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Title 

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

Authors 

T Y JungD LiJ T ParkS M YoonP L TranB H OhS JanecekSung Goo ParkEui-Jeon WooK H Park

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2012

Citation 

Journal of Biological Chemistry, vol. 287, no. 11, pp. 7979-7989

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 along 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-loopstrand region forming a part of the substrate binding pocket with several aromatic residues, including Phe-95, Phe-96, and Tyr-99.Astructural 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 with in 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.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.M111.304774

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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