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Acta Biochimica et Biophysica Sinica 2009 41(2):116-122; doi:10.1093/abbs/gmn013
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© The Author 2009. Published by ABBS Editorial Office in association with Oxford University Press on behalf of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences.

Identification, expression, and characterization of the highly conserved D-xylose isomerase in animals

Ming Ding1, Yigang Teng1, Qiuyu Yin1, Wei Chen2 and Fukun Zhao1,2,*

1 Key Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 20031, China
2 College of Life Science, Zhejiang Sci-Tech University, Hangzhou 310018, China

* Correspondence address. Tel: +86-21-54921155; Fax: +86-21-54921011; E-mail: fkzhao{at}sibs.ac.cn


  Abstract

D-xylose is a necessary sugar for animals. The xylanase from a mollusk, Ampullaria crossean, was previously reported by our laboratory. This xylanase can degrade the xylan into D-xylose. But there is still a gap in our knowledge on its metabolic pathway. The question is how does the xylose enter the pentose pathway? With the help of genomic databases and bioinformatic tools, we found that some animals, such as bacteria, have a highly conserved D-xylose isomerase (EC 5.3.1.5 [EC] ). The xylose isomerase from a sea squirt, Ciona intestinalis, was heterogeneously expressed in Escherichia coli and purified to confirm its function. The recombinant enzyme had good thermal stability in the presence of Mg2+. At the optimum temperature and optimum pH environment, its specific activity on D-xylose was 0.331 µmol/mg/min. This enzyme exists broadly in many animals, but it disappeared in the genome of Amphibia-like Xenopus laevis. Its sequence was highly conserved. The xylose isomerases from animals are very interesting proteins for the study of evolution.

Keywords    xylose isomerase; xylanase; animals; D-xylose; Ciona intestinalis; heterogeneous expression

Received: October 12, 2008; Accepted: December 25, 2008
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