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J. Biochem, 2003, Vol. 134, No. 5 731-738
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Interaction between Pyridoxal Kinase and Pyridoxal-5-phosphate–Dependent Enzymes

Pik-Yuen Cheung1, Chi-Chun Fong2, Kang-To Ng1, Wan-Chuen Lam1, Yun-Chung Leung1, Chun-Wai Tsang1, Mengsu Yang*,2 and Man-Sau Wong§,1

1 The Central Laboratory of the Institute of Molecular Technology for Drug Discovery and Synthesis, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong SAR, P.R.C.; and 2 Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenu, Kowloon, Hong Kong SAR, P.R.C.

The interactions of two pyridoxal-5-phosphate (PLP)–dependent enzymes, alanine aminotransferase (ALT) and glutamate decarboxylase (GAD), with pyridoxal kinase (PK) were studied by fluorescence polarization as well as surface plasmon resonance techniques. The results demonstrated that PK can specifically bind to ALT and GAD. Moreover, binding profiles of both enzymes to immobilized PK were altered by excess amount of PLP. The equilibrium affinity constants for ALT in the absence and presence of PLP are 20.4 x 104 M–1and 6.7 x 104 M–1, and for GAD are 37 x 104 M–1and 20.8 x 104 M–1, respectively. It appears that specific interactions occur between PK and PLP-dependent enzymes, and the binding affinities of PK for PLP-dependent enzymes decrease in the presence of PLP. The results support our hypothesis that PLP transfer from PK to PLP-dependent enzymes requires a specific interaction between PK and the enzyme.

* To whom correspondence should be addressed. Fax: +852-2788-7406, E-mail: bhmyang{at}cityu.edu.hk

§ To whom correspondence should be addressed. Tel: +852-27666695, Fax: +852-23649932, E-mail: bcmswong{at}polyu.edu.hk


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