Characterization of aspartate transcarbamoylase in the archaebacterium Methanococcus jannaschii

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The ATCase characterized in this study is from the extreme thermophilinc Archaebacterium, Methanococcus jannaschii. The enzyme was very stable at elevated temperatures and possessed activity from 20ºC to 90ºC. M. jannaschii ATCase retained 75 percent of its activity after incubation at 100ºC for a period of 90 minutes.

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Stewart, John E. B. (John Edward Bakos) December 1996.

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The ATCase characterized in this study is from the extreme thermophilinc Archaebacterium, Methanococcus jannaschii. The enzyme was very stable at elevated temperatures and possessed activity from 20ºC to 90ºC. M. jannaschii ATCase retained 75 percent of its activity after incubation at 100ºC for a period of 90 minutes.

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  • December 1996

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  • Nov. 15, 2016, 10:54 a.m.

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  • July 14, 2017, 11:26 a.m.

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Stewart, John E. B. (John Edward Bakos). Characterization of aspartate transcarbamoylase in the archaebacterium Methanococcus jannaschii, thesis or dissertation, December 1996; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc935724/: accessed August 21, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .