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1. Initial adhesion of Listeria monocytogenes to fine polished stainless steel under flow conditions is determined by prior growth conditions
by Skovager, Anne and Larsen, Marianne Halberg and Castro-Mejia, Josue Leonardo and Hecker, Michael and Albrecht, Dirk and Gerth, Ulf and Arneborg, Nils and Ingmer, Hanne
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
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2. Serine Protease MP2 Activates Prophenoloxidase in the Melanization Immune Response of Drosophila melanogaster: e79533
by An, Chunju and Zhang, Mingming and Chu, Yuan and Zhao, Zhangwu
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
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3. Structural Insights into the Effector - Immunity System Tae4/Tai4 from Salmonella typhimurium. e67362
by Benz, Juliane and Reinstein, Jochen and Meinhart, Anton
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
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4. Rational design for enhancing promiscuous activity of Candida antarcticalipase B: a clue for the molecular basis of dissimilar activities between lipase and serine-protease
by Jung, Suhyun and Kim, Juhyun and Park, Seongsoon
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
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5. Full Text Bacterial peptidoglycan (murein) hydrolases
by Vollmer, Waldemar and Joris, Bernard and Charlier, Paulette and Foster, Simon
FEMS Microbiology Reviews, ISSN 0168-6445, 03/2008, Volume 32, Issue 2, pp. 259 - 286
Most bacteria have multiple peptidoglycan hydrolases capable of cleaving covalent bonds in peptidoglycan sacculi or its fragments. An overview of the different... 
peptidoglycan | lytic transglycosylase | endopeptidase | glucosaminidase | peptidoglycan hydrolase | amidase | Peptidoglycan | Lytic transglycosylase | Peptidoglycan hydrolase | Endopeptidase | Amidase | Glucosaminidase | YYCG/YYCF 2-COMPONENT SYSTEM | L-ALANINE AMIDASE | STREPTOCOCCUS-PNEUMONIAE R6 | BETA-LACTAMASE INDUCTION | CELL-WALL HYDROLASE | SIGNAL-TRANSDUCTION SYSTEM | MICROBIOLOGY | GRAM-NEGATIVE BACTERIA | SOLUBLE LYTIC TRANSGLYCOSYLASE | BACILLUS-SUBTILIS 168 | PENICILLIN-BINDING PROTEINS | Peptidoglycan - metabolism | N-Acetylmuramoyl-L-alanine Amidase - physiology | Bacteriolysis | Cell Division | Cell Wall - metabolism | Spores, Bacterial - enzymology | N-Acetylmuramoyl-L-alanine Amidase - classification | Bacterial Physiological Phenomena | Bacterial Proteins - classification | Cell Wall - enzymology | Bacterial Proteins - physiology | Physiological aspects | Enzymes | Hydrolases | Peptidoglycans
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6. Full Text Enabling cell–cell communication via nanopore formation: structure, function and localization of the unique cell wall amidase AmiC2 of Nostoc punctiforme
by Büttner, Felix M and Faulhaber, Katharina and Forchhammer, Karl and Maldener, Iris and Stehle, Thilo
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
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7. Full Text Expression, purification, and characterization of a bifunctional 99-kDa peptidoglycan hydrolase from Pediococcus acidilactici ATCC 8042
by García-Cano, Israel and Campos-Gómez, Manuel and Contreras-Cruz, Mariana and Serrano-Maldonado, Carlos Eduardo and González-Canto, Augusto and Peña-Montes, Carolina and Rodríguez-Sanoja, Romina and Sánchez, Sergio and Farrés, Amelia
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
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8. Full Text Characterization of an endolysin, LysBPS13, from a Bacillus cereus bacteriophage
by Park, Jaeeun and Yun, Jiae and Lim, Jeong-A and Kang, Dong-Hyun and Ryu, Sangryeol
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
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9. Full Text Activity of the major staphylococcal autolysin Atl
by Biswas, Raja and Voggu, Lalitha and Simon, Uwe Karsten and Hentschel, Petra and Thumm, Günther and Götz, Friedrich
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
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10. Full Text LytA, major autolysin of Streptococcus pneumoniae, requires access to nascent peptidoglycan
by Mellroth, Peter and Daniels, Robert and Eberhardt, Alice and Rönnlund, Daniel and Blom, Hans and Widengren, Jerker and Normark, Staffan and Henriques-Normark, Birgitta and Skolan för teknikvetenskap (SCI) and Experimentell biomolekylär fysik and Tillämpad fysik and KTH and Cellens fysik
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
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11. Full Text Unraveling the differential structural stability and dynamics features of T7 endolysin partially folded conformations
by Sharma, Meenakshi and Kumar, Dinesh and Poluri, Krishna Mohan
BBA - General Subjects, ISSN 0304-4165, 04/2018, Volume 1862, Issue 4, pp. 924 - 935
Characterization of partially collapsed protein conformations at atomic level is a daunting task due to their inherent flexibility and conformational... 
Partially folded conformation | Bacteriophage | T7 endolysin | Lysozyme | Amidase | Molten globule | L-ALANINE AMIDASE | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | STATE | PRION PROTEIN | LYTIC ACTIVITY | TRANSITION | NMR | BIOPHYSICS | BACTERIOPHAGE-T7 LYSOZYME | DLC8 | Protein Structure, Tertiary | Amino Acid Sequence | Temperature | Bacteriophage T7 - genetics | Magnetic Resonance Spectroscopy | Protein Structure, Secondary | Viral Proteins - chemistry | Models, Molecular | Spectrometry, Fluorescence | Viral Proteins - genetics | N-Acetylmuramoyl-L-alanine Amidase - genetics | Viral Proteins - metabolism | Protein Folding | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Bacteriophage T7 - metabolism | Protein Conformation | Circular Dichroism | Hydrogen-Ion Concentration | N-Acetylmuramoyl-L-alanine Amidase - chemistry
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12. Full Text Amidase activity of AmiC controls cell separation and stem peptide release and is enhanced by NlpD in Neisseria gonorrhoeae
by Lenz, Jonathan D and Stohl, Elizabeth A and Robertson, Rosanna M and Hackett, Kathleen T and Fisher, Kathryn and Xiong, Kalia and Lee, Mijoon and Hesek, Dusan and Mobashery, Shahriar and Seifert, H. Steven and Davies, Christopher and Dillard, Joseph P
Journal of Biological Chemistry, ISSN 0021-9258, 05/2016, Volume 291, Issue 20, pp. 10916 - 10933
The human-restricted pathogen Neisseria gonorrhoeae encodes a single N-acetylmuramyl-L-alanine amidase involved in cell separation (AmiC), as compared with... 
MYCOBACTERIUM-TUBERCULOSIS | L-ALANINE AMIDASE | SOLUBLE PEPTIDOGLYCAN | LYTIC TRANSGLYCOSYLASE | PSEUDOMONAS-AERUGINOSA | NOSTOC-PUNCTIFORME | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PENICILLIN-BINDING PROTEINS | BACTERIAL PEPTIDOGLYCAN | FALLOPIAN-TUBE MUCOSA | Peptidoglycan - metabolism | Humans | Peptidoglycan - chemistry | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Catalytic Domain - genetics | Substrate Specificity | N-Acetylmuramoyl-L-alanine Amidase - genetics | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Cations, Divalent - metabolism | Bacterial Proteins - metabolism | Protein Interaction Domains and Motifs | Enzyme Activation | Neisseria gonorrhoeae - genetics | Neisseria gonorrhoeae - metabolism | Neisseria gonorrhoeae - pathogenicity | Amino Acid Substitution | N-Acetylmuramoyl-L-alanine Amidase - chemistry | NOD-like receptor (NLR) | peptidoglycan | Neisseria gonorrhoeae | Microbiology | infectious disease | cell separation | Gram-negative bacteria | cell wall | pathogen-associated molecular pattern (PAMP) | amidase
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13. Full Text The cell wall amidase AmiB is essential for Pseudomonas aeruginosa cell division, drug resistance and viability
by Yakhnina, Anastasiya A and McManus, Heather R and Bernhardt, Thomas G
Molecular Microbiology, ISSN 0950-382X, 09/2015, Volume 97, Issue 5, pp. 957 - 973
Summary The physiological function of cell wall amidases has been investigated in several proteobacterial species. In all cases, they have been implicated in... 
SIGNAL-TRANSDUCTION | L-ALANINE AMIDASE | OUTER-MEMBRANE | GRAM-NEGATIVE BACTERIA | PEPTIDOGLYCAN AMIDASES | CAULOBACTER-CRESCENTUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | 2-COMPONENT SYSTEM | MICROBIOLOGY | ENVELOPE STRESS-RESPONSE | CYTOKINETIC RING | Cell Division - genetics | Amino Acid Sequence | N-Acetylmuramoyl-L-alanine Amidase - deficiency | Microbial Viability - genetics | Pseudomonas aeruginosa - physiology | Cell Wall - enzymology | Pseudomonas aeruginosa - drug effects | N-Acetylmuramoyl-L-alanine Amidase - genetics | Cytokinesis - genetics | Drug Resistance - genetics | Pseudomonas aeruginosa - genetics | Escherichia coli - genetics | Pseudomonas aeruginosa - enzymology | Cell Wall - metabolism | Proteins | Physiological aspects | Pseudomonas aeruginosa | Drug resistance | antibiotic | cell division | peptidoglycan | cell wall | cell envelope | amidase
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