상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Mutational analysis of the active site residues of a d-psicose 3-epimerase from Agrobacterium tumefaciens

Authors 

H J KimS J YeomK KimS RheeDoo Il KimD K Oh

Publisher 

Springer Verlag (Germany)

Issue Date 

2010

Citation 

Biotechnology Letters, vol. 32, no. 2, pp. 261-268

Keywords 

Active siteAgrobacterium tumefaciensCircular dichroismd-Psicose 3-epimeraseSite directed mutagenesis

Abstract 

d-Psicose 3-epimerase from Agrobacterium tumefacience catalyzes the conversion of d-fructose to d-psicose. According to mutational analysis, the ring at position 112, the negative charge at position 156, and the positive charge at position 215 were essential components for enzyme activity and for binding fructose and psicose. The surface contact area and distance to the bound substrate by molecular modeling suggest that the positive charge of Arg215 was involved in stabilization of cis-endiol intermediate. The distances between the catalytic residues (Glu150 and Glu244) and Mn2+ are critical to the catalysis, and the negative charges of the metal-binding residues are important for interaction with metal ion. The kinetic parameters of the D183E and H209A mutants for metal-binding residues with substrate and the near-UV circular dichroism spectra indicate that the metal ion bound to Asp183 and His209 is involved not only in catalysis but also in substrate binding.

ISSN 

0141-5492

Link 

http://dx.doi.org/10.1007/s10529-009-0148-5

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)