PdxH Proteins of Mycobacteria Are Typical Members of the Classical pyridoxine/pyridoxamine 5'-phosphate Oxidase Family

FEBS Lett. 2016 Feb;590(4):453-60. doi: 10.1002/1873-3468.12080. Epub 2016 Feb 15.

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.

Keywords: flavin mononucleotide; mycobacteria; pyridoxal 5′-phosphate; pyridoxine/pyridoxamine 5′-phosphate oxidase; salvage pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / classification
  • Bacterial Proteins / genetics
  • Mycobacterium leprae / enzymology*
  • Mycobacterium marinum / enzymology*
  • Mycobacterium tuberculosis / enzymology*
  • Pyridoxal Phosphate / analogs & derivatives
  • Pyridoxal Phosphate / biosynthesis
  • Pyridoxal Phosphate / chemistry
  • Pyridoxamine / analogs & derivatives
  • Pyridoxamine / chemistry
  • Pyridoxaminephosphate Oxidase / chemistry*
  • Pyridoxaminephosphate Oxidase / classification
  • Pyridoxaminephosphate Oxidase / genetics
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Pyridoxal Phosphate
  • Pyridoxamine
  • Pyridoxaminephosphate Oxidase
  • pyridoxamine phosphate
  • pyridoxine 5-phosphate