Unknown

Dataset Information

0

Aminopeptidase C of Aspergillus niger is a novel phenylalanine aminopeptidase.


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-beta NA) and phenylalanine para-nitroanilide (F-pNA), but it also displayed activity towards other amino acids with aromatic side chains coupled to beta NA; other amino acids with non-aromatic side chains coupled to either pNA or beta NA were not hydrolyzed or were poorly hydrolyzed. ApsC was not able to hydrolyze N-acetylalanine-pNA, a substrate for acyl-peptide hydrolases.

SUBMITTER: Basten DE 

PROVIDER: S-EPMC143615 | biostudies-literature | 2003 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Aminopeptidase C of Aspergillus niger is a novel phenylalanine aminopeptidase.

Basten Daniëlle E J W DE   Dekker Peter J T PJ   Schaap Peter J PJ  

Applied and environmental microbiology 20030201 2


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-beta NA) and phenylalanine para-nitroanilide (F-pNA), but it also displayed activity towards other amino  ...[more]

Similar Datasets

| S-EPMC6862759 | biostudies-literature
| S-EPMC4510182 | biostudies-literature
| S-EPMC1287679 | biostudies-literature
| S-EPMC3505779 | biostudies-literature
| S-EPMC7256640 | biostudies-literature
| S-EPMC8151901 | biostudies-literature
| S-EPMC1183701 | biostudies-other
| S-EPMC4893740 | biostudies-literature
| S-EPMC5161314 | biostudies-literature
| S-EPMC1865650 | biostudies-literature