Basically the peptidoglycan of Myxobater AL-1 consists of alternating beta-1,4-linked N-acetylglucosamic-N-acetylmuramic acid chains. After splitting the aminosugar backbone with a specific algal enzyme three subunits arise: a monomer, a dimer and a timer. Investigation of the monomer with specific enzymes and comparison of the degradation products to standards derived from other bacterial peptidoglycans suggest the following structure of the monomer peptide: L-alanyl-D-glutamic-L-meso-diaminopimelic-D-alanine. A D-alanyl-D-meso-diaminopimelic acid bond is the bridgebond between the peptides of the subunits.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/BF00436358 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Unlocking dual-mode enzyme activities on bacterial surface: Directional recognition and swift capture of Alicyclobacillus acidoterrestris from fruit juices.
Food Res Int
January 2025
State Key Laboratory of Marine Food Processing and Safety Control, Dalian Polytechnic University, Dalian 116034, Liaoning, China. Electronic address:
The acidophilic and heat-resistant characteristics of Alicyclobacillus acidoterrestris (A. acidoterrestris) pose significant challenges to fruit juice production. Traditional thermal removal methods are often ineffective against this resilient bacterium.
View Article and Find Full Text PDFStructural and Functional Insights into UDP-N-acetylglucosamine-enolpyruvate Reductase (MurB) from Brucella ovis.
Arch Biochem Biophys
January 2025
Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, Zaragoza, Spain; Instituto de Biocomputación y Física de Sistemas Complejos (BIFI) Universidad de Zaragoza, and GBsC (Unizar) join unit to CSIC, Zaragoza, Spain. Electronic address:
The peptidoglycan biosynthetic pathway involves a series of enzymatic reactions in which UDP-N-acetylglucosamine-enolpyruvate reductase (MurB) plays a crucial role in catalyzing the conversion of UDP-N-acetylglucosamine-enolpyruvate (UNAGEP) to UDP-N-acetylmuramic acid. This reaction relies on NADPH and FAD and, since MurB is not found in eukaryotes, it is an attractive target for the development of antimicrobials. MurB from Brucella ovis, the causative agent of brucellosis in sheep, is characterized here.
View Article and Find Full Text PDFCell wall components of gut commensal bacteria stimulate peritrophic matrix formation in malaria vector mosquitoes through activation of the IMD pathway.
PLoS Biol
January 2025
State Key Laboratory of Genetic Engineering, School of Life Sciences, Department of Infectious Diseases, Zhongshan Hospital, Fudan University, Shanghai, China.
The peritrophic matrix (PM) acts as a physical barrier that influences the vector competence of mosquitoes. We have previously shown that gut microbiota promotes PM formation in Anopheles stephensi, although the underlying mechanisms remain unclear. In this study, we identify that the cell wall components of gut commensal bacteria contribute to PM formation.
View Article and Find Full Text PDFRibosomes translocation into the spore of Bacillus subtilis is highly organised and requires peptidoglycan rearrangements.
Nat Commun
January 2025
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
In the spore-forming bacterium Bacillus subtilis transcription and translation are uncoupled and the translational machinery is located at the cell poles. During sporulation, the cell undergoes morphological changes including asymmetric division and chromosome translocation into the forespore. However, the fate of translational machinery during sporulation has not been described.
View Article and Find Full Text PDFExploring the Impact of Amidation Status in -Diaminopimelic-Acid-Containing Disaccharide Peptidoglycan Fragments on Host Innate Immune Activation.
ACS Chem Biol
January 2025
School of Chemistry, Chemical Engineering and Biotechnology, Nanyang Technological University, Singapore 637371, Singapore.
Bacterial peptidoglycan, the essential cell surface polymer that protects bacterial integrity, also serves as the molecular pattern recognized by the host's innate immune system. Although the minimal motifs of bacterial peptidoglycan fragments (PGNs) that activate mammalian NOD1 and NOD2 sensors are well-known and often represented by small canonical ligands, the immunostimulatory effects of natural PGNs, which are structurally more complex and potentially can simultaneously activate both the NOD1 and NOD2 signaling pathways in hosts, have not been comprehensively investigated. In particular, many bacteria incorporate additional structural modifications in peptidoglycans to evade host immune surveillance, resulting in diverse structural variations among natural PGNs that may influence their biological effects in hosts.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!