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Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.

Changes in subunit interaction energies linked to the allosteric transition of the regulatory enzyme aspartate transcarbamoylase (ATCase; EC 2.1.3.2) from Escherichia coli are localized in part at interfaces between the six catalytic (c) and six regulatory (r) polypeptide chains. Site-directed mutag...

詳細記述

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書誌詳細
出版年:Proc Natl Acad Sci U S A
主要な著者: Eisenstein, E, Markby, D W, Schachman, H K
フォーマット: Artigo
言語:Inglês
出版事項: National Academy of Sciences 1989
主題:
オンライン・アクセス:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC287071/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2566165/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.86.9.3094
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