Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cyclodextrin glycosyltransferase (CGTase) catalyzes the formation of cyclodextrins from starch. Among the CGTases with known three-dimensional structure, Thermoanaerobacterium thermosulfurigenes CGTase has the highest thermostability. By replacing amino acid residues in the B-domain of Bacillus circulans CGTase with those from T. thermosulfurigenes CGTase, we identified a B. circulans CGTase mutant (with N188D and K192R mutations), with a strongly increased activity half-life at 60 degrees C. Asp188 and Arg192 form a salt bridge in T. thermosulfurigenes CGTase. Structural analysis of the B. circulans CGTase mutant revealed that this salt bridge is also formed in the mutant. Thus, the activity half-life of this enzyme can be enhanced by rational protein engineering.
Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge.,Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L Proteins. 2004 Jan 1;54(1):128-34. PMID:14705029[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L. Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge. Proteins. 2004 Jan 1;54(1):128-34. PMID:14705029 doi:10.1002/prot.10516
