EC Number   |
General Information |
Reference  |
|---|
    2.7.1.35 | physiological function |
pyridoxal kinase is a key enzyme in the metabolism of vitamin B6 |
722183 |
| 2.7.1.35 | physiological function |
the enzyme is essential for growth of Trypanosoma brucei in vitro and for infectivity in mice |
723219 |
| 2.7.1.35 | malfunction |
root growth of a sos4 mutant is significantly decreased when grown on either 100 mM or 200 mM sucrose as compared to root growth on10 mM sucrose. The sos4 mutant plant accumulates phytoglycogen |
723449 |
| 2.7.1.35 | physiological function |
the SOS4 pyridoxal kinase is required for maintenance of vitamin B6-mediated processes in chloroplasts. SOS4 is required for maintenance of phosphorylated B6 vitamer concentrations in chloroplasts |
723449 |
| 2.7.1.35 | more |
experimental resurrection of the last common ancestor of the hydroxymethyl pyrimidine kinase group based on comparison of hydroxymethyl pyrimidine and pyridoxal kinases. Probably the last common ancestor was not able to use pyridoxal under physiological conditions. The pyridoxal kinase activity present in the current bifunctional enzymes must have appeared in a convergent event independently of the pyridoxal kinase activity of pdxY and pdxK genes. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor |
738234 |
| 2.7.1.35 | physiological function |
vitamin B6 enters the cells after hydrolysis of the phosphorylated forms by the membrane-bound tissue non-specific alkaline phosphatase (TNSALP, EC 3.1.3.1). Once inside the cells, pyridoxal kinase (PL kinase, PDXK, EC 2.7.1.35) phosphorylates the hydroxymethyl group of PL, PN and PM to their respective 5'-phosphate forms |
758844 |
| 2.7.1.35 | evolution |
pyridoxine/pyridoxal kinase (PdxK) belongs to the ribokinase family and is involved in the vitamin B6 salvage pathway by phosphorylating pyridoxal (PL) into an active form. In the human malaria parasite, Plasmodium falciparum, PfPdxK functions to salvage vitamin B6 from both itself and its host |
759093 |
| 2.7.1.35 | more |
a FIxxIIxL motif at the C-terminus of the disordered repeat motif (XNXH)m that is implicated in binding the WD40 domain and may provide temporal control of PfPdxK through an interaction with a E3 ligase complex. Molecular docking and modelling, overview. Binding structure of AMP-PNP with PdxK |
759093 |
| 2.7.1.35 | physiological function |
pyridoxine/pyridoxal kinase (PdxK) belongs to the ribokinase family and is involved in the vitamin B6 salvage pathway by phosphorylating pyridoxal (PL) into an active form. In the human malaria parasite, Plasmodium falciparum, PfPdxK functions to salvage vitamin B6 from both itself and its host |
759093 |
| 2.7.1.35 | physiological function |
biotransformation of pyridoxal to pyridoxal 5'-phosphate (PLP) by pyridoxal kinase (pdxY) supports cadaverine production in Escherichia coli. PLP is an essential cofactor of lysine decarboxylase and the major bottleneck in the cadaverine biosynthesis pathway |
759126 |
