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1 ents an Escherichia coli mutant defective in pyridoxal kinase.
2 kidney cells confirmed that it encodes human pyridoxal kinase.
3 d residues that is homologous to a bacterial pyridoxal kinase.
4 rst for a novel family of "HMPP kinase-like" pyridoxal kinases.
5 now report the crystal structure of E. coli pyridoxal kinase 1 (ePL kinase 1), encoded by a pdxK gen
6 y been published, including Escherichia coli pyridoxal kinase 2 (ePL kinase 2) and sheep pyridoxal ki
8 dium significantly increased the activity of pyridoxal kinase and pyridoxamine 5'-phosphate oxidase.
9 ate by a preincubation with a combination of pyridoxal kinase and pyridoxine 5'-phosphate oxidase.
10 gh to account for product inhibition of both pyridoxal kinase and pyridoxine 5'-phosphate oxidase.
11 d active site flap types) of PdxY with other pyridoxal kinases as well as the ribokinase superfamily
13 K and pdxY genes have been found to code for pyridoxal kinases, enzymes involved in the pyridoxal pho
19 superfamily members reveal that B. subtilis pyridoxal kinase is more closely related in both sequenc
20 report on the characterization of T. brucei pyridoxal kinase (PdxK), an enzyme required for the salv
22 pyridoxal kinase 2 (ePL kinase 2) and sheep pyridoxal kinase, products of the pdxY and pdxK genes, r
23 doxine/pyridoxamine 5'-phosphate oxidase and pyridoxal kinase, respectively, are the only known genes
26 to the family of HMPP kinases than to other pyridoxal kinases, suggesting that this structure repres
28 ly of enzymes and has sequence homology with pyridoxal kinases that phosphorylate pyridoxal at the C-
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