Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase.
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Human PNPO catalyzes the terminal step of PLP synthesis; the purified recombinant enzyme is an FMN-containing homodimer with low turnover and low-micromolar KM for both PNP and PMP, and binds one PLP product molecule tightly per subunit (product inhibition).
"The purified human enzyme is a homodimer that exhibits a low catalytic rate constant of approximately 0.2 sec(-1)"
Genomic organization, tissue distribution and deletion mutation of human pyridoxine 5'-phosphate oxidase.
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Human brain PNPO expressed in E. coli; N-terminal 56-residue deletion does not affect coenzyme binding or activity; ubiquitous housekeeping-type expression highest in liver, skeletal muscle and kidney.
"deletion of the N-terminal 56 residues affects neither the binding of coenzyme nor catalytic activity."
Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase.
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Biallelic PNPO mutations cause PLP-responsive, pyridoxine-resistant neonatal epileptic encephalopathy; expression of human variants in CHO cells showed R229W markedly reduces oxidase activity and splice/stop mutations are null.
"having been resistant to treatment with pyridoxine,"
Widespread macromolecular interaction perturbations in human genetic disorders.
Architecture of the human interactome defines protein communities and disease networks.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
2xPNPO:2xFMN oxidizes PDXP to PXLP
2xPNPO:2xFMN oxidizes PXAP to PXLP