.[1] [2] [3]
References
- ↑ Ge L, Seah SY. Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa. J Bacteriol. 2006 Oct;188(20):7205-10. PMID:17015659 doi:https://dx.doi.org/10.1128/JB.00949-06
- ↑ Meneely KM, Barr EW, Bollinger JM Jr, Lamb AL. Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry. 2009 May 26;48(20):4371-6. doi: 10.1021/bi900442z. PMID:19368334 doi:https://dx.doi.org/10.1021/bi900442z
- ↑ Visca P, Ciervo A, Orsi N. Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa. J Bacteriol. 1994 Feb;176(4):1128-40. PMID:8106324
