Lysine 144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase
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...
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Veröffentlicht in: | Yeast (Chichester, England) England), 1993-11, Vol.9 (11), p.1241-1249 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | 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. |
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ISSN: | 0749-503X 1097-0061 |
DOI: | 10.1002/yea.320091111 |