Loading...
Please wait, while we are loading the content...
Similar Documents
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Nguyen-Distèche, Martine Leyh-Bouille, Mélina Pirlot, S. Frère, Jean Marie Ghuysen, J. M. |
| Copyright Year | 1986 |
| Abstract | In water, the purified 26 000-Mr membrane-bound DD-peptidase of Streptomyces K15 hydrolyses the ester carbonyl donor Ac2-L-Lys-D-Ala-D-lactate (release of D-lactate) and the amide carbonyl donor Ac2-L-Lys-D-Ala-D-Ala (release of D-alanine) with accumulation of acyl- (Ac2-L-Lys-D-alanyl-)enzyme. Whereas hydrolysis of the ester substrate proceeds to completion, hydrolysis of the amide substrate is negligible because of the capacity of the K15 DD-peptidase for utilizing the released D-alanine in a transfer reaction (Ac2-L-Lys-D-Ala-D-Ala + D-Ala----Ac2-L-Lys-D-Ala-D-Ala + D-Ala) that maintains the concentration of the amide substrate at a constant level. In the presence of an amino acceptor X-NH2 (Gly-Gly or Gly-L-Ala) related to the Streptomyces peptidoglycan, both amide and ester carbonyl donors are processed without detectable accumulation of acyl-enzyme. Under proper conditions, the acceptor activity of water and, in the case of the amide substrate, the acceptor activity of the released D-alanine can be totally overcome so that the two substrates are quantitatively converted into transpeptidated product Ac2-L-Lys-D-Ala-NH-X (and hydrolysis is prevented). Experimental evidence suggests that the amino acceptor modifies both the binding of the carbonyl donor to the enzyme and the ensuing rate of enzyme acylation. |
| File Format | PDF HTM / HTML |
| DOI | 10.1042/bj2350167 |
| PubMed reference number | 2874789 |
| Journal | Medline |
| Volume Number | 235 |
| Issue Number | 1 |
| Alternate Webpage(s) | http://orbi.ulg.ac.be/bitstream/2268/83010/1/DISTECHE_1986-Streptomyces-K15-DD-peptidase.pdf |
| Alternate Webpage(s) | https://doi.org/10.1042/bj2350167 |
| Journal | The Biochemical journal |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
