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  • Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus.

Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus.

The Journal of biological chemistry (2012-01-10)
Tae-Yang Jung, Dan Li, Jong-Tae Park, Se-Mi Yoon, Phuong Lan Tran, Byung-Ha Oh, Štefan Janeček, Sung Goo Park, Eui-Jeon Woo, Kwan-Hwa Park
ABSTRACT

Staphylothermus marinus maltogenic amylase (SMMA) is a novel extreme thermophile maltogenic amylase with an optimal temperature of 100 °C, which hydrolyzes α-(1-4)-glycosyl linkages in cyclodextrins and in linear malto-oligosaccharides. This enzyme has a long N-terminal extension that is conserved among archaic hyperthermophilic amylases but is not found in other hydrolyzing enzymes from the glycoside hydrolase 13 family. The SMMA crystal structure revealed that the N-terminal extension forms an N' domain that is similar to carbohydrate-binding module 48, with the strand-loop-strand region forming a part of the substrate binding pocket with several aromatic residues, including Phe-95, Phe-96, and Tyr-99. A structural comparison with conventional cyclodextrin-hydrolyzing enzymes revealed a striking resemblance between the SMMA N' domain position and the dimeric N domain position in bacterial enzymes. This result suggests that extremophilic archaea that live at high temperatures may have adopted a novel domain arrangement that combines all of the substrate binding components within a monomeric subunit. The SMMA structure provides a molecular basis for the functional properties that are unique to hyperthermophile maltogenic amylases from archaea and that distinguish SMMA from moderate thermophilic or mesophilic bacterial enzymes.

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Sigma-Aldrich
Amylase, Maltogenic from Bacillus sp.