Bacterial β-peptidyl aminopeptidases: on the hydrolytic degradation of β-peptides

• Published in: Applied microbiology and biotechnology 2007-04, Vol.74 (6), p.1197-1204
• Main Authors: Geueke, B, Kohler, H.-P. E
• Format: Article
• Language: English
• Subjects: Amino Acids - chemistry; Amino Acids - metabolism; Aminopeptidase; Aminopeptidases - chemistry; Aminopeptidases - metabolism; Bacteria; Beta-amino acid; Beta-peptide; Biological and medical sciences; Biotechnology; Fundamental and applied biological sciences. Psychology; Hydrolysis; Molecular Structure; Peptides - chemistry; Peptides - metabolism; Proteobacteria; Proteobacteria - metabolism
• ISSN: 0175-7598; 1432-0614
• DOI: 10.1007/s00253-007-0872-5

The special chemical and biological features of β-peptides have been investigated intensively during recent years. Many studies emphasize the restricted biodegradability and the high metabolic stability of this class of compounds. β-Peptidyl aminopeptidases form the first family of enzymes that hydrolyze a variety of short β-peptides and β-amino-acid-containing peptides. All representatives of this family were isolated from Gram-negative bacteria. The substrate specificities of the peptidases vary greatly, but the enzymes have common structural properties, and a similar reaction mechanism can be expected. This review gives an overview on the β-peptidyl aminopeptidases with emphasis on their biochemical and structural properties. Their possible physiological function is discussed. Functionally and structurally related enzymes are compared to the β-peptidyl aminopeptidases.