Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/17651
Title: Crystal structure of brain pyridoxal kinase, a novel member of the ribokinase superfamily
Authors: Li, MH
Kwok, F
Chang, WR
Lau, CK
Zhang, JP
Lo, SCL 
Jiang, T
Liang, DC
Issue Date: 2002
Publisher: Amer Soc Biochemistry Molecular Biology Inc
Source: Journal of biological chemistry, 2002, v. 277, no. 48, p. 46385-46390 How to cite?
Journal: Journal of Biological Chemistry 
Abstract: The three-dimensional structures of brain pyridoxal kinase and its complex with the nucleotide ATP have been elucidated in the dimeric form at 2.1 and 2.6 Å, respectively. Results have shown that pyridoxal kinase, as an enzyme obeying random sequential kinetics in catalysis, does not possess a lid shape structure common to all kinases in the ribokinase superfamily. This finding has been shown to be in line with the condition that pyridoxal kinase binds substrates with variable sizes of chemical groups at position 4 of vitamin B6 and its derivatives. In addition, the enzyme contains a 12-residue peptide loop in the active site for the prevention of premature hydrolysis of ATP. Conserved amino acid residues Asp118 and Tyr127 in the peptide loop could be moved to a position covering the nucleotide after its binding so that its chance to hydrolyze in the aqueous environment of the active site was reduced. With respect to the evolutionary trend of kinase enzymes, the existence of this loop in pyridoxal kinase could be classified as an independent category in the ribokinase superfamily according to the structural feature found and mechanism followed in catalysis.
URI: http://hdl.handle.net/10397/17651
ISSN: 0021-9258
DOI: 10.1074/jbc.M208600200
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