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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

Authors 

H J KimB C LimS J YeomY S KimDoo Il KimD K Oh

Publisher 

Springer Verlag (Germany)

Issue Date 

2010

Citation 

Biotechnology Letters, vol. 32, no. 1, pp. 113-118

Keywords 

Agrobacterium tumefaciensD-Psicose 3-epimeraseProtein stabilitySite-directed mutagenesisSubstrate specificity

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.

ISSN 

0141-5492

Link 

http://dx.doi.org/10.1007/s10529-009-0115-1

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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