Mutational analysis of Asp51 of Anabaena azollae glutamine synthetase. D51E mutation confers resistance to the active site inhibitors L-methionine-DL-sulfoximine and phosphinothricin

Citation
Jl. Crespo et al., Mutational analysis of Asp51 of Anabaena azollae glutamine synthetase. D51E mutation confers resistance to the active site inhibitors L-methionine-DL-sulfoximine and phosphinothricin, EUR J BIOCH, 266(3), 1999, pp. 1202-1209
Citations number
48
Categorie Soggetti
Biochemistry & Biophysics
Journal title
EUROPEAN JOURNAL OF BIOCHEMISTRY
ISSN journal
00142956 → ACNP
Volume
266
Issue
3
Year of publication
1999
Pages
1202 - 1209
Database
ISI
SICI code
0014-2956(199912)266:3<1202:MAOAOA>2.0.ZU;2-V
Abstract
The role of Asp51 in the catalytic activity of glutamine synthetase from th e cyanobacterium Anabaena azollae has been analyzed. Five mutant enzymes. D 51S, D51A, D51E, D51N and D51R, were constructed by site-directed mutagenes is and characterized. Asp51 appears to participate in the binding of ammoni um ion, as affinity for this substrate was affected in all cases, although it varied according to the charge and/or size of the amino-acid residue, de creasing in the order Glu > Asn > Ser > Ala. The replacement of Asp51 by Gl u (D51E) conferred besides a high resistance to the herbicides L-methionine -DL-sulfoximine and phosphinothricin, as a result of a decreased phosphoryl ation ability.