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J. Biol. Chem., Vol. 278, Issue 11, 9875-9884, March 14, 2003

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Differential Regulation of a Hyperthermophilic -Amylase with a Novel (Ca,Zn) Two-metal Center by Zinc^*

Anni Linden, Olga Mayans^§, Wolfram Meyer-Klaucke, Garabed Antranikian^¶, and Matthias Wilmanns

From the  European Molecular Biology Laboratory, Notkestrasse 85, D-22603 Hamburg, Germany and the ^¶ Department of Technical Microbiology, Technical University Hamburg-Harburg, Kasernenstrasse 12, D-21073 Hamburg, Germany

The crystal structure of the -amylase from the hyperthermophilic archaeon Pyrococcus woesei was solved in the presence of three inhibitors: acarbose, Tris, and zinc. In the absence of exogenous metals, this -amylase bound 1 and 4 molar eq of zinc and calcium, respectively. The structure reveals a novel, activating, two-metal (Ca,Zn)-binding site and a second inhibitory zinc-binding site that is found in the 1 sugar-binding pocket within the active site. The data resolve the apparent paradox between the zinc requirement for catalytic activity and its strong inhibitory effect when added in molar excess. They provide a rationale as to why this -amylase, in contrast to commercially available -amylases, does not require the addition of metal ions for full catalytic activity, suggesting it as an ideal target to maximize the efficiency of industrial processes like liquefaction of starch.

The atomic coordinates and the structure factors (code 1MWO, 1MXD, and 1MXG) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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