Recombinant Pseudomonas Aeruginosa L-Ornithine 5-Monooxygenase (PVDA) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-04127P

Greater than 90% as determined by SDS-PAGE.
Recombinant Pseudomonas Aeruginosa L-Ornithine 5-Monooxygenase (PVDA) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-04127P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Pseudomonas Aeruginosa L-Ornithine 5-Monooxygenase (PVDA) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | Q51548 |
Target Symbol | PVDA |
Synonyms | pvdA; pvd-1; PA2386; L-ornithine N(5)-monooxygenase; EC 1.14.13.195; L-ornithine N(5)-hydroxylase; Ornithine hydroxylase; L-ornithine N(5)-oxygenase; Pyoverdin biosynthesis protein A |
Species | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
Expression System | E.coli |
Tag | N-6His-SUMO |
Target Protein Sequence | MTQATATAVVHDLIGVGFGPSNIALAIALQERAQAQGALEVLFLDKQGDYRWHGNTLVSQSELQISFLKDLVSLRNPTSPYSFVNYLHKHDRLVDFINLGTFYPCRMEFNDYLRWVASHFQEQSRYGEEVLRIEPMLSAGQVEALRVISRNADGEELVRTTRALVVSPGGTPRIPQVFRALKGDGRVFHHSQYLEHMAKQPCSSGKPMKIAIIGGGQSAAEAFIDLNDSYPSVQADMILRASALKPADDSPFVNEVFAPKFTDLIYSREHAERERLLREYHNTNYSVVDTDLIERIYGVFYRQKVSGIPRHAFRCMTTVERATATAQGIELALRDAGSGELSVETYDAVILATGYERQLHRQLLEPLAEYLGDHEIGRDYRLQTDERCKVAIYAQGFSQASHGLSDTLLSVLPVRAEEISGSLYQHLKPGTAARALHEHALAS |
Expression Range | 1-443aa |
Protein Length | Full Length |
Mol. Weight | 65.5kDa |
Research Area | Others |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target Function | 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. |
Subcellular Location | Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. |
Protein Families | Lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family |
Database References | KEGG: pae:PA2386 STRING: 208964.PA2386 |
Gene Functions References
- PvdA is a membrane-associated protein located at the old cell pole PMID: 22498339
- The first two structures of a class B N-hydroxylating monooxygenase were determined with FAD in oxidized (1.9 A resolution) and reduced (3.03 A resolution) states PMID: 21757711
- overexpression and purification of active recombinant L-ornithine N5-hydroxylase, PvdA; detailed steady-state kinetic analysis to determine the substrate and coenzyme specificities PMID: 17015659
- The membrane topogenic determinants of PvdA were studies, and PvdA appears to have a single N-terminal domain anchored to the inner membrane. PMID: 18757814
- PvdA employs a kinetic mechanism that is a hybrid of those previously documented for other flavin-dependent hydroxylases PMID: 19368334