Characterisation of Aspergillus niger prolyl aminopeptidase

E.J.W. Basten, A.P.H.A. Moers, A.J.J. van Ooyen, P.J. Schaap

Research output: Contribution to journalArticleAcademicpeer-review

21 Citations (Scopus)

Abstract

We have cloned a gene (papA) that encodes a prolyl aminopeptidase from Aspergillus niger. Homologous genes are present in the genomes of the Eurotiales A. nidulans, A. fumigatus and Talaromyces emersonii, but the gene is not present in the genome of the yeast Saccharomyces cerevisiae. Cell extracts of strains overexpressing the gene under the control of its own promoter showed a fourfold to sixfold increase in prolyl aminopeptidase activity, but no change in phenylalanine or leucine aminopeptidase activity. The overexpressed enzyme was subsequently purified and characterised. The enzyme specifically removes N-terminal proline and hydroxyproline residues from peptides. It is the first enzyme of its kind from a eukaryotic organism that has been characterised
Original languageEnglish
Pages (from-to)673-679
JournalMolecular Genetics and Genomics
Volume272
Issue number6
DOIs
Publication statusPublished - 2005

Keywords

  • proline iminopeptidase gene
  • subsp bulgaricus cnrz-397
  • campestris pv. citri
  • oligopeptidase family
  • serratia-marcescens
  • bacillus-coagulans
  • expressed enzyme
  • cloning
  • identification
  • mutagenesis

Fingerprint Dive into the research topics of 'Characterisation of Aspergillus niger prolyl aminopeptidase'. Together they form a unique fingerprint.

  • Cite this