β-Aminopeptidases: Insight into Enzymes without a Known Natural Substrate.

ABSTRACT: β-Aminopeptidases have the unique capability to hydrolyze N-terminal β-amino acids, with varied preferences for the nature of β-amino acid side chains. This unique capability makes them useful as biocatalysts for synthesis of β-peptides and to kinetically resolve β-peptides and amides for the production of enantiopure β-amino acids. To date, six β-aminopeptidases have been discovered and functionally characterized, five from Gram-negative bacteria and one from a fungus, Aspergillus Here we report on the purification and characterization of an additional four β-aminopeptidases, one from a Gram-positive bacterium, Mycolicibacterium smegmatis (BapA_Ms), one from a yeast, Yarrowia lipolytica (BapA_Ylip), and two from Gram-negative bacteria isolated from

SUBMITTER: John-White M 

PROVIDER: S-EPMC6643246 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature