A surrogate structural platform informed by ancestral reconstruction and resurrection of a putative carbohydrate binding module hybrid illuminates the neofunctionalization of a pectate lyase

2019 ◽  
Vol 207 (3) ◽  
pp. 279-286 ◽  
Author(s):  
Darryl R. Jones ◽  
Richard McLean ◽  
Joanne K. Hobbs ◽  
D. Wade Abbott
2001 ◽  
Vol 355 (1) ◽  
pp. 155 ◽  
Author(s):  
Ian E. BROWN ◽  
Marie H. MALLEN ◽  
Simon J. CHARNOCK ◽  
Gideon J. DAVIES ◽  
Gary W. BLACK

2017 ◽  
Vol 12 (2) ◽  
pp. 36-43
Author(s):  
Rekha Chamanlal Akhani ◽  
Arti Thakarshibhai Patel ◽  
Manisha Jignesh Patel ◽  
Samir Ramnikbhai Dedania ◽  
Darshan Hasmukhbhai Patel

FEBS Journal ◽  
2015 ◽  
Vol 282 (22) ◽  
pp. 4341-4356 ◽  
Author(s):  
Renee M. Happs ◽  
Xiaoyang Guan ◽  
Michael G. Resch ◽  
Mark F. Davis ◽  
Gregg T. Beckham ◽  
...  

2004 ◽  
Vol 238 (1) ◽  
pp. 71-78
Author(s):  
Fernando M.V. Dias ◽  
Arun Goyal ◽  
Harry J. Gilbert ◽  
José A.M. Prates ◽  
Luís M.A. Ferreira ◽  
...  

2010 ◽  
Vol 192 (24) ◽  
pp. 6492-6493 ◽  
Author(s):  
Angel Angelov ◽  
Susanne Liebl ◽  
Meike Ballschmiter ◽  
Mechthild Bömeke ◽  
Rüdiger Lehmann ◽  
...  

ABSTRACT Spirochaeta thermophila is a thermophilic, free-living anaerobe that is able to degrade various α- and β-linked sugar polymers, including cellulose. We report here the complete genome sequence of S. thermophila DSM 6192, which is the first genome sequence of a thermophilic, free-living member of the Spirochaetes phylum. The genome data reveal a high density of genes encoding enzymes from more than 30 glycoside hydrolase families, a noncellulosomal enzyme system for (hemi)cellulose degradation, and indicate the presence of a novel carbohydrate-binding module.


2010 ◽  
Vol 114 (1) ◽  
pp. 49-58 ◽  
Author(s):  
Toshifumi Yui ◽  
Hirohide Shiiba ◽  
Yuya Tsutsumi ◽  
Sachio Hayashi ◽  
Tatsuhiko Miyata ◽  
...  

2005 ◽  
Vol 18 (10) ◽  
pp. 497-501 ◽  
Author(s):  
Emily M. Kwan ◽  
Alisdair B. Boraston ◽  
Bradley W. McLean ◽  
Douglas G. Kilburn ◽  
R. Antony J. Warren

2009 ◽  
Vol 76 (1) ◽  
pp. 356-360 ◽  
Author(s):  
Sasikala Anbarasan ◽  
Janne Jänis ◽  
Marja Paloheimo ◽  
Mikko Laitaoja ◽  
Minna Vuolanto ◽  
...  

ABSTRACT The effects of different structural features on the thermostability of Thermopolyspora flexuosa xylanase XYN10A were investigated. A C-terminal carbohydrate binding module had only a slight effect, whereas a polyhistidine tag increased the thermostability of XYN10A xylanase. In contrast, glycosylation at Asn26, located in an exposed loop, decreased the thermostability of the xylanase. The presence of a substrate increased stability mainly at low pH.


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