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Lu2021-Genome scale metabolic models for 11 outgroup fungi species


ABSTRACT: This is genome-scale metabolic model of Schizosaccharomyces pombe as the representative species for the clade Ascomycota. This model was generated through homology search using a fungal pan-GEM largely based on Yeast8 for Saccharomyces cerevisiae, in addition to manual curation. This model has been produced by the Yeast-Species-GEMs project from Sysbio (www.sysbio.se). This is model version 1.0.0 accompanying the publication (DOI: 10.15252/msb.202110427), currently hosted on BioModels Database and identified by MODEL2109240001. Further curations of this model will be tracked in the GitHub repository: https://github.com/SysBioChalmers/Yeast-Species-GEMs Models for species of the same clade includes: Arthrobotrys oligospora; Aspergillus nidulans; Botrytis cinerea; Coccidioides immitis; Fusarium graminearum; Neurospora crassa; Saitoella complicata; Schizosaccharomyces pombe; Sclerotinia sclerotiorum; Stagonospora nodorum; Xylona heveae. These models are available in the zip file.. To cite BioModels, please use: V Chelliah et al; BioModels: ten-year anniversary. Nucleic Acids Res 2015; 43 (D1): D542-D548. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to MIT License for more information.

SUBMITTER: feiran  

PROVIDER: MODEL2109240001 | BioModels | 2021-11-01

REPOSITORIES: BioModels

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Publications

Characterization and gene cloning of 1,3-beta-D-glucan synthase from Saccharomyces cerevisiae.

Inoue S B SB   Takewaki N N   Takasuka T T   Mio T T   Adachi M M   Fujii Y Y   Miyamoto C C   Arisawa M M   Furuichi Y Y   Watanabe T T  

European journal of biochemistry 19950801 3


1,3-beta-D-Glucan synthase of Saccharomyces cerevisiae was solubilized and purified up to 700-fold by product entrapment. The specific activity of the partially purified enzyme was around 4 mumol glucose incorporated.min-1.mg protein-1. In SDS/PAGE, enrichment of a 200-kDa protein was clearly observed in parallel with the increase in specific activity. mAbs that could immunoprecipitate the 1,3-beta-D-glucan synthase activity were isolated, and some of them also recognized this 200-kDa protein in  ...[more]

Publication: 1/314

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