NDLI: Properties of trehalose-6-phosphate synthase fromSaccharomycopsis fibuligera

Content Provider	Springer Nature Link
Author	Liang, Likun Chi, Zhenming Wang, Xiaoke Zhu, Kailing
Copyright Year	2006
Abstract	In this paper, we investigated the properties of trehalose-6- phosphate synthase (SfTps1) inSaccharomycopsis fibuligera sdu a high-trehalose-accumulating strain. The purified SfTps1 showed a band on Native-PAGE and SDS-PAGE of about 66 kDa. The optimal pH and temperature of the purified enzyme were 6.6 and 37 °C, respectively. The enzyme was activated by Ca$^{2+}$, K$^{+}$ and Mg$^{2+}$, inhibited by Mn$^{2+}$, Cu$^{2+}$, Fe$^{3+}$, Hg$^{2+}$ and Co$^{2+}$. Iodoacetic acid, EDTA and PMSF had inhibitory effect on the enzyme activity. K$_{m}$ values of the enzyme for glucose-6-phosphate and UDP-glucose were 38.6 mM and 9.3 mM, respectively. The effects of various stress conditions on SfTps1 activity and trehalose content in this strain were also studied. Neither the activation of SfTps1 nor the change in trehalose content was observed under stress exposure ofSaccharomycopsis fibuligera cells. Our results indicate that the SfTps1 protein and trehalose metabolism in response to stress conditions inSaccharomycopsis fibuligera clearly differ from that ofSaccharomyces cerevisiae and most of other eukaryotes.
Starting Page	241
Ending Page	245
Page Count	5
File Format	PDF
ISSN	15904261
Journal	Annals of Microbiology
Volume Number	56
Issue Number	3
e-ISSN	18692044
Language	English
Publisher	Springer-Verlag
Publisher Date	2006-01-01
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	properties trehalose-6-phosphate synthase trehalose yeast Microbiology Microbial Genetics and Genomics Microbial Ecology Fungus Genetics Medical Microbiology Applied Microbiology
Content Type	Text
Resource Type	Article
Subject	Applied Microbiology and Biotechnology

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