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Lu2021-Genome scale metabolic model for yeast species of clade CUG-Ala


ABSTRACT: This is genome-scale metabolic model of Pachysolen tannophilus as the representative yeast species for the clade CUG-Ala. 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 MODEL2109130004. 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: Nakazawaea peltata; Pachysolen tannophilus; Peterozyma xylosa; Peterozyma toletana; Nakazawaea holstii. 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: MODEL2109130004 | BioModels | 2021-11-01

REPOSITORIES: BioModels

Dataset's files

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MODEL2109130004?filename=CUG-Ala.zip Other
MODEL2109130004?filename=Pachysolen_tannophilus.xml Xml
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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: 1/358

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