Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/33713
Title: Conformational changes in the reaction of Pyridoxal Kinase
Authors: Li, MH
Kwok, F
Chang, WR
Liu, SQ
Lo, SCL 
Zhang, JP
Jiang, T
Liang, DC
Issue Date: 2004
Source: Journal of biological chemistry, 2004, v. 279, no. 17, p. 17459-17465 How to cite?
Journal: Journal of Biological Chemistry 
Abstract: To understand the processes involved in the catalytic mechanism of pyridoxal kinase (PLK), we determined the crystal structures of PLK-AMP-PCP-pyridoxamine, PLK-ADP-PLP, and PLK-ADP 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 PLK-ATP complex. The distance between the reacting groups of the two substrates is 5.8 Å apart, indicating that the position of ATP is not favorable to spontaneous transfer of its phosphate group. However, the structure of PLK-ADP-PLP complex exhibited significant changes in both the conformation of the enzyme and the location of the ligands at the active site. Therefore, it appears that after binding of both substrates, the enzyme-substrate complex requires changes in the protein structure to enable the transfer of the phosphate group from ATP to vitamin B6. Furthermore, a conformation of the enzyme-substrate complex before the transition state of the enzymatic reaction was also hypothesized.
URI: http://hdl.handle.net/10397/33713
ISSN: 0021-9258
DOI: 10.1074/jbc.M312380200
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