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A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization.
Biochem Biophys Res Commun 2005; 329(2):429-36BB

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 49,871Da 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.

Authors+Show Affiliations

Research Institute of Food and Nutritional Sciences, Department of Food and Nutrition, Yonsei University, Seoul 120-749, Republic of Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15737605

Citation

Ryu, Soo-In, et al. "A Novel Trehalose-synthesizing Glycosyltransferase From Pyrococcus Horikoshii: Molecular Cloning and Characterization." Biochemical and Biophysical Research Communications, vol. 329, no. 2, 2005, pp. 429-36.
Ryu SI, Park CS, Cha J, et al. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem Biophys Res Commun. 2005;329(2):429-36.
Ryu, S. I., Park, C. S., Cha, J., Woo, E. J., & Lee, S. B. (2005). A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochemical and Biophysical Research Communications, 329(2), pp. 429-36.
Ryu SI, et al. A Novel Trehalose-synthesizing Glycosyltransferase From Pyrococcus Horikoshii: Molecular Cloning and Characterization. Biochem Biophys Res Commun. 2005 Apr 8;329(2):429-36. PubMed PMID: 15737605.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. AU - Ryu,Soo-In, AU - Park,Cheon-Seok, AU - Cha,Jaeho, AU - Woo,Eui-Jeon, AU - Lee,Soo-Bok, PY - 2005/01/20/received PY - 2005/3/2/pubmed PY - 2005/5/6/medline PY - 2005/3/2/entrez SP - 429 EP - 36 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 329 IS - 2 N2 - 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 49,871Da 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. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/15737605/A_novel_trehalose_synthesizing_glycosyltransferase_from_Pyrococcus_horikoshii:_molecular_cloning_and_characterization_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(05)00196-8 DB - PRIME DP - Unbound Medicine ER -