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Title 

Structural Analysis of α-L-arabinofuranosidase from Thermotoga maritima reveals characteristics for thermostability and substrate specificity

Authors 

A DumbrepatilJ M ParkTae Yang JungHyung Nam SongM U JangN S HanT J KimEui-Jeon Woo

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2012

Citation 

Journal of Microbiology and Biotechnology, vol. 22, no. 12, pp. 1724-1730

Keywords 

α-l-arabinofuranosidaseStructural analysisThermotoga maritimaX-ray crystallography

Abstract 

An α-L-arabinofuranosidase (TmAFase) from Thermotoga maritima MSB8 is a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes. In the present study, we carried out the enzymatic characterization and structural analysis of TmAFase. Tight domain associations found in TmAFase, such as an inter-domain disulfide bond (Cys306 and Cys476) in each monomer, a novel extended arm (amino acids 374-385) at the dimer interface, and total 12 salt bridges in the hexamer, may account for the thermostability of the enzyme. One of the xylan binding determinants (Trp96) was identified in the active site, and a region of amino acids (374-385) protrudes out forming an obvious wall at the substrate-binding groove to generate a cavity. The altered cavity shape with a strong negative electrostatic distribution is likely related to the unique substrate preference of TmAFase towards branched polymeric substrates.

ISSN 

1017-7825

Link 

http://dx.doi.org/10.4014/jmb.1208.08043

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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