000133399 001__ 133399
000133399 005__ 20250923084427.0
000133399 0247_ $$2doi$$a10.3390/ijms25063174
000133399 0248_ $$2sideral$$a138103
000133399 037__ $$aART-2024-138103
000133399 041__ $$aeng
000133399 100__ $$aRivero, Maribel$$uUniversidad de Zaragoza
000133399 245__ $$aPyridoxal 5'-phosphate biosynthesis by pyridox-(am)-ine 5'-phosphate oxidase: species-specific features
000133399 260__ $$c2024
000133399 5060_ $$aAccess copy available to the general public$$fUnrestricted
000133399 5203_ $$aEnzymes reliant on pyridoxal 5′-phosphate (PLP), the metabolically active form of vitamin B6, hold significant importance in both biology and medicine. They facilitate various biochemical reactions, particularly in amino acid and neurotransmitter metabolisms. Vitamin B6 is absorbed by organisms in its non-phosphorylated form and phosphorylated within cells via pyridoxal kinase (PLK) and pyridox-(am)-ine 5′-phosphate oxidase (PNPOx). The flavin mononucleotide-dependent PNPOx enzyme converts pyridoxine 5′-phosphate and pyridoxamine 5′-phosphate into PLP. PNPOx is vital for both biosynthesis and salvage pathways in organisms producing B6 vitamers. However, for those depending on vitamin B6 as a nutrient, PNPOx participates only in the salvage pathway. Transferring the PLP produced via PNPOx to client apo-enzymes is indispensable for their catalytic function, proper folding and targeting of specific organelles. PNPOx activity deficiencies due to inborn errors lead to severe neurological pathologies, particularly neonatal epileptic encephalopathy. PNPOx maintains PLP homeostasis through highly regulated mechanisms, including structural alterations throughout the catalytic cycle and allosteric PLP binding, influencing substrate transformation at the active site. Elucidation at the molecular level of the mechanisms underlying PNPOx activity deficiencies is a requirement to develop personalized approaches to treat related disorders. Finally, despite shared features, the few PNPOx enzymes molecularly and functionally studied show species-specific regulatory properties that open the possibility of targeting it in pathogenic organisms.
000133399 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E35-23R$$9info:eu-repo/grantAgreement/ES/MICINN/PID2022-136369NB-I00
000133399 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000133399 590__ $$a4.9$$b2024
000133399 592__ $$a1.273$$b2024
000133399 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b72 / 319 = 0.226$$c2024$$dQ1$$eT1
000133399 593__ $$aMedicine (miscellaneous)$$c2024$$dQ1
000133399 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b70 / 239 = 0.293$$c2024$$dQ2$$eT1
000133399 593__ $$aPhysical and Theoretical Chemistry$$c2024$$dQ1
000133399 593__ $$aComputer Science Applications$$c2024$$dQ1
000133399 593__ $$aInorganic Chemistry$$c2024$$dQ1
000133399 593__ $$aSpectroscopy$$c2024$$dQ1
000133399 593__ $$aOrganic Chemistry$$c2024$$dQ1
000133399 593__ $$aMolecular Biology$$c2024$$dQ2
000133399 593__ $$aCatalysis$$c2024$$dQ2
000133399 655_4 $$ainfo:eu-repo/semantics/review$$vinfo:eu-repo/semantics/publishedVersion
000133399 700__ $$aNovo, Nerea
000133399 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, Milagros$$uUniversidad de Zaragoza
000133399 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000133399 773__ $$g25, 6 (2024), 3174 [23 pp.]$$pInt. j. mol. sci.$$tInternational Journal of Molecular Sciences$$x1661-6596
000133399 8564_ $$s5649029$$uhttps://zaguan.unizar.es/record/133399/files/texto_completo.pdf$$yVersión publicada
000133399 8564_ $$s2784135$$uhttps://zaguan.unizar.es/record/133399/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000133399 909CO $$ooai:zaguan.unizar.es:133399$$particulos$$pdriver
000133399 951__ $$a2025-09-22-14:40:53
000133399 980__ $$aARTICLE