Roles of Ile66 and Ala107 of d-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its substrate, d-fructose

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Title
Roles of Ile66 and Ala107 of d-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its substrate, d-fructose
Author(s)
H J Kim; B C Lim; Soo Jin Yeom; Y S Kim; Doo Il Kim; D K Oh
Bibliographic Citation
Biotechnology Letters, vol. 32, no. 1, pp. 113-118
Publication Year
2010
Abstract
Using site-directed mutagenesis, we investigated the roles of Ile66 and Ala107 of d-psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its true substrate, D-fructose. When Ile66 was substituted with alanine, glycine, cysteine, leucine, phenylalanine, tryptophan, tyrosine or valine, all the mutants dramatically increased the Km for d-tagatose but slightly decreased the Km for d-fructose, indicating that Ile66 is involved in substrate recognition. When Ala107 was substituted by either isoleucine or valine, the substituted mutants had lower thermostability than the wild-type enzyme whereas the proline-substituted mutant had higher thermostability. Thus, Ala107 is involved in enzyme stability.
Keyword
Substrate specificityAgrobacterium tumefaciensD-Psicose 3-epimeraseProtein stabilitySite-directed mutagenesis
ISSN
0141-5492
Publisher
Springer
DOI
http://dx.doi.org/10.1007/s10529-009-0115-1
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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