EC Number   |
General Information |
Reference |
|---|
  2.5.1.152 | metabolism |
the NADPH is oxidized to NADP+ by the Staphylococcus aureus SaODH (EC 1.5.1.52) in the presence of nicotianamine synthase (PaNAS), S-adenosyl-L-methionine (SAM,) and the correct amino acid and 2-oxo acid substrates. The combination of D-histidine and pyruvate results in significant oxidation of NADPH by SaODH |
-, 764141 |
| 2.5.1.152 | physiological function |
opine dehydrogenases (ODHs) typically form a secondary amine by condensation of an amino acid with an alpha-keto acid. Staphylococcus aureus encodes the enzymes nicotianamine synthase (NAS) and opine dehydrogenase (ODH), biosynthesizing the nicotianamine-like opine metallophore staphylopaline. In Staphylococcus aureus, ODH uses the primary amine of the D-histidine-aminobutyrate product of NAS as a nucleophile in a condensation with pyruvate followed by hydride transfer from NADPH. SaNAS is specific for D-histidine |
-, 764141 |
| 2.5.1.152 | physiological function |
the enzyme participates in the biosynthesis of the metallophore staphylopine. Staphylopine biosynthesis is impaired in the CntL mutant. The import of iron, zinc, nickel, and cobalt are all decreased in CntL mutants. CntL mutant strains are resistant to a concentration of cobalt that is toxic to the wild-type strain |
-, 749374 |
