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Chloroplast pentose‐5‐phosphate 3‐epimerase from potato: cloning, cDNA sequence, and tissue‐specific enzyme accumulation
Author(s) -
Markus Teige,
Stanislav Kopriva,
Hermann Bauwe,
KarlHeinz Süss
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01373-3
Subject(s) - transketolase , pentose , pentose phosphate pathway , biochemistry , chloroplast , biology , complementary dna , enzyme , transaldolase , microbiology and biotechnology , gene , glycolysis , fermentation
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.