Structural highlights
Function
[PEPA_PIG] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
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 structure of porcine pepsin crystallized in the presence of dimethyl sulphoxide has been analysed by X-ray crystallography to obtain insights into the structural events that occur at the onset of chemical denaturation of proteins. The results show that one dimethyl sulphoxide molecule occupies a site on the surface of pepsin interacting with two of its residues. An increase in the average temperature factor of pepsin in the presence of dimethyl sulphoxide has been observed indicating protein destabilization induced by the denaturant. Significant increase in the temperature factor and weakening of the electron density have been observed for the catalytic water molecule located between the active aspartates. The conformation of pepsin remains unchanged in the crystal structure. However, the enzyme assay and circular dichroism studies indicate that dimethyl sulphoxide causes a slight change in the secondary structure and complete loss of activity of pepsin in solution.
Effect of dimethyl sulphoxide on the crystal structure of porcine pepsin.,Kesavulu MM, Ramasubramanian S, Suguna K Biochem Biophys Res Commun. 2005 Jun 17;331(4):1510-4. PMID:15883044[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kesavulu MM, Ramasubramanian S, Suguna K. Effect of dimethyl sulphoxide on the crystal structure of porcine pepsin. Biochem Biophys Res Commun. 2005 Jun 17;331(4):1510-4. PMID:15883044 doi:10.1016/j.bbrc.2005.03.247
