A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: Molecular cloning and characterization

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Title
A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: Molecular cloning and characterization
Author(s)
S I Ryu; C S Park; J Cha; Eui-Jeon Woo; S B Lee
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 329, no. 2, pp. 429-436
Publication Year
2005
Abstract
A gene (ORF PH1035), annotated to encode an uncharacterized hypothetical protein in Pyrococcus horikoshii, was first cloned and expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity by Ni-NTA affinity chromatography and its molecular mass was determined to be 49,871 Da by MALDI-TOF mass spectrometry. When the purified enzyme was reacted with nucleoside diphosphate-glucoses including UDP-glucose as a donor and glucose, rather than glucose-6-phosphate, as an acceptor, it specifically created a free trehalose. The enzyme was also able to partly hydrolyze the trehalose to glucose. The optimum pH was 5.5 and the enzyme was highly stable from pH 6 to 8. The deduced amino acid sequence showed a high homology with that of the glycosyl transferase group 1 (Pfam00534) in the BLAST search. The results suggest that the enzyme is a novel glycosyltransferase catalyzing the synthesis of the trehalose in the archaeon.
Keyword
GlycosyltransferaseNucleoside diphosphate-glucosePyrococcus horikoshiiTrehaloseTrehalose synthase
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2005.01.149
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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