{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(4)"],"submitter":["Kaman WE"],"pubmed_abstract":["Previously we described the discovery of a Bacillus spp. specific peptidase activity related to d-stereospecific peptidases (DSPs). The peptidase showed a strong preference for d-leucine and d-valine amino acids. These amino acids are present in the structure of the non-ribosomal peptide (NRP) antibiotics gramicidin A, B and C and polymyxin E. To examine if the Bacillus spp. DSP-related peptidase can hydrolyze these NRPs, the effect of gramicidin A and C and polymyxin E on peptidase activity in Bacillus anthracis culture supernatant was monitored. It was found that both gramicidins inhibited the DSP-related activity in a competitive manner. MALDI-TOF analysis revealed that upon incubation with B. anthracis culture supernatant gramicidin A hydrolyzation products appeared. This study shows that the Bacillus spp. specific DSP-like peptidase was potentially produced by the bacteria to gain intrinsic resistance against NRP antibiotics. These results are of utmost importance in research towards antimicrobial resistance, whereas transfer of DSP-related activity to other clinically relevant pathogens can be a serious threat to human health."],"journal":["Environmental microbiology reports"],"pagination":["570-576"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9541196"],"repository":["biostudies-literature"],"pubmed_title":["Gramicidin A is hydrolyzed by a d-stereospecific peptidase produced by Bacillus anthracis."],"pmcid":["PMC9541196"],"pubmed_authors":["Kaman WE","Bikker FJ","Voskamp-Visser AI","Nazmi K"],"additional_accession":[]},"is_claimable":false,"name":"Gramicidin A is hydrolyzed by a d-stereospecific peptidase produced by Bacillus anthracis.","description":"Previously we described the discovery of a Bacillus spp. specific peptidase activity related to d-stereospecific peptidases (DSPs). The peptidase showed a strong preference for d-leucine and d-valine amino acids. These amino acids are present in the structure of the non-ribosomal peptide (NRP) antibiotics gramicidin A, B and C and polymyxin E. To examine if the Bacillus spp. DSP-related peptidase can hydrolyze these NRPs, the effect of gramicidin A and C and polymyxin E on peptidase activity in Bacillus anthracis culture supernatant was monitored. It was found that both gramicidins inhibited the DSP-related activity in a competitive manner. MALDI-TOF analysis revealed that upon incubation with B. anthracis culture supernatant gramicidin A hydrolyzation products appeared. This study shows that the Bacillus spp. specific DSP-like peptidase was potentially produced by the bacteria to gain intrinsic resistance against NRP antibiotics. These results are of utmost importance in research towards antimicrobial resistance, whereas transfer of DSP-related activity to other clinically relevant pathogens can be a serious threat to human health.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-04-08T13:41:21.372Z","creation":"2025-04-19T04:47:56.833Z"},"accession":"S-EPMC9541196","cross_references":{"pubmed":["35403341"],"doi":["10.1111/1758-2229.13069"]}}