Structure Modeling of Azoreductase AZR and Site-directed Mutagenesis of Its K~(109) Residue / 微生物学通报
Microbiology
; (12)1992.
Article
en Zh
| WPRIM
| ID: wpr-685881
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WPRO
ABSTRACT
Three-dimensional structure model of azoreductase AZR of Rhodobacter sphaeroides was con- structed using homology modeling method. It is a flavodoxin adopting ?/? structure. Structure alignment of two different types of flavin-dependent azoreductases revealed that they possessed high similarity. Based on sequence and structure analysis, site-directed mutagenesis of K109H and K109A were performed. The opti- mal pH values are pH 6 and pH 9 for K109H and K109A mutant protein, respectively. The optimal tempera- ture (30℃) is not affected by mutagenesis. Positively charged residues at position 109 is necessary for the binding of methyl red, while K109H is not a conserved mutagenesis for the binding of NADPH. K109 may only be involved in the binding of the 2’-phosphate group of NADPH and have no effect on the binding of NADH.
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WPRIM
Idioma:
Zh
Revista:
Microbiology
Año:
1992
Tipo del documento:
Article