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International Journal of Food Microbiology, ISSN 0168-1605, 07/2013, Volume 165, Issue 1, pp. 35 - 42
Listeria monocytogenes is a food-borne pathogen known to persist in food production environments, where it is able to attach and form biofilms, potentially... 
Amidase
Journal Article
PLoS ONE, 11/2013, Volume 8, Issue 11
In arthropods, melanization plays a major role in the innate immune response to encapsulate and kill the invasive organisms. It is mediated by a serine... 
Amidase
Journal Article
PLoS ONE, 06/2013, Volume 8, Issue 6
Type-6-secretion systems of Gram-negative bacteria are widely distributed needle-like multi-protein complexes that are involved in microbial defense... 
Amidase
Journal Article
RSC Advances, 01/2013, Volume 3, Issue 8, pp. 2590 - 2594
Lipase and serine-protease display distinct activities toward esters and amides, although they share a common catalytic triad (Asp/Glu-His-Ser). Lipases can... 
Amidase
Journal Article
The FEBS Journal, ISSN 1742-464X, 04/2016, Volume 283, Issue 7, pp. 1336 - 1350
To orchestrate a complex life style in changing environments, the filamentous cyanobacterium Nostoc punctiforme facilitates communication between neighboring... 
cell–cell communication | multicellular cyanobacteria | AmiC | bacterial cell wall | N‐acetylmuramoyl‐l‐alanine amidase | N-acetylmuramoyl- l -alanine amidase | cell-cell communication | SYSTEM | VISUALIZATION | DOMAIN | RECOGNITION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PEPTIDOGLYCAN | CYANOBACTERIA | N-acetylmuramoyl-L-alanine amidase | DIFFERENTIATION | HETEROCYST DEVELOPMENT | REVEALS | Peptidoglycan - metabolism | Protein Structure, Tertiary | Nostoc - enzymology | Catalytic Domain | Temperature | Biocatalysis | Protein Structure, Secondary | Peptidoglycan - chemistry | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Models, Molecular | Crystallography, X-Ray | Binding Sites - genetics | Cell Wall - enzymology | Nostoc - cytology | Nanopores | N-Acetylmuramoyl-L-alanine Amidase - genetics | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Bacterial Proteins - metabolism | Mutation | Circular Dichroism | Microscopy, Fluorescence | Nostoc - genetics | N-Acetylmuramoyl-L-alanine Amidase - chemistry | Glutamate | Enzymes | Cellular biology | Cyanobacteria | Crystal structure | Biological properties | Glutamic acid | High resolution | Intercellular signalling | Separation | Amidase | Homology | Biochemistry | Cell interactions | Data bases | Control | N-Acetylmuramoyl-L-alanine amidase | Databases | E coli | L-Alanine | Bacteria | Cell septa | Recycling | Catalysis | Localization | Communication | Binding | Alanine | Cell walls | Peptidoglycans | Changing environments | Septum | Cell division | Waste management | Splitting | Point mutation | Holes | Porosity | Arrays | Immunofluorescence | Structure-function relationships
Journal Article
Applied Microbiology and Biotechnology, ISSN 0175-7598, 10/2015, Volume 99, Issue 20, pp. 8563 - 8573
Pediococcus acidilactici ATCC 8042 is a lactic acid bacteria that inhibits pathogenic microorganisms such as Staphylococcus aureus through the production of... 
Life Sciences | Zymogram | Biotechnology | 4-Nitrophenyl N -acetyl-β- d -glucosamine | Pediococcus acidilactici ATCC 8042 | Peptidoglycan hydrolase | Microbiology | N -acetylmuramoyl-L-alanine amidase | Microbial Genetics and Genomics | N -acetylglucosaminidase | 4-Nitrophenyl N-acetyl-β-d-glucosamine | N-acetylglucosaminidase | N-acetylmuramoyl-L-alanine amidase | LISTERIA-MONOCYTOGENES | LYSOZYME | CELL WALL HYDROLASES | IDENTIFICATION | ANTIBACTERIAL ACTIVITY | BACILLUS-SUBTILIS | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | 4-Nitrophenyl N-acetyl-beta-D-glucosamine | LACTIC-ACID BACTERIA | DIVERSITY | LYSOSTAPHIN | SEPARATION | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Temperature | Molecular Weight | Microbial Viability - drug effects | Enzyme Stability | Molecular Sequence Data | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | N-Acetylmuramoyl-L-alanine Amidase - genetics | Pediococcus - enzymology | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Recombinant Proteins - isolation & purification | Sequence Alignment | Cloning, Molecular | N-Acetylmuramoyl-L-alanine Amidase - isolation & purification | Chromatography, Gel | Micrococcus - drug effects | Hydrogen-Ion Concentration | N-Acetylmuramoyl-L-alanine Amidase - chemistry | Enzymes | Analysis | Hydrolases | Influence | Research | Gene expression | Peptide bonds | Studies | Pathogens | Peptides | Bacteria | Biosynthesis
Journal Article
FEMS Microbiology Letters, ISSN 0378-1097, 07/2012, Volume 332, Issue 1, pp. 76 - 83
Abstract Use of bacteriophages as biocontrol agents is a promising tool for controlling pathogenic bacteria including antibiotic-resistant bacteria. Not only... 
N‐acetylmuramyl‐l‐alanine amidase | endolysin | Bacillus cereus | N-acetylmuramyl-l-alanine amidase | Endolysin | L-ALANINE AMIDASE | FOOD POISONING TOXINS | MURAMIC ACID | HYDROLASES | PEPTIDOGLYCAN | LYSIN | RECOGNITION PROTEINS PGRPS | LYSOZYME | MICROBIOLOGY | Peptidoglycan - metabolism | Temperature | Viral Proteins - metabolism | Endopeptidases - chemistry | Osmolar Concentration | Anti-Bacterial Agents - chemistry | Genes, Viral | Bacteriophages - genetics | Binding Sites | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Endopeptidases - metabolism | Viral Proteins - chemistry | Enzyme Stability | Glycerol | Recombinant Proteins - chemistry | Viral Proteins - genetics | Anti-Bacterial Agents - metabolism | Edetic Acid | Recombinant Proteins - genetics | Detergents | N-Acetylmuramoyl-L-alanine Amidase - genetics | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Endopeptidases - genetics | Bacillus cereus - chemistry | Bacillus cereus - virology | Muramic Acids - metabolism | Hydrogen-Ion Concentration | N-Acetylmuramoyl-L-alanine Amidase - chemistry | Bacteriophages | Alanine | Incubation | Cell walls | Biological control | Food contamination | Phages | Amidase | Peptidoglycans | Antimicrobial agents | Genomes | Thermal stability | Antibiotics | Ethylenediaminetetraacetic acids | Antibiotic resistance | L-Alanine | Bacteria
Journal Article
FEMS Microbiology Letters, ISSN 0378-1097, 06/2006, Volume 259, Issue 2, pp. 260 - 268
Abstract The major autolysin of Staphylococcus aureus (AtlA) and of Staphylococcus epidermidis (AtlE) are well-studied enzymes. Here we created an atlA... 
peptidoglycan | Staphylococcus epidermidis | major autolysin | Staphylococcus aureus | N‐acetylmuramoyl‐l‐alanine amidase | Major autolysin | Peptidoglycan | N-acetylmuramoyl-l-alanine amidase | BACTERIAL CELL-WALLS | L-ALANINE AMIDASE | AUREUS AUTOLYSIN | MICROBIOLOGY | IDENTIFICATION | BETA-N-ACETYLGLUCOSAMINIDASE | D-GLUTAMIC ACID | GENE | BACILLUS-SUBTILIS | N-acetylmuramoyl-L-alanine amidase | EPIDERMIDIS | Peptidoglycan - metabolism | Recombinant Proteins - metabolism | Staphylococcus aureus - genetics | Genes, Bacterial | Green Fluorescent Proteins - metabolism | Virulence | Green Fluorescent Proteins - genetics | Recombinant Proteins - genetics | Genetic Complementation Test | N-Acetylmuramoyl-L-alanine Amidase - genetics | Staphylococcus aureus - pathogenicity | Staphylococcus epidermidis - genetics | Staphylococcus epidermidis - metabolism | Bacterial Adhesion | Hydrolysis | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Mutagenesis | Recombination, Genetic | Gene Deletion | Staphylococcus epidermidis - pathogenicity | Staphylococcus aureus - metabolism | Alanine | Cell walls | Amidase | Peptidoglycans | Electron micrographs | Cell surface | Substrates | Gene sequencing | Deletion mutant | Biofilms | Clonal deletion | Acids | E coli | Substrate specificity | Penicillin | L-Alanine | Deletion | Acetylation
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2012, Volume 287, Issue 14, pp. 11018 - 11029
Background: The regulation of cell wall hydrolysis by the pneumococcal autolysin LytA is poorly understood. Results: The cell wall is susceptible to... 
PENICILLIN RESISTANCE | PNEUMOCOCCAL AUTOLYSIN | ENZYME-ACTIVITY | FRATRICIDE | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ATTENUATION | SURFACE-PROTEINS | RECOGNITION PROTEIN | VIRULENCE | PNEUMOLYSIN | Peptidoglycan - metabolism | Bacteriolysis - drug effects | Detergents - pharmacology | Streptococcus pneumoniae - drug effects | Extracellular Space - drug effects | Cytoplasm - metabolism | Protein Transport - drug effects | N-Acetylmuramoyl-L-alanine Amidase - genetics | Streptococcus pneumoniae - cytology | Cell Division - drug effects | Protein Sorting Signals | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Peptidoglycan - biosynthesis | Extracellular Space - metabolism | Deoxycholic Acid - pharmacology | N-Acetylmuramoyl-L-alanine Amidase - pharmacology | Streptococcus pneumoniae - metabolism | Anti-Bacterial Agents - pharmacology | Cell Proliferation - drug effects | Cytoplasm - drug effects | Streptococcus pneumoniae - enzymology | N-Acetylmuramoyl-L-alanine Amidase - chemistry | Cell Wall | Autolysis | Peptidoglycan | Streptococcus | Microbiology | Molecular Biology | Antibiotics | Pneumococcus | LytA | Biological Sciences | Sensitized cells | Cell walls | Amidase | Extracellular concentration | Peptidoglycans | Cell wall synthesis | Choline binding domain | Threshold concentrations | Extracellular | Exponential growth | Nutrient depletion | Streptococcus pneumoniae | Naturvetenskap | Biokemi och molekylärbiologi | Virulence factors | Biologiska vetenskaper | Biochemistry and Molecular Biology | Natural Sciences | Biological approach | Potential substrate | Stationary phase
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2016, Volume 291, Issue 20, pp. 10916 - 10933
Journal Article