Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase.

A comparison of the three-dimensional structures of the closely related mesophilic Clostridium beijerinckii alcohol dehydrogenase (CBADH) and the hyperthermophilic Thermoanaerobacter brockii alcohol dehydrogenase (TBADH) suggested that extra proline residues in TBADH located in strategically importa...

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Autores principales: Bogin, O., Peretz, M., Hacham, Y., Korkhin, Y., Frolow, F., Kalb(Gilboa), A. J., Burstein, Y.
Formato: Artigo
Lenguaje:Inglês
Publicado: Cold Spring Harbor Laboratory Press 1998
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Research Article
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144005/
https://ncbi.nlm.nih.gov/pubmed/9836874
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