Role of Disulfide Bridges in the Activity and Stability of a Cold-Active α-Amylase

The cold-adapted α-amylase from Pseudoalteromonas haloplanktis unfolds reversibly and cooperatively according to a two-state mechanism at 30°C and unfolds reversibly and sequentially with two transitions at temperatures below 12°C. To examine the role of the four disulfide bridges in activity and co...

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Hlavní autoři: Siddiqui, Khawar Sohail, Poljak, Anne, Guilhaus, Michael, Feller, Georges, D'Amico, Salvino, Gerday, Charles, Cavicchioli, Ricardo
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Microbiology 2005
Témata:
Enzymes and Proteins
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1196145/
https://ncbi.nlm.nih.gov/pubmed/16109962
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.187.17.6206-6212.2005
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