UDP-glucose-4-epimerase from Poterioochromonas malhamensis |
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Authors: | Klaus-Sten Thomson Christine Jung Heinrich Kauss |
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Institution: | Fachbereich Biologie, Universität Kaiserslautern, Postfach 3049, 6750 Kaiserslautern, Federal Republic of Germany |
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Abstract: | UDP-glucose-4-epimerase of Poterioochromonas malhamensis, Peterfi has been purified to apparent electrophoretic homogeneity. The enzyme has an apparent MW of 120 000 as determined by gel filtration of the active enzyme. Sodium dodecylsulfate polyacrylamide gel electrophoresis gave a MW of 59 000, thus indicating a dimeric structure. The epimerase does not require external NAD for activity. The apparent Km values for UDP-glucose and UDP-galactose were calculated to be 1.67 mM and 0.26 mM, respectively. The pH optimum is at pH 8.7 and the isoelectric point is at pH 5.1 ± 0.15. |
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Keywords: | Chrysophyceae UDP-glucose-4-epimerase |
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