作者: Pik-Yuen Cheung , Chi-Chun Fong , Kang-To Ng , Wan-Chuen Lam , Yun-Chung Leung
DOI: 10.1093/JB/MVG201
关键词: Surface plasmon resonance 、 Binding affinities 、 Pyridoxal kinase 、 Enzyme 、 Pyridoxal 5-Phosphate 、 Biochemistry 、 Glutamate decarboxylase 、 Fluorescence anisotropy 、 Stereochemistry 、 Alanine aminotransferase 、 Chemistry
摘要: 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 surface plasmon resonance techniques. results demonstrated that PK can specifically bind to ALT GAD. Moreover, binding profiles both enzymes immobilized altered excess amount PLP. equilibrium affinity constants for in the absence presence PLP are 20.4 x 10 4 M - 1 6.7 , GAD 37 20.8 respectively. It appears specific occur between PLP-dependent affinities decrease support our hypothesis transfer from requires a interaction enzyme.