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Lysine 144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase
Author(s) -
Miosga Thomas,
SchaaffGerstenschläger Ine,
Franken Eva,
Zimmermann Friedrich K.
Publication year - 1993
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320091111
Subject(s) - transaldolase , biology , saccharomyces cerevisiae , biochemistry , pentose phosphate pathway , histidine , enzyme , cysteine , pentose , lysine , amino acid , yeast , fermentation , glycolysis
Replacement of lysine 144 by glutamine in the pentose phosphate pathway enzyme transaldolase of Saccharomyces cerevisiae is associated with the complete loss of activity indicating the essential role in catalysis. Neither histidine nor cysteine is important for catalytic activity as proposed for the Candida utilis enzyme. Also we could not find any evidence for a half‐site character of the enzyme as described for transaldolase of C. utilis . Therefore, the reaction mechanisms for the two enzymes are different.