The Molecular Mechanism of Thermostable α-Galactosidases AgaA and AgaB Explained by X-ray Crystallography and Mutational Studies

The α-galactosidase AgaA from the thermophilic microorganism Geobacillus stearothermophilus has great industrial potential because it is fully active at 338 K against raffinose and can increase the yield of manufactured sucrose. AgaB has lower affinity for its natural substrates but is a powerful to...

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Bibliographic Details
Main Authors: Merceron, Romain, Foucault, Marine, Haser, Richard, Mattes, Ralf, Watzlawick, Hildegard, Gouet, Patrice
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2012
Subjects:
Protein Structure and Folding
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC3501081/
https://ncbi.nlm.nih.gov/pubmed/23012371
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M112.394114
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