Conferral of allostery to Thermus sp. GH5 methylglyoxal synthase by a single mutation
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/152/6/531/2371009/mvs115.pdf
Reference21 articles.
1. Allostery: an illustrated definition for the ‘second secret of life’
2. Active-site mutants altering the cooperativity of E. coliphosphofructokinase
3. Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase
4. Triggering of Allostery in an Enzyme by a Point Mutation: Ornithine Transcarbamoylase
5. Conversion of the noncooperative Bacillus subtilis aspartate transcarbamoylase into a cooperative enzyme by a single amino acid substitution
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1. Deciphering Evolutionary Trajectories of Lactate Dehydrogenases Provides New Insights into Allostery;Molecular Biology and Evolution;2023-10
2. Protein Conformational Space at the Edge of Allostery: Turning a Nonallosteric Malate Dehydrogenase into an “Allosterized” Enzyme Using Evolution-Guided Punctual Mutations;Molecular Biology and Evolution;2022-09-01
3. An alternative allosteric pathway in thermophilic methylglyoxal synthase;International Journal of Biological Macromolecules;2016-12
4. Conversion of non-allosteric methylglyoxal synthase into a homotropic allosteric enzyme by C-terminal deletion;Journal of Molecular Catalysis B: Enzymatic;2014-09
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