PMID:7988883
| Citation |
Schroeder, U, Henrich, B, Fink, J and Plapp, R (1994) Peptidase D of Escherichia coli K-12, a metallopeptidase of low substrate specificity. FEMS Microbiol. Lett. 123:153-9 |
|---|---|
| Abstract |
Peptidase D of Escherichia coli was overproduced from a multicopy plasmid and purified to electrophoretic homogeneity. The pure enzyme was stable at 4 degrees C or -20 degrees C and had a pH optimum at pH 9, and a pI of 4.7; the temperature optimum was at 37 degrees C. As the enzyme was activated by Co2+ and Zn2+, and deactivated by metal chelators, it appears to be a metallopeptidase. By activity staining of native gels, 11 dipeptides which are preferentially cleaved by peptidase D were identified. Peptidase D activity required dipeptide substrates with an unblocked amino terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline were not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids were hydrolyzed. Km values of 2 to 5 mM indicate a relatively poor interaction of the enzyme with its substrates. |
| Links | |
| Keywords |
Dipeptidases/isolation & purification; Dipeptidases/metabolism; Enzyme Activation; Enzyme Stability; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Metalloendopeptidases/isolation & purification; Metalloendopeptidases/metabolism; Plasmids; Recombinant Proteins/isolation & purification; Substrate Specificity; Temperature |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.
