NDLI: The role of disulfide bond in hyperthermophilic endocellulase

Content Provider	Springer Nature Link
Author	Kim, Han Woo Ishikawa, Kazuhiko
Copyright Year	2013
Abstract	The hyperthermophilic endocellulase, EGPh (glycosyl hydrolase family 5) from Pyrococcus horikoshii possesses 4 cysteine residues forming 2 disulfide bonds, as identified by structural analysis. One of the disulfide bonds is located at the proximal region of the active site in EGPh, which exhibits a distinct pattern from that of the thermophilic endocellulase EGAc (glycosyl hydrolase family 5) of Acidothermus cellulolyticus despite the structural similarity between the two endocellulases. The structural similarity between EGPh and EGAc suggests that EGPh possesses a structure suitable for changing the position of the disulfide bond corresponding to that in EGAc. Introduction of this alternative disulfide bond in EGPh, while removing the original disulfide bond, did not result in a loss of enzymatic activity but the EGPh was no longer hyperthermostable. These results suggest that the contribution of disulfide bond to hyperthermostability at temperature higher than 100 °C is restrictive, and that its impact is dependent on the specific structural environment of the hyperthermophilic proteins. The data suggest that the structural position and environment of the disulfide bond has a greater effect on high-temperature thermostability of the enzyme than on the potential energy of the dihedral angle that contributes to disulfide bond cleavage.
Starting Page	593
Ending Page	599
Page Count	7
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	17
Issue Number	4
e-ISSN	14334909
Language	English
Publisher	Springer Japan
Publisher Date	2013-04-27
Publisher Place	Japan
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Disulfide bond Cellulase Archaea Thermostability Crystal structure Protein engineering Microbiology Biotechnology Biochemistry Microbial Ecology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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