Investigation of the mechanism of catalitical action and active sitestructure of glutamin(asparagin)ase by methods of computer analysis. I. Pharmacophore models of glutamine(asparagine) ase substrates
Veselovsky A.V., Lebedeva Z. I., Ivanov A.S., Berezov T.T.
Glutamine(asparagine)ase catalyses desamidation of both L-glutamine and L-asparagine, and their D-isomers. In this study the two-pharmacophore models of main enzyme substrates and their hydrolysed analogues were design. The received models reflect two stage of substrate interaction with the enzyme active site. These models allow to explain the wide substrate specificity of glutamine(asparagine)ase.
Download PDF:
Keywords: amidohydrolase, glutamine(asparagine)ase, substrates, computer modelling, pharmacophore model
Citation:
Veselovsky A.V., Lebedeva Z. I., Ivanov A.S., Berezov T.T. (1999) Investigation of the mechanism of catalitical action and active sitestructure of glutamin(asparagin)ase by methods of computer analysis. I. Pharmacophore models of glutamine(asparagine) ase substrates. Voprosy Meditsinskoi Khimii, 45(2), 178-184.
Veselovsky A.V. et al. Investigation of the mechanism of catalitical action and active sitestructure of glutamin(asparagin)ase by methods of computer analysis. I. Pharmacophore models of glutamine(asparagine) ase substrates // Voprosy Meditsinskoi Khimii. - 1999. - V. 45. -N 2. - P. 178-184.
Veselovsky A.V. et al., "Investigation of the mechanism of catalitical action and active sitestructure of glutamin(asparagin)ase by methods of computer analysis. I. Pharmacophore models of glutamine(asparagine) ase substrates." Voprosy Meditsinskoi Khimii 45.2 (1999): 178-184.
Veselovsky, A. V., Lebedeva, Z. , I., Ivanov, A. S., Berezov, T. T. (1999). Investigation of the mechanism of catalitical action and active sitestructure of glutamin(asparagin)ase by methods of computer analysis. I. Pharmacophore models of glutamine(asparagine) ase substrates. Voprosy Meditsinskoi Khimii, 45(2), 178-184.
References
Лебедева З.И., Берегов Т. Т. (1995) Усп. биол. химии, 35, 161 -187. Scholar google search