A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2018; you can also visit the original URL.
The file type is
Conformational Changes in the Reaction of Pyridoxal Kinase
Journal of Biological Chemistry
To understand the processes involved in the catalytic mechanism of pyridoxal kinase (PLK), 1 we determined the crystal structures of PLK⅐AMP-PCP-pyridoxamine, PLK⅐ADP⅐PLP, and PLK⅐ADP complexes. Comparisons of these structures have revealed that PLK exhibits different conformations during its catalytic process. After the binding of AMP-PCP (an analogue that replaced ATP) and pyridoxamine to PLK, this enzyme retains a conformation similar to that of the PLK⅐ATP complex. The distance between thedoi:10.1074/jbc.m312380200 pmid:14722069 fatcat:c2sbiylmqvdqhlq5qctqgxj6aq