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Structure predictions and functional insights into Amidase_3 domain containing N-acetylmuramyl-L-alanine amidases from Deinococcus indicus DR1.
- Source :
- BMC Microbiology; 3/26/2024, Vol. 24 Issue 1, p1-15, 15p
- Publication Year :
- 2024
-
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<subscript>Di</subscript> and Ami2<subscript>Di</subscript> from D. indicus DR1. Both Ami1<subscript>Di</subscript> and Ami2<subscript>Di</subscript> suppress cell separation defects in E. coli amidase mutants, suggesting that these enzymes are able to cleave septal cell wall. Ami1<subscript>Di</subscript> and Ami2<subscript>Di</subscript> proteins possess the Amidase_3 catalytic domain with conserved –GHGG- motif and Zn<superscript>2+</superscript> binding sites. Zn<superscript>2+</superscript>- binding in Ami1<subscript>Di</subscript> is crucial for amidase activity. AlphaFold2 structures of both Ami1<subscript>Di</subscript> and Ami2<subscript>Di</subscript> were predicted, and Ami1<subscript>Di</subscript> was a closer homolog to AmiA of E. coli. Conclusion: Our results indicate that Ami1<subscript>Di</subscript> and Ami2<subscript>Di</subscript> enzymes can cleave peptidoglycan, and structural prediction studies revealed insights into the activity and regulation of these enzymes in D. indicus DR1. [ABSTRACT FROM AUTHOR]
- Subjects :
- AMIDASES
ESCHERICHIA coli
ENZYME regulation
PEPTIDES
METALLOENZYMES
CELL separation
Subjects
Details
- Language :
- English
- ISSN :
- 14712180
- Volume :
- 24
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- BMC Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 176265332
- Full Text :
- https://doi.org/10.1186/s12866-024-03225-4