Találati lista | Tudóstér

001-es BibID:	BIBFORM040692
Első szerző:	Tőzsér József (molekuláris biológus, biokémikus, vegyész)
Cím:	Comparison of the substrate specificity of two potyvirus proteases / Tözsér József, Tropea Joseph E., Cherry Scott, Bagossi Peter, Copeland Terry D., Wlodawer Alexander, Waugh David S.
Dátum:	2005
ISSN:	1742-464X
Megjegyzések:	The substrate specificity of the nuclear inclusion protein a (NIa) proteolytic enzymes from two potyviruses, the tobacco etch virus (TEV) and tobacco vein mottling virus (TVMV), was compared using oligopeptide substrates. Mutations were introduced into TEV protease in an effort to identify key determinants of substrate specificity. The specificity of the mutant enzymes was assessed by using peptides with complementary substitutions. The crystal structure of TEV protease and a homology model of TVMV protease were used to interpret the kinetic data. A comparison of the two structures and the experimental data suggested that the differences in the specificity of the two enzymes may be mainly due to the variation in their S4 and S3 binding subsites. Two key residues predicted to be important for these differences were replaced in TEV protease with the corresponding residues of TVMV protease. Kinetic analyses of the mutants confirmed that these residues play a role in the specificity of the two enzymes. Additional residues in the substrate-binding subsites of TEV protease were also mutated in an effort to alter the specificity of the enzyme.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Febs Journal. - 272 : 2 (2005), p. 514-523. -
További szerzők:	Tropea, Joseph E. Cherry, Scott Bagossi Péter (1966-2011) (biokémikus, vegyész) Copeland, Terry D. Wlodawer, Alexander Waugh, David S.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: