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J Biosci Bioeng. 2013 Apr;115(4):377-81. doi: 10.1016/j.jbiosc.2012.10.021. Epub 2012 Dec 1.

Cloning and characterization of the l-ribose isomerase gene from Cellulomonas parahominis MB426.

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  • 1Rare Sugar Research Center, Kagawa University, Miki-cho, Kagawa, Japan.

Abstract

A newly isolated bacterium, Cellulomonas parahominis MB426, produced l-ribose isomerase (CeLRI) on a medium containing l-ribose as a sole carbon source. A 32 kDa protein isomerizing l-ribose to l-ribulose was purified to homogeneity from this bacterium. A set of degenerated primers were synthesized based on amino acid sequences of the purified CeLRI, and a 747 bp gene encoding CeLRI was cloned, sequenced and overexpressed in Escherichia coli. This gene encoded a 249 amino acid protein with a calculated molecular mass of 27,435. The deduced amino acid sequence of this gene showed the highest identity with l-ribose isomerase from Acinetobacter calcoaceticus DL-28 (71%). The recombinant l-ribose isomerase (rCeLRI) was optimally active at pH 9.0 and 40°C, and was stable up to 40°C for 1 h and not dependent for metallic ions for its activity. The rCeLRI showed widely substrate specificity for the rare sugar which involved l-erythro form such as l-ribose, d-lyxose, d-talose, d-mannose, l-gulose, and l-allose.

Copyright © 2012 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.

PMID:
23207370
[PubMed - indexed for MEDLINE]

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