Conserved residues of liquefying alpha-amylases are concentrated in the vicinity of active site |
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Authors: | M Vihinen P M?nts?l? |
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Institution: | Department of Biochemistry, University of Turku, Finland. |
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Abstract: | Three dimensional structure of three liquefying type Bacillus alpha-amylases were modeled based on sequence analyses and refined structure of Aspergillus oryzae enzyme. The models suggest that the overall folding motif of alpha-amylases is conserved. The active site, substrate binding and stabilizing calcium binding residues are conserved and concentrated in a cleft between two domains. They constitute the core of alpha-amylases to which other, less conserved regions are attached. The bacterial enzymes have a loop of about 45 residues near the active site and Ca2+ binding region. The loop may be important for the liquefying function of these enzymes. |
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