Premium
Activity of Pyridoxamine as a Substrate for Brain Pyridoxal Kinase
Author(s) -
Gregory Jesse F.
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb06297.x
Subject(s) - pyridoxamine , pyridoxal , biochemistry , substrate (aquarium) , pyridoxine , chemistry , enzyme , phosphorylation , kinase , biology , ecology
The substrate activity of pyridoxamine (PM) for brain pyridoxal (PL) kinase was examined in view of a recent report which indicated that PM was a poor substrate for this enzyme. Bovine brain PL kinase was shown by liquid chromatography to catalyze the phosphorylation of PM ( K m = 65 μ m ). The identity of the reaction product, pyridoxamine 5′‐phosphate, was confirmed by its ability to act as a substrate for liver pyridoxine (pyridoxamine) 5′‐phosphate oxidase. These results, which indicate that PM is a good substrate for brain PL kinase, are consistent with the proposed role of intracellular phosphorylation in the uptake of vitamin B‐6 brain tissue.