This entry represents the N-terminal Rieske domain of the oxygenase alpha subunit of aminopyrrolnitrin oxygenase (PrnD). PrnD is a novel Rieske N-oxygenase that catalyzes the final step in the pyrrolnitrin biosynthetic pathway, the oxidation of the amino group in aminopyrrolnitrin to a nitro group, forming the antibiotic pyrrolnitrin. The biosynthesis of pyrrolnitrin is one of the best examples of enzyme-catalyzed arylamine oxidation. Although arylamine oxygenases are widely distributed within the microbial world and used in a variety of metabolic reactions, PrnD represents one of only two known examples of arylamine oxygenases or N-oxygenases involved in arylnitro group formation, the other being AurF involved in aureothin biosynthesis [, ].
Prion protein (PrP) is intimately linked with transmissible spongiform encephalopathies (TSEs). The human PrP gene (PRNP) locus contains three genes: PRNP, DOPPEL and PRND. A novel gene, designated PRNT, has been identified 3kb 3' to PRND and is transcribed to generate at least three alternatively spliced mRNAs. PRNT constitutes a family of putative prion-related proteins expressed in the testis [, ]. This group of eukaryotic proteins are typically between 52 and 94 amino acids in length.
