Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Human pyridoxal kinase: overexpression and properties of the recombinant enzyme.
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Recombinant human pyridoxal kinase phosphorylates vitamin B6; Zn2+ is the most effective divalent cation and the enzyme is optimally active at pH 5.5-6.0.
"Zn2+ is the most effective divalent cation in the phosphorylation of pyridoxal, and the human enzyme has maximum catalytic activity in the narrow pH range of 5.5-6.0."
Crystal structure of human pyridoxal kinase.
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Human pyridoxal kinase is a ribokinase-superfamily enzyme that catalyzes ATP-dependent phosphorylation of vitamin B6; solved as a homodimer.
"Pyridoxal kinase, a member of the ribokinase superfamily, catalyzes the ATP-dependent phosphorylation reaction of vitamin B6 and is an essential enzyme in the formation of pyridoxal-5'-phosphate"
Cell array-based intracellular localization screening reveals novel functional features of human chromosome 21 proteins.
Crystal Structure of human pyridoxal kinase: structural basis of M(+) and M(2+) activation.
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Human pyridoxal kinase phosphorylates all three B6 vitamers; Mg2+ and Na+ act in tandem to anchor ATP at the active site, and K+/Na+ modulate activity.
"The crystal structure of the MgATP complex also reveals Mg(2+) and Na(+) acting in tandem to anchor the ATP at the active site."
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Kinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase.
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Active-site Asp235 is important for pyridoxal kinase activity; mutation lowers substrate affinity and turnover.
"A D235A variant shows 7-fold and 15-fold decreases in substrate affinity and activity, respectively."
Proteomic characterization of the human sperm nucleus.
PDXK mutations cause polyneuropathy responsive to pyridoxal 5'-phosphate supplementation.
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Biallelic PDXK mutations reduce enzyme activity and cellular PLP, causing an autosomal recessive axonal polyneuropathy with optic atrophy that responds to PLP supplementation.
"Low PDXK ATP binding resulted in decreased erythrocyte PDXK activity and low pyridoxal 5'-phosphate (PLP) concentrations."
Human pyridoxal kinase. cDNA cloning, expression, and modulation by ligands of the benzodiazepine receptor.
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cDNA cloning and expression confirm the protein is human pyridoxal kinase; ubiquitously expressed, abundant in testis, and inhibited by benzodiazepine receptor ligands.
"Transient expression of the cDNA in human embryonic kidney cells confirmed that it encodes human pyridoxal kinase."
Kinetic studies of the effects of K+, Na+ and Li+ on the catalytic activity of human erythrocyte pyridoxal kinase.
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Monovalent cations activate human erythrocyte pyridoxal kinase; K+ is the most effective, Na+ increases Vmax and ATP affinity, and Li+ is a poor activator.
"Among them, K+ is the most effective, improving both PK affinity for the substrates and maximal velocity."
Exocytosis of secretory granule lumen proteins
Exocytosis of specific granule lumen proteins
2xPDXK:2xZn2+ phosphorylates PXA
2xPDKX:2xZn2+ phosphorylates PDX
2xPDXK:2xZn2+ phosphorylates PXL