title: PdxH proteins of mycobacteria are typical members of the classical pyridoxine/pyridoxamine 5'-phosphate oxidase family.
abstract: Pyridoxal 5'-phosphate (PLP) biosynthesis is essential for the survival and virulence of Mycobacterium tuberculosis (Mtb). PLP functions as a cofactor for 58 putative PLP-binding proteins encoded by the Mtb genome and could also act as a potential antioxidant. De novo biosynthesis of PLP in Mtb takes place through the 'deoxyxylulose 5'-phosphate (DXP)-independent' pathway, whereas PdxH enzymes, possessing pyridoxine/pyridoxamine 5'-phosphate oxidase (PNPOx) activity, are involved in the PLP salvage pathway. In this study, we demonstrate that the annotated PdxH enzymes from various mycobacterial species are bona fide members of the classical PNPOx enzyme family, capable of producing PLP using both pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP) substrates.
authors.affiliation: Structural Biology Laboratory and Maurice Wilkins Centre for Molecular Biodiscovery, School of Biological Sciences, The University of Auckland, New Zealand.
authors.forename: Karthik
authors.initials: K
authors.lastname: Ankisettypalli
authors.affiliation: Structural Biology Laboratory and Maurice Wilkins Centre for Molecular Biodiscovery, School of Biological Sciences, The University of Auckland, New Zealand.
authors.forename: Jasmin Jo-Yu
authors.initials: JJ
authors.lastname: Cheng
authors.affiliation: Structural Biology Laboratory and Maurice Wilkins Centre for Molecular Biodiscovery, School of Biological Sciences, The University of Auckland, New Zealand.
authors.forename: Edward N
authors.initials: EN
authors.lastname: Baker
authors.affiliation: Structural Biology Laboratory and Maurice Wilkins Centre for Molecular Biodiscovery, School of Biological Sciences, The University of Auckland, New Zealand.
authors.forename: Ghader
authors.identifier: http://orcid.org/0000-0002-5092-3749
authors.initials: G
authors.lastname: Bashiri
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D009166:Mycobacterium leprae / Q000201:enzymology*; D019910:Mycobacterium marinum / Q000201:enzymology*; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D011732:Pyridoxal Phosphate / Q000031:analogs & derivatives / Q000096:biosynthesis / Q000737:chemistry; D011733:Pyridoxamine / Q000031:analogs & derivatives / Q000737:chemistry; D011734:Pyridoxaminephosphate Oxidase / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D011732:Pyridoxal Phosphate; D011733:Pyridoxamine; D011734:Pyridoxaminephosphate Oxidase; C010627:pyridoxamine phosphate; C024593:pyridoxine 5-phosphate
keywords: flavin mononucleotide; mycobacteria; pyridoxal 5′-phosphate; pyridoxine/pyridoxamine 5′-phosphate oxidase; salvage pathway