Effect of the C-terminal domains and terminal residues of catalytic domain on enzymatic activity and thermostability of lichenase from Clostridium thermocellum.
To elucidate the effects of C-terminal domains of LicMB (mature lichenase from Clostridium thermocellum) and terminal residues of LicMB-CD (catalytic domain of LicMB) on the properties of lichenase, a series of truncated genes were constructed and expressed in E. coli. The Thr-Pro box had a positive effect while the dockerin domain had a negative impact on the properties of LicMB. The N-terminal 10-25th and C-terminal 1-9th residues of LicMB-CD were necessary to retain high thermostability while the N-terminal 1-7th and C-terminal 1-3rd residues were not necessary to maintain enzymatic activity.
College of Animal Sciences, Zhejiang University, 310029, Hangzhou, China.
Dong
D
Niu
Xu-Xia
XX
Zhou
Tao-Yan
TY
Yuan
Zhi-Wei
ZW
Lin
Hui
H
Ruan
Wei-Fen
WF
Li
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D048013:Acetivibrio thermocellus / Q000201:enzymology*; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D050505:Mutant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D055550:Protein Stability; D017384:Sequence Deletion; D013696:Temperature
D001426:Bacterial Proteins; D050505:Mutant Proteins; D006026:Glycoside Hydrolases; C028020:licheninase