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Title 

A hexokinase with broad sugar specificity from a thermophilic bacterium

Authors 

Jungdon BaeDooil KimYongseok ChoiSukhoon KohJung Eun ParkJoong Su KimSeong Hoon MoonBo-Hyun ParkMi Ri ParkHye-Eun SongSuk-In HongDae Sil Lee

Publisher 

Elsevier

Issue Date 

2005

Citation 

Biochemical and Biophysical Research Communications, vol. 334, no. 3, pp. 754-763

Keywords 

glycolysishexokinasemolecular modelingROKsubstrate specificitythermusadenosine triphosphatealloseglucosamine

Abstract 

A recombinant thermophilic Thermus caldophilus GK24 hexokinase, one of the ROK-type (repressor protein, open reading frames, and sugar kinase) proteins, exists uniquely as a 120 kDa molecule with four subunits (31 kDa), in contrast to eukaryotic and bacterial sugar kinases which are monomers or dimers. The optimal temperature and pH for the enzyme reaction are 70-80°C and 7.5, respectively. This enzyme shows broad specificity toward glucose, mannose, glucosamine, allose, 2-deoxyglucose, and fructose. To understand the sugar specificity at a structural level, the enzyme-ATP/Mg2+-sugar binding complex models have been constructed. It has been shown that the sugar specificity is probably dependent on the interaction energy occurred by the positional proximity of sugars bound in the active site of the enzyme, which exhibits a tolerance to modification at C2 or C3 of glucose.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2005.06.160

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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