Literature DB >> 23001647

Homologous Alkalophilic and Acidophilic L-Arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability.

Sang-Jae Lee1, Sang Jun Lee, Yong-Jik Lee, Seong-Bo Kim, Sung-Kun Kim, Dong-Woo Lee.   

Abstract

To study the pH dependence of l-arabinose isomerase (AI) activity and stability, we compared homologous AIs with their chimeras. This study demonstrated that an ionizable amino acid near the catalytic site determines the optimal pH (pH(opt)) for activity, whereas the N-terminal surface R residues play an important role in determining the pH(opt) for stability.

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Year:  2012        PMID: 23001647      PMCID: PMC3502938          DOI: 10.1128/AEM.02114-12

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  31 in total

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4.  Stereochemical evidence for a cis-enediol intermediate in Mn-dependent aldose isomerases.

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9.  pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme.

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  3 in total

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2.  The secreted L-arabinose isomerase displays anti-hyperglycemic effects in mice.

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