ArticleMolecular genetics and genomics : MGG2005
Characterisation of Aspergillus niger prolyl aminopeptidase.
Article in Molecular genetics and genomics : MGG, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 28 citations in OpenAlex.
- Fungal biotransformation of okara into functional food: Comparative species-dependent metabolomic and antioxidant profiles.Current research in food science · 2026Article
- Large-scale genomic analyses with machine learning uncover predictive patterns associated with fungal phytopathogenic lifestyles and traits.Scientific reports · 2023Article
- On the Presence of Gluten-Cleaving Activity in Sodiomyces alkalinus and S. magadiensis Strains.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2023Article
- Article
- Optimized expression of prolyl aminopeptidase in Pichia pastoris and its characteristics after glycosylation.World journal of microbiology & biotechnology · 2016Article
- Studies on the molecular docking and amino Acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis.The protein journal · 2015Article
- Characterization of a multimeric, eukaryotic prolyl aminopeptidase: an inducible and highly specific intracellular peptidase from the non-pathogenic fungus Talaromyces emersonii.Microbiology (Reading, England) · 2009Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
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