Chloroplast pentose-5-phosphate 3-epimerase from potato: cloning, cDNA sequence, and tissue-specific enzyme accumulation

A cDNA clone encoding the chloroplast enzyme pentose-5-phosphate 3-epimerase (EC 5.1.3.1) in potato ( Solanum tuberosum) was isolated and sequenced. The deduced sequence of 235 amino acids is similar to protein sequences of bacterial epimerases. Northern blot analysis showed the highest level of epi...

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Bibliographic Details
Published in:FEBS letters 1995-12, Vol.377 (3), p.349-352
Main Authors: Teige, Markus, Kopriva, Stanislav, Bauwe, Hermann, Süss, Karl-Heinz
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Blotting, Northern
Blotting, Western
Carbohydrate Epimerases - chemistry
Carbohydrate Epimerases - genetics
cDNA sequence
Chloroplast
Chloroplasts - enzymology
DNA, Complementary - genetics
Gene Library
Molecular Sequence Data
Pentose-5-phosphate 3-epimerase
Plant Leaves - enzymology
Sequence Analysis
Sequence Homology, Amino Acid
Solanum tuberosum
Solanum tuberosum - enzymology
Solanum tuberosum - genetics
Tissue Distribution
Tissue-specific enzyme accumulation
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Summary:A cDNA clone encoding the chloroplast enzyme pentose-5-phosphate 3-epimerase (EC 5.1.3.1) in potato ( Solanum tuberosum) was isolated and sequenced. The deduced sequence of 235 amino acids is similar to protein sequences of bacterial epimerases. Northern blot analysis showed the highest level of epimerase mRNA expression in potato leaves, whereas it was low in roots, tubers, and stems. Epimerase protein is mulated only in plant tissues possessing chloroplasts, i.e. in land to a lesser extent in stem. In contrast, transketolase, a sequential enzyme of epimerase in the reductive and oxidative pentose phosphate cycle, is accumulated in all plant tissues.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)01373-3