Structural highlights
Function
[SUBT_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
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
The crystal structure of subtilisin Carlsberg lightly cross-linked with glutaraldehyde was solved in aqueous solution by X-ray crystallography at 2.3 A resolution. It was found to be virtually identical to the recently determined (Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. & Klibanov, A.M. (1993) Proc. Natl. Acad. Sci. USA 90, 8653) structure of the cross-linked enzyme in anhydrous acetonitrile. The latter structure was found to be significantly more rigid than in water, as reflected by their average B factors. The numbers of subtilisin-bound water molecules in the two structures are similar (114 and 99 in water and in acetonitrile, respectively), but the locations of some half of these bound waters are distinct.
X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile.,Fitzpatrick PA, Ringe D, Klibanov AM Biochem Biophys Res Commun. 1994 Jan 28;198(2):675-81. PMID:8297378[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fitzpatrick PA, Ringe D, Klibanov AM. X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile. Biochem Biophys Res Commun. 1994 Jan 28;198(2):675-81. PMID:8297378 doi:http://dx.doi.org/10.1006/bbrc.1994.1098
