Purification and Characterization of UDP-Arabinopyranose Mutase from <i>Chlamydomonas reinhardtii</i>
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- KOTANI Ayana
- Faculty of Agriculture, University of the Ryukyus
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- TSUJI Maki
- Faculty of Agriculture, University of the Ryukyus
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- AZAMA Yasushi
- Faculty of Agriculture, University of the Ryukyus
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- ISHII Tadashi
- Forestry and Forest Products Research Institute
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- TAKEDA Takumi
- Iwate Biotechnology Research Center
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- YAMASHITA Tetsuro
- Faculty of Agriculture, Iwate University
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- SHIMOJIMA Mie
- Tokyo Institute of Technology, Center for Biological Resources and Informatics
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- KONISHI Teruko
- Faculty of Agriculture, University of the Ryukyus
Bibliographic Information
- Other Title
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- Purification and Characterization of UDP-Arabinopyranose Mutase from Chlamydomonas reinhardtii
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Abstract
Chlamydomonas reinhardtii cells are surrounded by a mixture of hydroxyprolin-rich glycoproteins consisting of L-arabinose, D-galactose, D-glucose, and D-mannose residues. The L-arabinose residue is thought to be attached by a transfer of UDP-L-arabinofuranose (UDP-Araf), which is produced from UDP-L-arabinopyranose (UDP-Arap) by UDP-arabinopyranose mutase (UAM). UAM was purified from the cytosol to determine the involvement of C. reinhardtii UAM (CrUAM) in glycoprotein synthesis. CrUAM was purified 94-fold to electrophoretic homogeneity by hydrophobic and size-exclusion chromatography. CrUAM catalyzed the reversible conversion between UDP-Arap and UDP-Araf and exhibited autoglycosylation activity when UDP-D-[14C]glucose was added as substrate. Compared to the properties of native and recombinant CrUAM overexpressed in Escherichia coli, native CrUAM showed a higher affinity for UDP-Arap than recombinant CrUAM did. This increased affinity for UDP-Arap might have been caused by post-translational modifications that occur in eukaryotes but not in prokaryotes.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 77 (9), 1874-1878, 2013
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390282681455362688
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- NII Article ID
- 10031202737
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- NII Book ID
- AA10824164
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- COI
- 1:STN:280:DC%2BC3sbmsFamtw%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 024897582
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- PubMed
- 24018663
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed