Bacterial beta-peptidyl aminopeptidases: on the hydrolytic degradation of beta-peptides.
The special chemical and biological features of beta-peptides have been investigated intensively during recent years. Many studies emphasize the restricted biodegradability and the high metabolic stability of this class of compounds. beta-Peptidyl aminopeptidases form the first family of enzymes that hydrolyze a variety of short beta-peptides and beta-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 beta-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 beta-peptidyl aminopeptidases.
Geueke
B
B
Swiss Federal Institute of Aquatic Science and Technology (Eawag), Ueberlandstrasse 133, 8600 Dübendorf, Switzerland. birgit.geueke@eawag.ch
Kohler
H-P E
HP
D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000626:Aminopeptidases / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D020560:Proteobacteria / Q000378:metabolism*
D000596:Amino Acids; D010455:Peptides; D000626:Aminopeptidases