Abstract
The gene coding for glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase was cloned from Pseudomonas sp. GK16 and some of its characteristics were analyzed. The complete nucleotide sequence revealed that the putative open reading frame is 2160 bases long and encodes 720 amino acids. By SDS-PAGE three proteins, approximately corresponding to 70, 54 and 16 kDa of molecular weight, were detected in E. coli cells carrying pGAP18. The largest protein should be a precursor which is not processed yet, while the other two proteins must be derived from the precursor by the proteolytic processing.
| Original language | English |
|---|---|
| Pages (from-to) | 375-380 |
| Number of pages | 6 |
| Journal | Journal of microbiology and biotechnology |
| Volume | 6 |
| Issue number | 6 |
| Publication status | Published - 1996 Dec |
Keywords
- Cloning
- Expression
- GL-7-ACA acylase
- Nucleotide sequence
- Processing
- Pseudomonas sp. GK16
ASJC Scopus subject areas
- Biotechnology
- Applied Microbiology and Biotechnology