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A temperature-sensitive Mycobacterium smegmatis glgE mutation leads to a loss of GlgE enzyme activity and thermostability and the accumulation of α-maltose-1-phosphate
Karl Syson, Sibyl F. D. Batey, Steffen Schindler, Rainer Kalscheuer, View ORCID ProfileStephen Bornemann
doi: https://doi.org/10.1101/2020.04.23.057067
Karl Syson
aBiological Chemistry Department, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom
Sibyl F. D. Batey
aBiological Chemistry Department, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom
Steffen Schindler
bInstitute of Pharmaceutical Biology and Biotechnology, Heinrich Heine University, 40225 Düsseldorf, Germany
Rainer Kalscheuer
bInstitute of Pharmaceutical Biology and Biotechnology, Heinrich Heine University, 40225 Düsseldorf, Germany
Stephen Bornemann
aBiological Chemistry Department, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom
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Posted October 22, 2020.
A temperature-sensitive Mycobacterium smegmatis glgE mutation leads to a loss of GlgE enzyme activity and thermostability and the accumulation of α-maltose-1-phosphate
Karl Syson, Sibyl F. D. Batey, Steffen Schindler, Rainer Kalscheuer, Stephen Bornemann
bioRxiv 2020.04.23.057067; doi: https://doi.org/10.1101/2020.04.23.057067
A temperature-sensitive Mycobacterium smegmatis glgE mutation leads to a loss of GlgE enzyme activity and thermostability and the accumulation of α-maltose-1-phosphate
Karl Syson, Sibyl F. D. Batey, Steffen Schindler, Rainer Kalscheuer, Stephen Bornemann
bioRxiv 2020.04.23.057067; doi: https://doi.org/10.1101/2020.04.23.057067
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