Structure predictions and functional insights into Amidase_3 domain containing N-acetylmuramyl-L-alanine amidases from Deinococcus indicus DR1.

ABSTRACT:

Background

N-acetylmuramyl-L-alanine amidases are cell wall modifying enzymes that cleave the amide bond between the sugar residues and stem peptide in peptidoglycan. Amidases play a vital role in septal cell wall cleavage and help separate daughter cells during cell division. Most amidases are zinc metalloenzymes, and E. coli cells lacking amidases grow as chains with daughter cells attached to each other. In this study, we have characterized two amidase enzymes from Deinococcus indicus DR1. D. indicus DR1 is known for its high arsenic tolerance and unique cell envelope. However, details of their cell wall biogenesis remain largely unexplored.

Results

We have characterized two amidases Ami1_Di and Ami2_Di from D. indicus DR1. Both Ami1_Di and A

SUBMITTER: Modi M 

PROVIDER: S-EPMC10964502 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature