133399 20260217205506.0 doi 10.3390/ijms25063174 sideral 138103 ART-2024-138103 eng Rivero, Maribel Universidad de Zaragoza Pyridoxal 5'-phosphate biosynthesis by pyridox-(am)-ine 5'-phosphate oxidase: species-specific features 2024 Access copy available to the general public Unrestricted Enzymes reliant on pyridoxal 5′-phosphate (PLP), the metabolically active form of vitamin B6, hold significant importance in both biology and medicine. They facilitate various biochemical reactions, particularly in amino acid and neurotransmitter metabolisms. Vitamin B6 is absorbed by organisms in its non-phosphorylated form and phosphorylated within cells via pyridoxal kinase (PLK) and pyridox-(am)-ine 5′-phosphate oxidase (PNPOx). The flavin mononucleotide-dependent PNPOx enzyme converts pyridoxine 5′-phosphate and pyridoxamine 5′-phosphate into PLP. PNPOx is vital for both biosynthesis and salvage pathways in organisms producing B6 vitamers. However, for those depending on vitamin B6 as a nutrient, PNPOx participates only in the salvage pathway. Transferring the PLP produced via PNPOx to client apo-enzymes is indispensable for their catalytic function, proper folding and targeting of specific organelles. PNPOx activity deficiencies due to inborn errors lead to severe neurological pathologies, particularly neonatal epileptic encephalopathy. PNPOx maintains PLP homeostasis through highly regulated mechanisms, including structural alterations throughout the catalytic cycle and allosteric PLP binding, influencing substrate transformation at the active site. Elucidation at the molecular level of the mechanisms underlying PNPOx activity deficiencies is a requirement to develop personalized approaches to treat related disorders. Finally, despite shared features, the few PNPOx enzymes molecularly and functionally studied show species-specific regulatory properties that open the possibility of targeting it in pathogenic organisms. info:eu-repo/grantAgreement/ES/DGA/E35-23R info:eu-repo/grantAgreement/ES/MICINN/PID2022-136369NB-I00 info:eu-repo/semantics/openAccess by https://creativecommons.org/licenses/by/4.0/deed.es 4.9 2024 BIOCHEMISTRY & MOLECULAR BIOLOGY 72 / 320 = 0.225 2024 Q1 T1 CHEMISTRY, MULTIDISCIPLINARY 70 / 239 = 0.293 2024 Q2 T1 1.273 2024 Medicine (miscellaneous) 2024 Q1 Physical and Theoretical Chemistry 2024 Q1 Computer Science Applications 2024 Q1 Inorganic Chemistry 2024 Q1 Spectroscopy 2024 Q1 Organic Chemistry 2024 Q1 Molecular Biology 2024 Q2 Catalysis 2024 Q2 9.0 2024 info:eu-repo/semantics/review info:eu-repo/semantics/publishedVersion Novo, Nerea Medina, Milagros Universidad de Zaragoza (orcid)0000-0001-8743-0182 1002 060 Universidad de Zaragoza Dpto. Bioq.Biolog.Mol. Celular Área Bioquímica y Biolog.Mole. 25, 6 (2024), 3174 [23 pp.] Int. j. mol. sci. International Journal of Molecular Sciences 1661-6596 5649029 http://zaguan.unizar.es/record/133399/files/texto_completo.pdf Versión publicada 2784135 http://zaguan.unizar.es/record/133399/files/texto_completo.jpg?subformat=icon icon Versión publicada oai:zaguan.unizar.es:133399 articulos driver 2026-02-17-20:23:31 ARTICLE