Cloning of a prolidase gene from Aspergillusnidulans and characterisation of its product
- Cite this article as:
- Jalving, R., Bron, P., Kester, H. et al. Mol Gen Genomics (2002) 267: 218. doi:10.1007/s00438-002-0655-8
- 71 Downloads
Using EST sequence information available from the filamentous fungus Aspergillusnidulans as a starting point, we have cloned the prolidase-encoding gene, designated pepP. Introduction of multiple copies of this gene into the A. nidulans genome leads to overexpression of an intracellular prolidase activity. Prolidase was subsequently purified and characterised from an overexpressing strain. The enzyme activity is dependent on manganese as a cofactor, is specific for dipeptides and hydrolyses only dipeptides with a C-terminal proline residue. Although these proline dipeptides are released both intracellularly and extracellularly, prolidase activity was detected only intracellularly.