Interaction between pyridoxal kinase and pyridoxal-5-phosphate-dependent enzymes.

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Cheung PY, Fong CC, Ng KT, Lam WC, Leung YC, Tsang CW, Yang M, Wong MS

Interaction between pyridoxal kinase and pyridoxal-5-phosphate-dependent enzymes.

J Biochem. 2003 Nov;134(5):731-8.

PubMed ID

14688239 [ View in PubMed

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Abstract

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 10(4) M(-1)and 6.7 x 10(4) M(-1), and for GAD are 37 x 10(4) M(-1)and 20.8 x 10(4) 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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Pyridoxal phosphate	Alanine aminotransferase 1	Protein	Humans	Unknown	Cofactor	Details