EC Number   |
General Information |
Reference |
|---|
  1.5.1.B7 | metabolism |
opine dehydrogenases (ODHs) from the bacterial pathogens, e.g. Staphylococcus aureus, Pseudomonas aeruginosa, and Yersinia pestis, perform the final enzymatic step in the biosynthesis of the class of opine metallophores, which includes staphylopine, pseudopaline, and yersinopine, respectively. Comparison of structure-function relationships, overview |
-, 748236 |
| 1.5.1.B7 | metabolism |
the NADPH is oxidized to NADP+ by the PaODH in the presence of Pseudomonas aeruginosa nicotianamine synthase (PaNAS), S-adenosyl-L-methionine (SAM) and the correct amino acid and 2-oxo acid substrates. Pyruvate, oxaloacetate, and 2-oxoglutarate are screened with SAM, but no oxidation is observed, suggesting that SAM alone is not sufficient as a substrate for PaNAS. Screening of 42 L- and D-amino acid substrates in combination with pyruvate, oxaloacetate, or 2-oxoglutarate reveals that several amino acids, L-threonine, L-asparagine, and L-hydroxyproline (L-Hyp), show limited turnover, while the combination of L-histidine and 2-oxoglutarate results in significant oxidation of NADPH by PaODH. PaNAS is specific for L-histidine |
-, 764141 |
| 1.5.1.B7 | more |
structure-function analysis, stereochemic reaction, overview. Active site structure involving Asp153 and substrate binding analysis. The histidine is positioned to act as a general acid/general base deprotonating the nucleophile and then donating the proton back to the 2-carbon hydroxyl leading to water release and Schiff base formation. HisNA is oriented with the imidazole moiety deep in the active site to confer stereoselectivity. This places the primary amine of the aminobutyrate proximal to the plane between the hydride and His242, positioning the substrate for nucleophilic attack. The nicotinamide ring hydride is 8.5 A distant from the histidine proton, too far for catalysis, further supporting the necessity of domain closure |
-, 748236 |
| 1.5.1.B7 | physiological function |
opine dehydrogenases (ODHs) from the bacterial pathogens, e.g. Staphylococcus aureus, Pseudomonas aeruginosa, and Yersinia pestis, perform the final enzymatic step in the biosynthesis of the class of opine metallophores, which includes staphylopine, pseudopaline, and yersinopine, respectively. Important role for this pathway in metal acquisition and virulence in humans, including in lung and burn-wound infections (Pseudomonas aeruginosa) and in blood and heart infections (Staphylococcus aureus) |
-, 748236 |
| 1.5.1.B7 | physiological function |
opine dehydrogenases (ODHs) typically form a secondary amine by condensation of an amino acid with an alpha-keto acid. Pseudomonas aeruginosa encodes the enzymes nicotianamine synthase (NAS) and opine dehydrogenase (ODH), biosynthesizing the nicotianamine-like opine metallophore pseudopaline |
-, 764141 |
| 1.5.1.B7 | physiological function |
PaODH catalyzes a reversible reaction that specifically produces the (R)-opine metallophore diastereomer, kinetic mechanism, overview |
-, 765055 |
