ArticleBMC microbiology2024
Structure predictions and functional insights into Amidase_3 domain containing N-acetylmuramyl-L-alanine amidases from Deinococcus indicus DR1.
Article in BMC microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- The innate immune protein calprotectin ablates the bactericidal activity of β-lactam antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Inferred functional potential of microbial communities in traditional African fermented dairy products using 16S rRNA.Access microbiology · 2026Article
- The innate immune protein calprotectin incapacitates the bactericidal activity of β-lactam antibiotics.bioRxiv : the preprint server for biology · 2025Article
- Bioinformatics-guided decoding of the Ancylostoma duodenale genome for the identification of potential vaccine targets.BMC genomics · 2025Article
- Characterization ofAntibiotics (Basel, Switzerland) · 2025Article
- Comparative Transcriptomics of the Entomopathogenic Fungus Beauveria bassiana Grown on Aerial Surface and in Liquid Environment.Current microbiology · 2024Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundN-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.
resultsWe have characterized two amidases Ami1
conclusionOur results indicate that Ami1
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Registered trials
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