Aminopeptidase C of Aspergillus niger is a Novel Phenylalanine Aminopeptidase

E.J.W. Basten, P.J.T. Dekker, P.J. Schaap

Research output: Contribution to journalArticleAcademicpeer-review

12 Citations (Scopus)

Abstract

A novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share similarity with some mammalian acyl-peptide hydrolase sequences. ApsC was found to be most active towards phenylalanine beta-naphthylamide (F-betaNA) and phenylalanine para-nitroanilide (F-betaNA), but it also displayed activity towards other amino acids with aromatic side chains coupled to betaNA; other amino acids with nonaromatic side chains coupled to either pNA or betaNA were not hydrolyzed or were poorly hydrolyzed. ApsC was not able to hydrolyze N-acetylalanine-pNA, a substrate for acyl-peptide hydrolases.
Original languageEnglish
Pages (from-to)1246-1250
JournalApplied and Environmental Microbiology
Volume69
DOIs
Publication statusPublished - 2003

Keywords

  • flavored peptides
  • sequence-analysis
  • gene
  • cloning
  • proteins
  • enzyme
  • yeast
  • carboxypeptidase
  • bitterness
  • expression

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