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(GlcNAc-MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala)2 + H2O
?
-
-
-
?
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP + H2O
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP
-
-
-
-
?
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala
-
-
-
-
?
1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
?
-
-
-
?
1,6-anhydro-N-acetylmuramic-acid-L-Ala-gamma-D-Glu-L-Lys + H2O
1,6-anhydro-N-acetylmuramate + L-Ala-gamma-D-Glu-L-Lys
-
-
-
?
1,6-anhydromuropeptide + H2O
?
-
AmpD has a strict specificity for 1,6-anhydromuropeptides, three-dimensional structure, active site structure, catalytic mechanism, Lys-162 and Tyr-63 are probably involved in substrate binding
-
-
?
4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O
?
-
the substrate is likely not turned over in vitro by AmpD
-
-
?
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGln-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
?
-
-
-
-
?
bacterial peptidoglycan + H2O
?
-
-
-
-
?
bacterial spore peptidoglycan
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-Ala-D-isoglutaminyl-(L)-(beta-N-acetyl-glucosaminyl-(1-4)-N-acetylmuramoyl-L-Ala-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-Ala)-(D)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-(beta-N-acetyl-glucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine)-(D)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-(beta-N-acetyl-glucosaminyl-(1-4)-N-acetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine)-(D)-meso-2,6-diaminopimelic acid-(D)-amide
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoate + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramic acid + L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
-
-
-
?
biotin-peptidoglucan + H2O
?
-
-
-
?
GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
-
-
-
?
GlcNAc-anhydroMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
GlcNAc-anhydroMurNAc + L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala
biphasic behavior: rapid exponential phase preceding a linear phase (0.027 mM substrate, 0.000106 mM enzyme)
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
?
GlcNAc-MurNAc-anhydro-L-Ala-D-gluc-meso-diaminopimelyl-D-Ala + H2O
?
-
-
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoGIn-meso-diaminopimelyl-(D)-amide-(L)-D-Ala-D-Ala + H2O
?
-
-
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoGln-meso-diaminopimelyl-D-Ala + H2O
?
-
-
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala + H2O
N-acetylglucosaminyl-N-acetylmuramic acid + L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala
L-alanine-p-nitroanilide + H2O
?
-
-
-
-
?
murein + H2O
?
-
also murein extracted from cells grown in the presence of penicillin, N-acetylated murein
-
-
?
MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
MurNAc-L-Ala-D-isoGln-L-Lys + H2O
MurNAc + L-Ala-D-isoGln-L-Lys
MurNAc-tripeptide, minimum peptidoglycan fragment hydrolyzed by PGRP-L
-
-
?
MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala + H2O
MurNAc + L-Ala-D-isoGln-L-Lys-D-Ala
-
-
-
?
N-(beta-1,4-N-acetylglucosaminyl-N-acetylmuramoyl-L-alanyl-gamma-D-isoglutaminyl)-L-lysyl-D-alanine + H2O
?
-
-
-
-
?
N-acetyl-glucosaminyl(beta1-4)N-acetylmuramoyl-tetrapeptide + H2O
?
-
-
-
-
?
N-acetyl-glucosaminyl(beta1-4)N-acetylmuramoyl-tripeptide + H2O
?
-
-
-
-
?
N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-tripeptide + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
N-acetylmuramoyl-L-alanine-gamma-D-glutamyl-mesodiaminopimelic acid + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
N-acetylmuramoyl-L-alanyl-D-glutamine + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-gamma-D-glutaminyl-meso-diaminopimelic acid + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
?
-
-
-
-
?
peptidoglycan + H2O
peptidoglycan-derived fragment peptides
phospho-N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
?
-
-
-
-
?
uridine diphospho-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid + H2O
?
-
-
-
-
?
additional information
?
-
cell walls
?
-
from Bacillus megaterium, Bacillus subtilis
-
-
?
cell walls
?
-
from Bacillus subtilis, [14C] glucosamine-labeled
-
-
?
cell walls
?
-
from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
-
-
?
cell walls
?
-
from Bacillus subtilis
-
-
?
cell walls
?
-
from Bacillus subtilis, [14C] glucosamine-labeled
-
-
?
cell walls
?
-
from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
-
-
?
cell walls
?
Dubowvirus dv11
-
cell wall anchor structures from staphylococcal surface proteins
-
-
?
cell walls
?
-
from Bacillus lentus
-
-
?
cell walls
?
-
from Micrococcus luteus, Listeria monocytogenes
-
-
?
cell walls
?
-
from Bacillus polymyxa
-
-
?
cell walls
?
Pneumococcal bacteriophage HB-3
-
pneumococcal cell walls, labeled with [methyl-3H]choline, L-[4,5-3H]lysine monohydrochloride, or [2-14C]ethanolamine
-
-
?
cell walls
?
-
from Bacillus megaterium, Bacillus subtilis
-
-
?
cell walls
?
-
from Micrococcus luteus ATCC 46898
-
-
?
cell walls
?
-
from Micrococcus luteus ATCC 46898
-
-
?
cell walls
?
-
pneumococcal cell walls labeled with [methyl-3H] or [3H]lysine
-
-
?
cell walls
?
-
from Diplococcus pneumoniae
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
?
-
the cell separation amidase can utilize the small synthetic peptidoglycan a pentapeptide fragment as substrate. AmiC can cleave one peptide stem from synthetic PG dimer
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
?
-
the cell separation amidase can utilize the small synthetic peptidoglycan a pentapeptide fragment as substrate. AmiC can cleave one peptide stem from synthetic PG dimer
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
?
-
small synthetic peptidoglycan fragment
-
-
?
GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
?
-
small synthetic peptidoglycan fragment
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala + H2O
N-acetylglucosaminyl-N-acetylmuramic acid + L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala
-
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala + H2O
N-acetylglucosaminyl-N-acetylmuramic acid + L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala
-
-
-
?
MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
-
-
-
?
MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Bacillus cereus phage BPS13
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, the immunostimulatory properties of PGRP-SC1B-degraded peptidoglycan are highly reduced
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, peptidoglycan substrate from Escherichia coli, PGRP-SB1 is highly active against peptidoglycans that have a diaminopimelic acid residue in the cross-linking peptide, but lacks activity to most lysine-containing peptidoglycans
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme performs cell wall lysis by cleavage of N-acetylmuramoyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan, peptidoglycan substrates from Staphylococcus aureus, Micrococcus luteus, and Bacillus megaterium, the enzyme hydrolyzes the lactylamide bond between the glycan strand and the cross-linking peptides, analysis of the cleavage products by mass spectrometry
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme hydrolyzes bacterial peptidoglycan
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
-
the enzyme performs cell wall lysis by cleavage of N-acetylmuramyl-L-alanine bonds in dimeric cross-bridges that interlink the two murein strands in the peptidoglycan
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
-
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diamino [3,4,5-3H]pimelic acid (3H-MTP)
-
-
?
peptidoglucan + H2O
?
ChwA primarily hydrolyzes the N-acetylmuramoyl-L-alanyl amide bond, splits the linkage between polysaccharides and peptides, bacteriolytic/cell wall hydrolytic amidase, CwhA lyses CHCl3-treated Escherichia coli JM109 most efficiently, followed by Micrococcus luteus, Staphylococcus aureus IFO 13276, Enterococcus faecalis IFO 3971, Pediococcus acidilactici IFO3385 and intact Escherichia coli JM109
-
-
?
peptidoglucan + H2O
?
PGRP-L hydrolyzes the amide bond between MurNAc and L-Ala of peptidoglycan, Cys-419 is required for the amidase activity, polymeric soluble uncross-linked peptidoglycan from Staphylococcus aureus, digest products
-
-
?
peptidoglucan + H2O
?
cell autolysis, LytA rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone, LytA is an important pneumococcal virulence factor
-
-
?
peptidoglucan + H2O
?
LytA structure, 36.6 kDa modular enzyme comprising an N-terminal catalytic domain plus the C-terminal choline-binding domain, the former catalyzes the hydrolysis of the N-acetylmuramoyl-L-alanine bond present in the pneumococcal peptidoglycan backbone, fundamental role of the 11 C-terminal residues in the catalytic activity of LytA
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
peptidoglycan + H2O
?
Bacillus cereus phage BPS13
-
-
-
-
?
peptidoglycan + H2O
?
-
enzyme is required for the recognition of peptidoglycan, a component of bacterial cell walls, and therefore critical for the immune response
-
-
?
peptidoglycan + H2O
?
-
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
peptidoglycan + H2O
?
-
the enzyme can act on macromolecular peptidoglycan to liberate cross-linked and non-cross-linked peptides
-
-
?
peptidoglycan + H2O
?
-
the enzyme can act on macromolecular peptidoglycan to liberate cross-linked and non-cross-linked peptides
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
peptidoglycan + H2O
peptidoglycan-derived fragment peptides
-
enzyme AmiC displays high basal activity on peptidoglycan. In vivo assay of HA-tagged recombinant enzyme in Escherichia coli cells, usage of fluorescein-labeled peptidoglycan. Digesting gonococcal PG with AmiC results in the recovery of soluble fragments of predicted masses matching tripeptide stem (L-Ala-gamma-D-Glu-mDAP), tetrapeptide stem (L-Ala-gamma-D-Glu-mDAP-D-Ala), pentapeptide stem (L-Ala-gamma-D-Glu-mDAPD-Ala-D-Ala), cross-linked tetrapeptide-tripeptide (4-3), crosslinked tetrapeptide-tetrapeptide (4-4), and cross-linked tetrapeptide-tetrapeptide-tetrapeptide (4-4-4). Substrate specificity of wild-type and mutant enzymes and product release analysis, detailed overview
-
-
ir
peptidoglycan + H2O
peptidoglycan-derived fragment peptides
-
enzyme AmiC displays high basal activity on peptidoglycan. In vivo assay of HA-tagged recombinant enzyme in Escherichia coli cells, usage of fluorescein-labeled peptidoglycan. Digesting gonococcal PG with AmiC results in the recovery of soluble fragments of predicted masses matching tripeptide stem (L-Ala-gamma-D-Glu-mDAP), tetrapeptide stem (L-Ala-gamma-D-Glu-mDAP-D-Ala), pentapeptide stem (L-Ala-gamma-D-Glu-mDAPD-Ala-D-Ala), cross-linked tetrapeptide-tripeptide (4-3), crosslinked tetrapeptide-tetrapeptide (4-4), and cross-linked tetrapeptide-tetrapeptide-tetrapeptide (4-4-4). Substrate specificity of wild-type and mutant enzymes and product release analysis, detailed overview
-
-
ir
additional information
?
-
bacteriolytic/cell wall hydrolytic amidase
-
-
?
additional information
?
-
-
bacteriolytic/cell wall hydrolytic amidase
-
-
?
additional information
?
-
A0A1J9W3F9
recombinant enzyme CwlJ1 shows activity against the spore cortical fragments of Bacillus anthracis when added exogenously. CwlJ1 is active on both decoated spores and spore cortical fragments. The Bacillus spore cortex is composed of a thick layer of peptidoglycan (PG) containing alternating beta-1,4 linked N-acetylglucosamine (NAG), N-acetylmuramic acid (NAM), and muramic acid-delta-lactam (MAL) residues, with NAM residues attached to either tetrapeptide (TP) or a single L-Ala residue
-
-
?
additional information
?
-
-
recombinant enzyme CwlJ1 shows activity against the spore cortical fragments of Bacillus anthracis when added exogenously. CwlJ1 is active on both decoated spores and spore cortical fragments. The Bacillus spore cortex is composed of a thick layer of peptidoglycan (PG) containing alternating beta-1,4 linked N-acetylglucosamine (NAG), N-acetylmuramic acid (NAM), and muramic acid-delta-lactam (MAL) residues, with NAM residues attached to either tetrapeptide (TP) or a single L-Ala residue
-
-
?
additional information
?
-
A0A1J9W3F9
CwlJ1 mainly recognizes large segments of glycan chains in the cortex instead of the minimal structural unit tetrasaccharide, with specificity for muramic acid-delta-lactam-containing glycan chains and preference for the tetrapeptide side chain. The enzyme cleaves Bacillus anthracis spore cortex peptidoglycan, structure, and specificity of CwlJ1 on spore core fragements, overview. Mass spectrometry analysis of muropeptides released from digested spore cortical fragments
-
-
?
additional information
?
-
-
CwlJ1 mainly recognizes large segments of glycan chains in the cortex instead of the minimal structural unit tetrasaccharide, with specificity for muramic acid-delta-lactam-containing glycan chains and preference for the tetrapeptide side chain. The enzyme cleaves Bacillus anthracis spore cortex peptidoglycan, structure, and specificity of CwlJ1 on spore core fragements, overview. Mass spectrometry analysis of muropeptides released from digested spore cortical fragments
-
-
?
additional information
?
-
the enzyme shows very high lytic activity against Bacillus anthracis strain Sterne and Bacillus thuringiensis strain 97-27 isolates. More than 90% of the Bacillus anthracis cells are lysed by 1 nM protein and 99% are lysed by 50 nM protein in 60 min. Exposure to 10 nM for 10 min results in significantly less than 1% survival
-
-
?
additional information
?
-
the enzyme shows very high lytic activity against Bacillus anthracis strain Sterne and Bacillus thuringiensis strain 97-27 isolates. More than 90% of the Bacillus anthracis cells are lysed by 1 nM protein and 99% are lysed by 50 nM protein in 60 min. Exposure to 10 nM for 10 min results in significantly less than 1% survival
-
-
?
additional information
?
-
-
the enzyme shows very high lytic activity against Bacillus anthracis strain Sterne and Bacillus thuringiensis strain 97-27 isolates. More than 90% of the Bacillus anthracis cells are lysed by 1 nM protein and 99% are lysed by 50 nM protein in 60 min. Exposure to 10 nM for 10 min results in significantly less than 1% survival
-
-
?
additional information
?
-
-
AmiE hydrolyzes the N-acetylmuramoyl-L-Ala bond of N-acetylmuramic acid peptides releasing N-acetylglucosamine, N-acetylmuramic acid, and peptides, but does not hydrolyze this bond of muropeptides containing N-acetylglucosamine at the nonreducing end
-
-
?
additional information
?
-
-
AmiE hydrolyzes the N-acetylmuramoyl-L-Ala bond of N-acetylmuramic acid peptides releasing N-acetylglucosamine, N-acetylmuramic acid, and peptides, but does not hydrolyze this bond of muropeptides containing N-acetylglucosamine at the nonreducing end
-
-
?
additional information
?
-
-
determination of the sites of Bacillus thuringiensis cell wall cleavage by the enzyme, overview
-
-
?
additional information
?
-
-
the recombinant enzyme shows cell wall binding ability and amidase activity in vitro
-
-
?
additional information
?
-
-
recombinant His-tagged CwlC proteins purified from Escherichia coli were able to directly bind to and digest the Bacillus thuringiensis cell wall
-
-
?
additional information
?
-
-
recombinant His-tagged CwlC proteins purified from Escherichia coli were able to directly bind to and digest the Bacillus thuringiensis cell wall
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additional information
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determination of the sites of Bacillus thuringiensis cell wall cleavage by the enzyme, overview
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additional information
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the recombinant enzyme shows cell wall binding ability and amidase activity in vitro
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additional information
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the enzyme hydrolyses an Escherichia coli peptidoglycan
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additional information
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in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC
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additional information
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enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan
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additional information
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in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC
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additional information
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enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan
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additional information
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in Caulobacter crescentus cell division protein FtsN interacts with both endopeptidase DipM and N-acetylmuramoyl-L-alanine amidase AmiC
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additional information
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enzyme AmiC is active with peptidoglycan prepared from Caulobacter crescentus CB15N cells, assay is performed with RBB-labeled peptidoglycan
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additional information
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AmpD is involved in both peptidoglycan recycling and beta-lactamase induction
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additional information
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not: L-Ala-p-nitroanilide, D-Ala-p-nitroanilide, Gly-p-nitroanilide
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additional information
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the recombinant enzyme shows lytic activity against Clostridium perfringens cells
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additional information
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the enzyme performs cell wall lysis, and shows antibacterial activity against Bacillus megaterium
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additional information
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the enzyme does not show antibacterial activity
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additional information
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additional information
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the enzyme has no activity on MurNAc-L-Ala-D-Glu
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additional information
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the enzyme has no activity on MurNAc-L-Ala-D-Glu
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additional information
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additional information
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PGRP-L has no direct bacteriolytic activity for intact bacteria, not: MurNAc-L-Ala-D-isoGln, GlcNAc-MurNAc-L-Ala-D-isoGln
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additional information
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PGRP-L has no direct bacteriolytic activity for intact bacteria, not: MurNAc-L-Ala-D-isoGln, GlcNAc-MurNAc-L-Ala-D-isoGln
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additional information
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no activity on polymerized peptidoglycan
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additional information
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no activity on polymerized peptidoglycan
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additional information
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no activity on polymerized peptidoglycan
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additional information
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the enzyme performs cell wall lysis as peptidoglycan-degrading amidase, but can also promote autolysis in Neisseria gonorrhoeae, other enzymes are also involved in autolysis
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additional information
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enzyme AmiC displays high basal activity on peptidoglycan. Gonococcal AmiC (GC-AmiC) activity on whole GC sacculi, solubilization of whole gonococcal sacculi
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additional information
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enzyme AmiC displays high basal activity on peptidoglycan. Gonococcal AmiC (GC-AmiC) activity on whole GC sacculi, solubilization of whole gonococcal sacculi
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additional information
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the enzyme cleaves the amide linkage between the stem peptides and the lactyl moiety of muramoyl residues in bacterial cell wall heteropolymer peptidoglycan
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additional information
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the enzyme hydrolyzes Escherichia coli peptidoglycan. N-acetylmuramoyl-L-alanine amidases primarily hydrolyzes the amide between the MurNAc and L-alanine residue, releasing the glycan strand from the stem peptide
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additional information
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the enzyme hydrolyzes Escherichia coli peptidoglycan. N-acetylmuramoyl-L-alanine amidases primarily hydrolyzes the amide between the MurNAc and L-alanine residue, releasing the glycan strand from the stem peptide
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additional information
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the enzyme hydrolyzes Escherichia coli peptidoglycan. N-acetylmuramoyl-L-alanine amidases primarily hydrolyzes the amide between the MurNAc and L-alanine residue, releasing the glycan strand from the stem peptide
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additional information
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the enzyme performs cell wall lysis and is important in cell separation of Staphylococcus aureus
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additional information
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the activity of recombinant C-terminal and N-terminal enzyme fragments towards cell wall peptidoglycans is analyzed by MALDI-TOF MS
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additional information
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AtlE is involved in the initial attachment of the cells to polymer surfaces and thus in biofilm formation
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additional information
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AtlE is a multifunctional, surface-associated protein having both enzymic, 60 kDa amidase and 52 kDa glucosaminidase, and adhesive functions, AtlE binds to vitronectin
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additional information
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cell walls are treated with enzyme PlyGRCS, revealing that the catalytic activity is an amidase or endopeptidase, PlyGRCS spectrum of lytic activity, overview. The enzyme shows N-acetylmuramoyl-L-alanine amidase activity
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs lysis of pneumococcal, choline-containing cell walls
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs cell wall lysis
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additional information
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the enzyme performs lysis of pneumococcal, choline-containing cell walls
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additional information
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N-acetylmuramoyl-L-alanine amidase LytA shows the greatest efficiency in disintegrating Streptococcus pneumoniae biofilms. Biofilms formed by Streptococcus pseudopneumoniae and Streptococcus oralis are not destroyed by the Streptococcus pneumoniae autolysin LytA
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additional information
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N-acetylmuramoyl-L-alanine amidase LytA shows the greatest efficiency in disintegrating Streptococcus pneumoniae biofilms. Biofilms formed by Streptococcus pseudopneumoniae and Streptococcus oralis are not destroyed by the Streptococcus pneumoniae autolysin LytA
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additional information
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additional information
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N-acetylmuramoyl-L-alanine amidase activity is measured according to the protocol described previously. This method is based on the degradation of free muramic acid resulting from cleavage of the amide bond in the peptidoglycan to lactic acid followed by degradation of the latter to acetaldehyde which can be determined colorimetrically with 4-phenylphenol. Spectrophotometric measurements
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Bacterial Infections
Biochemical and biophysical characterization of PlyGRCS, a bacteriophage endolysin active against methicillin-resistant Staphylococcus aureus.
Bacterial Infections
Differential expression of peptidoglycan recognition protein 2 in the skin and liver requires different transcription factors.
Bacterial Infections
[Cloning of T7 lysozyme gene and construction of the vector for transgenic plants resistant to bacterial infection]
Carcinoma, Hepatocellular
Tumor-Derived PGLYRP2 Predicts Survival and Antitumor Immune Responses in Hepatocellular Carcinoma.
Cardiovascular Diseases
PGLYRP2 as a novel biomarker for the activity and lipid metabolism of systemic lupus erythematosus.
Cholera
Endopeptidase Regulation as a Novel Function of the Zur-Dependent Zinc Starvation Response.
Colitis
Peptidoglycan recognition protein 3 and Nod2 synergistically protect mice from dextran sodium sulfate-induced colitis.
Colitis
Role of mouse peptidoglycan recognition protein PGLYRP2 in the innate immune response to Salmonella enterica serovar Typhimurium infection in vivo.
Colorectal Neoplasms
CLytA-DAAO Chimeric Enzyme Bound to Magnetic Nanoparticles. A New Therapeutical Approach for Cancer Patients?
Dyslipidemias
PGLYRP2 as a novel biomarker for the activity and lipid metabolism of systemic lupus erythematosus.
Endophthalmitis
Intravitreal injection of the chimeric phage endolysin Ply187 protects mice from Staphylococcus aureus endophthalmitis.
Erythema
Measurement of Organ-Specific and Acute-Phase Blood Protein Levels in Early Lyme Disease.
Foodborne Diseases
Endolysin LysSA97 is synergistic with carvacrol in controlling Staphylococcus aureus in foods.
Glioblastoma
CLytA-DAAO Chimeric Enzyme Bound to Magnetic Nanoparticles. A New Therapeutical Approach for Cancer Patients?
Hepatitis C
Genome-wide transcriptome analysis identifies novel gene signatures implicated in human chronic liver disease.
Hypersensitivity
Specificity in transcriptional regulation in the absence of specific DNA binding sites: the case of T7 lysozyme.
Infections
A mutation in the yeast mitochondrial core RNA polymerase, Rpo41, confers defects in both specificity factor interaction and promoter utilization.
Infections
A novel STK1-targeted small-molecule as an "antibiotic resistance breaker" against multidrug-resistant Staphylococcus aureus.
Infections
A Peptidoglycan Amidase Activator Impacts Salmonella enterica Serovar Typhimurium Gut Infection.
Infections
Antibacterial properties of a pre-formulated recombinant phage endolysin, SAL-1.
Infections
Chemotherapeutic Strategies for Combating Staphylococcus aureus Infections.
Infections
Cloning, mRNA expression, and recombinant expression of peptidoglycan recognition protein II gene from large yellow croaker (Pseudosciaena crocea).
Infections
Comparative secretome investigation of Magnaporthe oryzae proteins responsive to nitrogen starvation.
Infections
Drosophila melanogaster mounts a unique immune response to the Rhabdovirus sigma virus.
Infections
Effects of Phage Endolysin SAL200 Combined with Antibiotics on Staphylococcus aureus Infection.
Infections
Evolution, purification, and characterization of RC0497: a peptidoglycan amidase from the prototypical spotted fever species Rickettsia conorii.
Infections
Evolutionary robustness of an optimal phenotype: re-evolution of lysis in a bacteriophage deleted for its lysin gene.
Infections
Interactions Between Atopic Dermatitis and Staphylococcus aureus Infection: Clinical Implications.
Infections
Multiple roles of T7 RNA polymerase and T7 lysozyme during bacteriophage T7 infection.
Infections
Peptidoglycan Recognition Protein 2 Regulates Neutrophil Recruitment Into the Lungs After Streptococcus pneumoniae Infection.
Infections
Quantitative Proteomics of the Endothelial Secretome Identifies RC0497 as Diagnostic of Acute Rickettsial Spotted Fever Infections.
Infections
Role of mouse peptidoglycan recognition protein PGLYRP2 in the innate immune response to Salmonella enterica serovar Typhimurium infection in vivo.
Infections
Studies on the role of bacteriophage T7 lysozyme during phage infection.
Infections
The depression of endolysin synthesis in bacteria infected with high multiplicities of phage lambda.
Infections
The Efficacy of Intranasal Administration of the Recombinant Endolysin, SAL200, in a Lethal Murine Staphylococcus aureus Pneumonia Model.
Infections
The germination-specific lytic enzymes SleB, CwlJ1, and CwlJ2 each contribute to Bacillus anthracis spore germination and virulence.
Leukemia, Myeloid, Acute
Expression and intracellular localization of the human N-acetylmuramyl-L-alanine amidase, a bacterial cell wall-degrading enzyme.
Leukemia-Lymphoma, Adult T-Cell
Characterization of AtlL, a bifunctional autolysin of Staphylococcus lugdunensis with N-acetylglucosaminidase and N-acetylmuramoyl-l-alanine amidase activities.
Lupus Erythematosus, Systemic
PGLYRP2 as a novel biomarker for the activity and lipid metabolism of systemic lupus erythematosus.
Lyme Disease
Transcription and genetic analyses of a putative N-acetylmuramyl-L-alanine amidase in Borrelia burgdorferi.
Meningitis, Bacterial
Differences in N-acetylmuramyl-L-alanine amidase and lysozyme in serum and cerebrospinal fluid of patients with bacterial meningitis.
Neoplasms
Tumor-Derived PGLYRP2 Predicts Survival and Antitumor Immune Responses in Hepatocellular Carcinoma.
Persistent Infection
Peptidoglycan Hydrolases RipA and Ami1 Are Critical for Replication and Persistence of Mycobacterium tuberculosis in the Host.
Pneumococcal Infections
Peptidoglycan Recognition Protein 2 Regulates Neutrophil Recruitment Into the Lungs After Streptococcus pneumoniae Infection.
Rickettsia Infections
Quantitative Proteomics of the Endothelial Secretome Identifies RC0497 as Diagnostic of Acute Rickettsial Spotted Fever Infections.
Sepsis
Proteomic profiling identifies N-acetylmuramoyl-l-alanine amidase as a novel biomarker of sepsis.
Spotted Fever Group Rickettsiosis
Evolution, purification, and characterization of RC0497: a peptidoglycan amidase from the prototypical spotted fever species Rickettsia conorii.
Spotted Fever Group Rickettsiosis
Quantitative Proteomics of the Endothelial Secretome Identifies RC0497 as Diagnostic of Acute Rickettsial Spotted Fever Infections.
Staphylococcal Food Poisoning
Characteristics for phage-encoded cell wall hydrolase of LysSAP27 to reduce staphylococcal food poisoning.
Staphylococcal Infections
Antibacterial properties of a pre-formulated recombinant phage endolysin, SAL-1.
Staphylococcal Infections
Effects of Phage Endolysin SAL200 Combined with Antibiotics on Staphylococcus aureus Infection.
Staphylococcal Infections
Pharmacokinetics and Tolerance of the Phage Endolysin-Based Candidate Drug SAL200 after a Single Intravenous Administration among Healthy Volunteers.
Staphylococcal Infections
The Efficacy of Intranasal Administration of the Recombinant Endolysin, SAL200, in a Lethal Murine Staphylococcus aureus Pneumonia Model.
Starvation
Endopeptidase Regulation as a Novel Function of the Zur-Dependent Zinc Starvation Response.
Starvation
Expressions of alkaline phosphatase genes during phosphate starvation are under positive influences of multiple cell wall hydrolase genes in Bacillus subtilis.
Starvation
Investigation of antibacterial mechanism and identification of bacterial protein targets mediated by antibacterial medicinal plant extracts.
Tuberculosis
Effect of Mycobacterium tuberculosis Rv3717 on cell division and cell adhesion.
Tuberculosis
Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase.
Tuberculosis
Mycobacterium tuberculosis Rv3717 enhances the survival of Mycolicibacterium smegmatis by inhibiting host innate immune and caspase-dependent apoptosis.
Tuberculosis
Structural and biochemical analyses of Mycobacterium tuberculosis N-acetylmuramyl L-alanine amidase Rv3717 point to a role in peptidoglycan fragment recycling.
Tuberculosis
The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis.
Tuberculosis, Multidrug-Resistant
Serum sCD14, PGLYRP2 and FGA as potential biomarkers for multidrug-resistant tuberculosis based on data-independent acquisition and targeted proteomics.
Typhus, Epidemic Louse-Borne
Quantitative Proteomics of the Endothelial Secretome Identifies RC0497 as Diagnostic of Acute Rickettsial Spotted Fever Infections.
Vaginosis, Bacterial
Engineered Phage Endolysin Eliminates Gardnerella Biofilm without Damaging Beneficial Bacteria in Bacterial Vaginosis Ex Vivo.
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evolution
the enzyme belongs to the Pfam family Amidase_3, the mode of substrate binding is likely shared by the Amidase_3 family proteins
evolution
Ami1 belongs to the amidase_3 domain family
evolution
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AmiC and AmiA structure comparisons. Neisseria gonorrhoeae has only one cell separation amidase (AmiC) in contrast to other baceria, e.g. Escherichia coli
evolution
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peptidoglycan recognition proteins (PGRPs) are a family of pattern recognition receptors that recognize peptidoglycans and modulate innate immune responses. Some PGRPs retain N-acetylmuramoyl-L-alanine amidase activity to hydrolyse bacterial peptidoglycans
evolution
the enzyme's the C-terminus does not display homology to any identifiable domain
evolution
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three main cell wall lytic enzymes, CwlB (also named LytC), CwlC, and CwlH, are identified in Bacillus subtilis. CwlB is the major vegetative autolysin produced at the end of exponential growth phase, and it is also present during sporulation. CwlC and CwlH are sporulation-specific autolysins whose production is Sigma K-dependent
evolution
two proteins, namely RC0497 and RC1358, belong to the AmpD superfamily containing an amidase_2 domain as defined in the Pfam database (PF01510) and potentially endowed with amidase activity, phylogenetic analysis. The PG_binding_1 domain is present only in RC0497 at the C-terminus, but missing in RC1358
evolution
-
Ami1 belongs to the amidase_3 domain family
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evolution
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the enzyme belongs to the Pfam family Amidase_3, the mode of substrate binding is likely shared by the Amidase_3 family proteins
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evolution
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three main cell wall lytic enzymes, CwlB (also named LytC), CwlC, and CwlH, are identified in Bacillus subtilis. CwlB is the major vegetative autolysin produced at the end of exponential growth phase, and it is also present during sporulation. CwlC and CwlH are sporulation-specific autolysins whose production is Sigma K-dependent
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evolution
-
Ami1 belongs to the amidase_3 domain family
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evolution
-
two proteins, namely RC0497 and RC1358, belong to the AmpD superfamily containing an amidase_2 domain as defined in the Pfam database (PF01510) and potentially endowed with amidase activity, phylogenetic analysis. The PG_binding_1 domain is present only in RC0497 at the C-terminus, but missing in RC1358
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malfunction
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vancomycin tolerance in clinical and laboratory Streptococcus pneumoniae isolates depends on reduced enzyme activity of the major LytA autolysin
malfunction
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mutation of gene cwlB delays spore release compared to the timing of spore release in the wild-type strain
malfunction
analysis of peptidoglycan (PG) muropeptide composition and glycan chain length distribution of wild-type strain 26695 and its amiA mutant: the analysis shows that Helicobacter pylori lacks muropeptides with a degree of cross-linking higher than dimeric muropeptides. The amiA mutant is also characterized by a decrease of muropeptides carrying 1,6-anhydro-N-acetylmuramic acid residues, which represent the ends of the glycan chains. This correlated with an increase of very long glycan strands in the amiA mutant. Modifications in PG composition of amiA mutant, overview. The susceptibility of the cells to different antibiotics is unaltered in the amiA mutant cells compared to wild-type cells
malfunction
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CwlC point mutations at the two conserved catalytic glutamic acid residues, Glu24 and Glu140, result in a complete loss of cell wall lytic activity. The CwlC protein consists of an N-terminal N-acetylmuramoyl-L-alanine amidase (MurNAc-LAA) domain and a C-terminal amidase02 domain. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis
malfunction
-
deletion of amiC from Neisseria gonorrhoeae results in severely impaired cell separation and altered peptidoglycan (PG) fragment release. Mutation Q316K results in an AmiC with increased enzymatic activity on macromolecular PG and on the synthetic PG derivative. Mutation Q316K also results in cell separation and PG fragment release defects
malfunction
-
deletion of amiC from Neisseria gonorrhoeae results in severely impaired cell separation and altered peptidoglycan fragment release
malfunction
deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cells. These lateral buds result from mislocalization of DivIVA, a major determinant in facilitating polar elongation in mycobacterial cells. Failure of DELTAami1 mutant cells to separate also leads to dysregulation of FtsZ ring bundling. Loss of Ami1 results in defects in septal peptidoglycan turnover with release of excess cell wall material from the septum or newly born cell poles. Signficant accumulation of 3-3 crosslinked muropeptides is observed in the DELTAami1 mutant. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery. Phenotype, detailed overview
malfunction
overexpression of AmiC causes cell separation defects and formation of chains, and overexpression of AmiC in cells inhibited for cell division leads to lysis. Overexpression of amidase leads to morphological aberrations
malfunction
various C-terminally truncated versions of Lytmu1/6 fail to cause lysis, indicating the necessity of the cell wall binding domain (CBD) for full enzyme activity
malfunction
-
overexpression of AmiC causes cell separation defects and formation of chains, and overexpression of AmiC in cells inhibited for cell division leads to lysis. Overexpression of amidase leads to morphological aberrations
-
malfunction
-
overexpression of AmiC causes cell separation defects and formation of chains, and overexpression of AmiC in cells inhibited for cell division leads to lysis. Overexpression of amidase leads to morphological aberrations
-
malfunction
-
deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cells. These lateral buds result from mislocalization of DivIVA, a major determinant in facilitating polar elongation in mycobacterial cells. Failure of DELTAami1 mutant cells to separate also leads to dysregulation of FtsZ ring bundling. Loss of Ami1 results in defects in septal peptidoglycan turnover with release of excess cell wall material from the septum or newly born cell poles. Signficant accumulation of 3-3 crosslinked muropeptides is observed in the DELTAami1 mutant. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery. Phenotype, detailed overview
-
malfunction
-
analysis of peptidoglycan (PG) muropeptide composition and glycan chain length distribution of wild-type strain 26695 and its amiA mutant: the analysis shows that Helicobacter pylori lacks muropeptides with a degree of cross-linking higher than dimeric muropeptides. The amiA mutant is also characterized by a decrease of muropeptides carrying 1,6-anhydro-N-acetylmuramic acid residues, which represent the ends of the glycan chains. This correlated with an increase of very long glycan strands in the amiA mutant. Modifications in PG composition of amiA mutant, overview. The susceptibility of the cells to different antibiotics is unaltered in the amiA mutant cells compared to wild-type cells
-
malfunction
-
CwlC point mutations at the two conserved catalytic glutamic acid residues, Glu24 and Glu140, result in a complete loss of cell wall lytic activity. The CwlC protein consists of an N-terminal N-acetylmuramoyl-L-alanine amidase (MurNAc-LAA) domain and a C-terminal amidase02 domain. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis
-
malfunction
-
mutation of gene cwlB delays spore release compared to the timing of spore release in the wild-type strain
-
malfunction
-
deletion of amiC from Neisseria gonorrhoeae results in severely impaired cell separation and altered peptidoglycan (PG) fragment release. Mutation Q316K results in an AmiC with increased enzymatic activity on macromolecular PG and on the synthetic PG derivative. Mutation Q316K also results in cell separation and PG fragment release defects
-
malfunction
-
deletion of amiC from Neisseria gonorrhoeae results in severely impaired cell separation and altered peptidoglycan fragment release
-
malfunction
-
analysis of peptidoglycan (PG) muropeptide composition and glycan chain length distribution of wild-type strain 26695 and its amiA mutant: the analysis shows that Helicobacter pylori lacks muropeptides with a degree of cross-linking higher than dimeric muropeptides. The amiA mutant is also characterized by a decrease of muropeptides carrying 1,6-anhydro-N-acetylmuramic acid residues, which represent the ends of the glycan chains. This correlated with an increase of very long glycan strands in the amiA mutant. Modifications in PG composition of amiA mutant, overview. The susceptibility of the cells to different antibiotics is unaltered in the amiA mutant cells compared to wild-type cells
-
malfunction
-
deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cells. These lateral buds result from mislocalization of DivIVA, a major determinant in facilitating polar elongation in mycobacterial cells. Failure of DELTAami1 mutant cells to separate also leads to dysregulation of FtsZ ring bundling. Loss of Ami1 results in defects in septal peptidoglycan turnover with release of excess cell wall material from the septum or newly born cell poles. Signficant accumulation of 3-3 crosslinked muropeptides is observed in the DELTAami1 mutant. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery. Phenotype, detailed overview
-
metabolism
-
AmiE and NagZ in conjunction liberate MurNAc by sequential hydrolysis of muropeptides
metabolism
analysis of regulation of daughter cell separation in Caulobacter crescentus, comparison with Escherichia coli
metabolism
-
gonococcal AmiC can utilize metal ions other than the zinc cofactor typically used by cell separation amidases, potentially protecting its ability to function in zinc-limiting environments. Deletion of amiC results in cells that grow in clusters and have formed septa but fail to separate. This phenotype is similar to that observed in Neisseria gonorrhoeae lacking the lytic transglycosylase LtgC, implying that LtgC may act in concert with AmiC. The amiCE229D mutant releases larger [3H]glucosamine-labeled peptidoglycan fragments, relative to the wild-type, and no disaccharide, overview. Loss of released peptides does not impact NOD-dependent NF-kappaB activation by gonococci
metabolism
higher enzymatic activity of RC0497 in peptidoglycan hydrolysis when compared to lysozyme
metabolism
-
analysis of regulation of daughter cell separation in Caulobacter crescentus, comparison with Escherichia coli
-
metabolism
-
AmiE and NagZ in conjunction liberate MurNAc by sequential hydrolysis of muropeptides
-
metabolism
-
analysis of regulation of daughter cell separation in Caulobacter crescentus, comparison with Escherichia coli
-
metabolism
-
gonococcal AmiC can utilize metal ions other than the zinc cofactor typically used by cell separation amidases, potentially protecting its ability to function in zinc-limiting environments. Deletion of amiC results in cells that grow in clusters and have formed septa but fail to separate. This phenotype is similar to that observed in Neisseria gonorrhoeae lacking the lytic transglycosylase LtgC, implying that LtgC may act in concert with AmiC. The amiCE229D mutant releases larger [3H]glucosamine-labeled peptidoglycan fragments, relative to the wild-type, and no disaccharide, overview. Loss of released peptides does not impact NOD-dependent NF-kappaB activation by gonococci
-
metabolism
-
higher enzymatic activity of RC0497 in peptidoglycan hydrolysis when compared to lysozyme
-
physiological function
-
LytA is associated with the bactericidal activity of quinolones
physiological function
-
under normal conditions, activation of bacterial LytA, together with the phage lysin, leads to greater phage progeny release. In the absence of phage lysin, LytA is able to mediate bacterial lysis and phage release in Streptococcus pneumoniae
physiological function
-
endolysin LysBPS13 demonstrates high lytic activity against Bacillus cereus
physiological function
-
LytN secretion into the cross-wall promotes peptidoglycan separation and completion of the staphylococcal cell cycle. LytN is required for proper staphylococcal growth. Overexpression of LytN triggers lysis of the staphylococcal cross-wall
physiological function
potential role for enzyme Rv3717 in peptidoglycan fragment recycling
physiological function
the amidase PlyCpAmi can kill stationary phase cells even though they may have a higher resistance to stress. The enzyme hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides
physiological function
-
the enzyme is involved in mother cell lysis, determination of the sites of cell wall cleavage by the enzyme, overview
physiological function
enzyme AmiC has septum splitting activity and can perform septal peptidoglycan splitting, it probably plays a role in cell separation. The enzymatic activity is essential for medial recruitment of AmiC, the amidase-3 family catalytic domain of AmiC is essential for medial localization. AmiC is a late cell division protein, overview
physiological function
-
enzyme AmiC is critical for proper cell separation, is necessary for normal peptidoglycan (PG) fragment release, and functions as an autolysin. The amidase activity of AmiC controls cell separation and stem peptide release and is enhanced by NlpD in Neisseria gonorrhoeae. The activation state is not the only factor determining normal AmiC activity
physiological function
enzyme LysSA97 specifically lyses the staphylococcal strains and effectively disrupts staphylococcal biofilms
physiological function
Mycobacteria possess a multi-layered cell wall that requires extensive remodelling during cell division. The amidase_3 domain-containing N-acetylmuramyl-L-alanine amidase is a peptidoglycan remodelling enzyme. The enzyme is required for mycobacterial cell division. Peptidoglycan synthesis is localized to the cell poles and/or septum, a pattern, which is retained upon deletion of ami1
physiological function
phage phiIBB_Pl23 is able to lyse 16 of the 20 strains (80%), its endolysin is active against all Paenibacillus larvae strains tested, but Bacillus and Lactobacillus strains are not lysed by the phage or by the enzyme, overview
physiological function
PlyGVE2CpCWB chimeric mutant effectiveness in lysis against various bacteria, overview
physiological function
RC0497 is a peptidoglycan hydrolase unique to spotted fever rickettsiae. The enzyme may potentially serve as moonlighting protein capable of performing multiple functions during host-pathogen interactions. RC0497 encoding the enzyme is highly expressed at the levels of both transcription and translation during Rickettsia conorii infection of cultured human microvascular endothelial cells (HMECs). Possibly RC0497 acts in association with RC1358 and AmpG aids in the breakdown of peptidoglycan (PG) fragments in the periplasm and their recycling to prevent activation of host immune responses. RC0497 may also interact with host components/proteins and play roles in facilitating the re-entry and spread of spotted fever group (SFG) rickettsiae during infection
physiological function
-
short peptidoglycan recognition protein 4 (PGRP-S4) can activate prophenoloxidase (proPO). In haemolymph, it may hydrolyse peptidoglycan to kill bacteria and enhance proPO activation. The recombinant enzyme PGRP-S4 binds bacteria and different peptidoglycans. In addition, it inhibits bacterial growth of Bacillus subtilis, not of Escherichia coli, Staphylococcus aureus, and Serratia marcescens, and hydrolyses an Escherichia coli peptidoglycan in the presence of Zn2+
physiological function
-
the cell wall hydrolase CwlC from Bacillus thuringiensis is essential for mother cell lysis. CwlC is an essential cell wall hydrolase for Bacillus thuringiensis mother cell lysis during sporulation
physiological function
A0A1J9W3F9
the germination enzyme CwlJ1 plays an important role in degrading the cortex during the germination of Bacillus anthracis spores. CwlJ1 is active on both decoated spores and spore cortical fragments. Once the cortex is degraded, Ca-DPA in the spore core is released and the core becomes hydrated, leading to spore germination. The cortex contains mainly glycans, while the coat is composed of highly crosslinked proteins
physiological function
-
the periplasmic N-acetylmuramyl-L-alanine amidase, AmiC, is involved in cell separation
physiological function
the two N-acetylmuramoyl-L-alanine amidases from two bacteriophages, PhiCP26F and PhiCP39O, are identical in the C-terminal cell-wall binding domain, but have only 55% identity to each other in the N-terminal catalytic domain. Both endolysins, PlyCP26F and PlyCP39O, lyse their parental phage host strains of Clostridium perfringens as well as other strains of the bacterium when exposed externally, but do not lyse bacteria beyond the species
physiological function
the two N-acetylmuramoyl-L-alanine amidases from two bacteriophages, PhiCP26F and PhiCP39O, are identical in the C-terminal cell-wall binding domain, but have only 55% identity to each other in the N-terminal catalytic domain. Both endolysins, PlyCP26F and PlyCP39O, lyse their parental phage host strains of Clostridium perfringens as well as other strains of the bacterium when exposed externally, but do not lyse bacteria beyond the species. PlyGVE2CpCWB chimeric mutant effectiveness in lysis against various bacteria, overview
physiological function
to orchestrate a complex life style in changing environments, the filamentous cyanobacterium Nostoc punctiforme facilitates communication between neighboring cells through septal junction complexes. This is achieved by nanopores that perforate the peptidoglycan (PGN) layer and traverse the cell septa. The N-acetylmuramoyl-L-alanine amidase AmiC2 (Npun_F1846) in Nostoc punctiforme generates arrays of such nanopores in the septal PGN, in contrast to homologous amidases that mediate daughter cell separation after cell division in unicellular bacteria
physiological function
-
enzyme AmiC has septum splitting activity and can perform septal peptidoglycan splitting, it probably plays a role in cell separation. The enzymatic activity is essential for medial recruitment of AmiC, the amidase-3 family catalytic domain of AmiC is essential for medial localization. AmiC is a late cell division protein, overview
-
physiological function
Bacillus cereus phage BPS13
-
endolysin LysBPS13 demonstrates high lytic activity against Bacillus cereus
-
physiological function
-
enzyme AmiC has septum splitting activity and can perform septal peptidoglycan splitting, it probably plays a role in cell separation. The enzymatic activity is essential for medial recruitment of AmiC, the amidase-3 family catalytic domain of AmiC is essential for medial localization. AmiC is a late cell division protein, overview
-
physiological function
-
to orchestrate a complex life style in changing environments, the filamentous cyanobacterium Nostoc punctiforme facilitates communication between neighboring cells through septal junction complexes. This is achieved by nanopores that perforate the peptidoglycan (PGN) layer and traverse the cell septa. The N-acetylmuramoyl-L-alanine amidase AmiC2 (Npun_F1846) in Nostoc punctiforme generates arrays of such nanopores in the septal PGN, in contrast to homologous amidases that mediate daughter cell separation after cell division in unicellular bacteria
-
physiological function
-
Mycobacteria possess a multi-layered cell wall that requires extensive remodelling during cell division. The amidase_3 domain-containing N-acetylmuramyl-L-alanine amidase is a peptidoglycan remodelling enzyme. The enzyme is required for mycobacterial cell division. Peptidoglycan synthesis is localized to the cell poles and/or septum, a pattern, which is retained upon deletion of ami1
-
physiological function
-
potential role for enzyme Rv3717 in peptidoglycan fragment recycling
-
physiological function
-
the cell wall hydrolase CwlC from Bacillus thuringiensis is essential for mother cell lysis. CwlC is an essential cell wall hydrolase for Bacillus thuringiensis mother cell lysis during sporulation
-
physiological function
-
the enzyme is involved in mother cell lysis, determination of the sites of cell wall cleavage by the enzyme, overview
-
physiological function
-
enzyme AmiC is critical for proper cell separation, is necessary for normal peptidoglycan (PG) fragment release, and functions as an autolysin. The amidase activity of AmiC controls cell separation and stem peptide release and is enhanced by NlpD in Neisseria gonorrhoeae. The activation state is not the only factor determining normal AmiC activity
-
physiological function
-
the periplasmic N-acetylmuramyl-L-alanine amidase, AmiC, is involved in cell separation
-
physiological function
-
Mycobacteria possess a multi-layered cell wall that requires extensive remodelling during cell division. The amidase_3 domain-containing N-acetylmuramyl-L-alanine amidase is a peptidoglycan remodelling enzyme. The enzyme is required for mycobacterial cell division. Peptidoglycan synthesis is localized to the cell poles and/or septum, a pattern, which is retained upon deletion of ami1
-
physiological function
-
RC0497 is a peptidoglycan hydrolase unique to spotted fever rickettsiae. The enzyme may potentially serve as moonlighting protein capable of performing multiple functions during host-pathogen interactions. RC0497 encoding the enzyme is highly expressed at the levels of both transcription and translation during Rickettsia conorii infection of cultured human microvascular endothelial cells (HMECs). Possibly RC0497 acts in association with RC1358 and AmpG aids in the breakdown of peptidoglycan (PG) fragments in the periplasm and their recycling to prevent activation of host immune responses. RC0497 may also interact with host components/proteins and play roles in facilitating the re-entry and spread of spotted fever group (SFG) rickettsiae during infection
-
additional information
the enzyme contains an extra disulfide-bonded beta-hairpin adjacent to the active site compared to other peptidoglycan amidases. Zn2 binding rearranges active site residues and disulfide formation promotes folding of the beta-hairpin. Although Zn2 is required for hydrolysis of muramyl dipeptide, disulfide oxidation is not required for activity on this substrate. The product L-alanine-iso-D-glutamine binds at the head of a closed tunnel. The orientation of the product in the active site suggests a role for a conserved Glu200 in catalysis
additional information
-
the enzyme contains an extra disulfide-bonded beta-hairpin adjacent to the active site compared to other peptidoglycan amidases. Zn2 binding rearranges active site residues and disulfide formation promotes folding of the beta-hairpin. Although Zn2 is required for hydrolysis of muramyl dipeptide, disulfide oxidation is not required for activity on this substrate. The product L-alanine-iso-D-glutamine binds at the head of a closed tunnel. The orientation of the product in the active site suggests a role for a conserved Glu200 in catalysis
additional information
amino acids essential for amidase_3 domain catalytic activity of AmiA in Bacillus anthracis 4229 include H341, E355, H415 and E486
additional information
-
amino acids essential for amidase_3 domain catalytic activity of AmiA in Bacillus anthracis 4229 include H341, E355, H415 and E486
additional information
analysis of peptidoglycan muropeptide composition and glycan chain length distribution, overview
additional information
enzyme PlyGRCS contains an N-terminal catalytic domain with an active site cysteine and histidine
additional information
-
enzyme residue Glu229 is critical for both normal cell separation and the release of peptidoglycan (PG) fragments by gonococci during growth. Residue Gln316 has an autoinhibitory role. AmiC and AmiA structure comparisons. Enzyme residue Glu229 is a critical residue necessary for the enzymatic activity of AmiC
additional information
Lytmu1/6 is neither a muramidase nor a glucosaminidase. The endolysin releases significant amounts of free amino acids from the peptidoglycan. The N-terminal domain is responsible for the catalytic activity of Lytmu1/6. Amino acid residues K27, H31, E109, H176, and D186 are important for catalytic activity, mutational analysis
additional information
N-acetylmuramoyl-L-alanine amidase is constitutively expressed during infection of cultured human microvascular endothelial cells at the levels of both mRNA transcript and encoded protein
additional information
-
N-acetylmuramoyl-L-alanine amidase is constitutively expressed during infection of cultured human microvascular endothelial cells at the levels of both mRNA transcript and encoded protein
additional information
overall structure and active site architecture of the enzyme's catalytic domain, AmiC2-cat, overview. AmiC2-cat adopts a mixed alphabeta-fold that is characteristic for Amidase_3 enzymes. Residues H447, E462, and H515 coordinate a zinc ion and mark the center of the active site. The conserved GHGG motif of residues Gly446, His447, Gly448, and Gly449 after strand beta1 permits two close turns and the tight folding at the top of the active site by the absence of side chains. Residue Glu578 is indispensable for catalysis
additional information
-
overall structure and active site architecture of the enzyme's catalytic domain, AmiC2-cat, overview. AmiC2-cat adopts a mixed alphabeta-fold that is characteristic for Amidase_3 enzymes. Residues H447, E462, and H515 coordinate a zinc ion and mark the center of the active site. The conserved GHGG motif of residues Gly446, His447, Gly448, and Gly449 after strand beta1 permits two close turns and the tight folding at the top of the active site by the absence of side chains. Residue Glu578 is indispensable for catalysis
additional information
the enzyme has an N-acetylmuramoyl-L-alanine amidase catalytic domain and exhibits a broad-spectrum activity against common Paenibacillus larvae genotypes. Identification of five putative amidase catalytic residues: His29, His129, Phe53, Lys135, and Cys137
additional information
the putative cell wall binding domain (CBD) of LysSA97 shows a specific binding spectrum against staphylococcal cells comparable to SH3 domain (PF08460)
additional information
-
the two conserved glutamic acid residues, Glu24 and Glu140, are critical for the catalytic activity, CwlC is an N-acetylmuramoyl-L-alanine amidase
additional information
-
overall structure and active site architecture of the enzyme's catalytic domain, AmiC2-cat, overview. AmiC2-cat adopts a mixed alphabeta-fold that is characteristic for Amidase_3 enzymes. Residues H447, E462, and H515 coordinate a zinc ion and mark the center of the active site. The conserved GHGG motif of residues Gly446, His447, Gly448, and Gly449 after strand beta1 permits two close turns and the tight folding at the top of the active site by the absence of side chains. Residue Glu578 is indispensable for catalysis
-
additional information
-
amino acids essential for amidase_3 domain catalytic activity of AmiA in Bacillus anthracis 4229 include H341, E355, H415 and E486
-
additional information
-
analysis of peptidoglycan muropeptide composition and glycan chain length distribution, overview
-
additional information
-
the enzyme contains an extra disulfide-bonded beta-hairpin adjacent to the active site compared to other peptidoglycan amidases. Zn2 binding rearranges active site residues and disulfide formation promotes folding of the beta-hairpin. Although Zn2 is required for hydrolysis of muramyl dipeptide, disulfide oxidation is not required for activity on this substrate. The product L-alanine-iso-D-glutamine binds at the head of a closed tunnel. The orientation of the product in the active site suggests a role for a conserved Glu200 in catalysis
-
additional information
-
the two conserved glutamic acid residues, Glu24 and Glu140, are critical for the catalytic activity, CwlC is an N-acetylmuramoyl-L-alanine amidase
-
additional information
-
analysis of peptidoglycan muropeptide composition and glycan chain length distribution, overview
-
additional information
-
amino acids essential for amidase_3 domain catalytic activity of AmiA in Bacillus anthracis 4229 include H341, E355, H415 and E486
-
additional information
-
N-acetylmuramoyl-L-alanine amidase is constitutively expressed during infection of cultured human microvascular endothelial cells at the levels of both mRNA transcript and encoded protein
-
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E90A
no bacteriolytic activity
H29N
no bacteriolytic activity
K135A
bacteriolytic activity similar to that of wild-type PlyG
E140A
-
site-directed mutagenesis, catalytically inactive mutant
E24A
-
site-directed mutagenesis, catalytically inactive mutant
E24A/E140A
-
site-directed mutagenesis, catalytically inactive mutant
E140A
-
site-directed mutagenesis, catalytically inactive mutant
-
E24A
-
site-directed mutagenesis, catalytically inactive mutant
-
E24A/E140A
-
site-directed mutagenesis, catalytically inactive mutant
-
E196A
site-directed mutagenesis, active site mutant
H182A
site-directed mutagenesis, inactive active site mutant, quantitative analysis of localization of AmiCH182A during the cell cycle, overview
H250A
site-directed mutagenesis, active site mutant
E196A
-
site-directed mutagenesis, active site mutant
-
H182A
-
site-directed mutagenesis, inactive active site mutant, quantitative analysis of localization of AmiCH182A during the cell cycle, overview
-
H250A
-
site-directed mutagenesis, active site mutant
-
E196A
-
site-directed mutagenesis, active site mutant
-
H182A
-
site-directed mutagenesis, inactive active site mutant, quantitative analysis of localization of AmiCH182A during the cell cycle, overview
-
H250A
-
site-directed mutagenesis, active site mutant
-
D164A
-
inactive mutant with lost ability to bind zinc, kinetics
E116A
-
inactive mutant, residue is not directly involved in catalytic mechanism, but rather in binding of zinc by contributing to the correct orientation of His-34, kinetics
H154A
-
mutation of a zinc ligand residue, kinetics
H154N
-
mutation of a zinc ligand residue, active mutant which can bind zinc, kinetics
H34A
-
inactive mutant with lost ability to bind zinc, kinetics
K162H
-
0.7% of wild-type activity, residue is probably involved in substrate binding, kinetics
K162Q
-
0.2% of wild-type activity, residue is probably involved in substrate binding, kinetics
Y63F
-
16% of wild-type activity, residue is probably involved in substrate binding, kinetics
C168A
site-directed mutagenesis, the mutant is enzymatically inactive but retains its peptidoglycan affinity
C168S
site-directed mutagenesis, the mutant is enzymatically inactive but retains its peptidoglycan affinity
H411A
mutant with full amidase activity
H436A
mutant with full amidase activity
W442A
mutant with reduced amidase activity
C29S
site-directed mutagenesis, catalytically inactive mutant
H92A
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
C116A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
C131A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
D128A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
D148A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
D186A
site-directed mutagenesis, inactive mutant
D186E
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
D21A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
D35A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
D70A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
E109A
site-directed mutagenesis, inactive mutant
E109D
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
E181A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
H176A
site-directed mutagenesis, inactive mutant
H184A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
H31A
site-directed mutagenesis, inactive mutant
H66A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
K27A
site-directed mutagenesis, inactive mutant
K27R
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
K87A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
L52P
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
N99A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
P71A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
Q107A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
Q78A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
R100A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
R97A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
T33A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
W140A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
W167A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
W5A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
E200X
inactive mutant
E200X
-
inactive mutant
-
E229D
-
mutation alters peptidoglycan fragment release and causes a defect in cell separation
E229D
-
site-directed mutagenesis, the mutation leads to reduced enzyme activity and causes a defect in cell separation. The amiCE229D mutant releases larger [3H]glucosamine-labeled peptidoglycan fragments relative to the wild-type and no disaccharide. The amiCE229D mutant does not release some [3H]DAP-labeled peptide fragments, similar to a DELTAamiC strain
Q316K
-
mutation results in an AmiC with increased enzymatic activity on macromolecular peptidoglycan and on the synthetic peptidoglycan derivative GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide). The same mutation also results in cell separation and peptidoglycan fragment release defects
Q316K
-
site-directed mutagenesis, mutation Q316K results in an AmiC with increased enzymatic activity on macromolecular peptidoglycan (PG) and on the synthetic PG derivative. The same Q316K mutation that increases AmiC activity also results in cell separation and PG fragment release defects. But amiCQ316K mutation has only intermediate effects on PG fragment release and causes a slight defect in cell separation. In addition, the mutation amiCQ316K causes increased activity on whole sacculi and lysis of Escherichia coli cells
E229D
-
mutation alters peptidoglycan fragment release and causes a defect in cell separation
-
E229D
-
site-directed mutagenesis, the mutation leads to reduced enzyme activity and causes a defect in cell separation. The amiCE229D mutant releases larger [3H]glucosamine-labeled peptidoglycan fragments relative to the wild-type and no disaccharide. The amiCE229D mutant does not release some [3H]DAP-labeled peptide fragments, similar to a DELTAamiC strain
-
Q316K
-
mutation results in an AmiC with increased enzymatic activity on macromolecular peptidoglycan and on the synthetic peptidoglycan derivative GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide). The same mutation also results in cell separation and peptidoglycan fragment release defects
-
Q316K
-
site-directed mutagenesis, mutation Q316K results in an AmiC with increased enzymatic activity on macromolecular peptidoglycan (PG) and on the synthetic PG derivative. The same Q316K mutation that increases AmiC activity also results in cell separation and PG fragment release defects. But amiCQ316K mutation has only intermediate effects on PG fragment release and causes a slight defect in cell separation. In addition, the mutation amiCQ316K causes increased activity on whole sacculi and lysis of Escherichia coli cells
-
additional information
deletion of the C-terminal region completely abolishes the lytic activity
additional information
-
gene cwlB and upstream gene cwlA form one transcriptional unit, construction of the cwlA, cwlB, and cwlAB deletion mutants and genetic complementation of the cwlB deletion mutant
additional information
-
construction of a deletion by gene replacement in Bacillus thuringiensis strain HD73. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Engineered Bacillus thuringiensis strains targeting cwlC allow the crystal inclusion to remain encapsulated in the mother cell at the end of sporulation. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis
additional information
-
construction of a deletion by gene replacement in Bacillus thuringiensis strain HD73. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Engineered Bacillus thuringiensis strains targeting cwlC allow the crystal inclusion to remain encapsulated in the mother cell at the end of sporulation. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis
-
additional information
-
gene cwlB and upstream gene cwlA form one transcriptional unit, construction of the cwlA, cwlB, and cwlAB deletion mutants and genetic complementation of the cwlB deletion mutant
-
additional information
a thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability, overview. A codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) from Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F which is identical to the PlyCP39O endolysin CWB domain from Clostridium phage phiCP39-O. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures
additional information
a codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) of Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F which is identical to the PlyCP39O endolysin CWB domain. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures
additional information
a thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability, overview. A codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) from Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures
additional information
N-terminal DELTA1-343 deletion mutant of PGRP-L with reduced activity, inactive C-terminal DELTA344-576 deletion mutant of PGRP-L
additional information
-
N-terminal DELTA1-343 deletion mutant of PGRP-L with reduced activity, inactive C-terminal DELTA344-576 deletion mutant of PGRP-L
additional information
construction of deletion mutants DELTA1-322, DELTA323-555, and DELTA474-555
additional information
-
construction of deletion mutants DELTA1-322, DELTA323-555, and DELTA474-555
additional information
generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery
additional information
-
generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery
additional information
-
generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery
-
additional information
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generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery
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additional information
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knockout mutants of amiC show no release of disaccharide units and diminished cell separation, but still undergo autolysis in stationary phase of the organism indicating that not only AmiC is responsible for autolysis, in growth phase the cell lysis rate is increased in the mutant, deletion of amiC increases outer membrane permeability
additional information
construction of enzyme AmiC residues 29-159 fused to GB1, the AmiC-NTD construct contains four beta strands, followed by a single alpha-helix and then a further four beta-strands
additional information
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construction of enzyme AmiC residues 29-159 fused to GB1, the AmiC-NTD construct contains four beta strands, followed by a single alpha-helix and then a further four beta-strands
additional information
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generation of an enzyme deletion mutant DELTAamiC
additional information
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construction of enzyme AmiC residues 29-159 fused to GB1, the AmiC-NTD construct contains four beta strands, followed by a single alpha-helix and then a further four beta-strands
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additional information
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construction of enzyme AmiC residues 29-159 fused to GB1, the AmiC-NTD construct contains four beta strands, followed by a single alpha-helix and then a further four beta-strands
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additional information
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generation of an enzyme deletion mutant DELTAamiC
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additional information
none of the Glu578-variants shows enzyme activity, suggesting that this residue is indispensable for catalysis
additional information
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none of the Glu578-variants shows enzyme activity, suggesting that this residue is indispensable for catalysis
additional information
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none of the Glu578-variants shows enzyme activity, suggesting that this residue is indispensable for catalysis
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additional information
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an insertion mutation of gene sle1 leads to impaired cell separation and induced cluster formation of the cells, the mutant cells are less pathogenic than the wild-type cells in mice, phenotype, overview
additional information
construction of diverse truncation mutants of endolysin. The mutants lacking more than 200 C-terminal amino acids or the cell wall-binding domain are inactive, while N-terminal truncation mutant, or C-terminal truncation mutants lacking less than 200 amino acids still show lytic activity, although less than the wild-type enzyme
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Neisseria gonorrhoeae (Q5F6P7), Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090 (Q5F6P7), Neisseria gonorrhoeae ATCC 700825 (Q5F6P7)
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Wu, X.; Grover, N.; Paskaleva, E.E.; Mundra, R.V.; Page, M.A.; Kane, R.S.; Dordick, J.S.
Characterization of the activity of the spore cortex lytic enzyme CwlJ1
Biotechnol. Bioeng.
112
1365-1375
2015
Bacillus anthracis (A0A1J9W3F9), Bacillus anthracis
brenda
Dubey, A.; Priyadarshini, R.
Amidase activity is essential for medial localization of AmiC in Caulobacter crescentus
Curr. Genet.
64
661-675
2018
Caulobacter vibrioides (A0A0H3C9I3), Caulobacter vibrioides CB15N (A0A0H3C9I3), Caulobacter vibrioides NA1000 (A0A0H3C9I3)
brenda
Farkasovska, J.; Godany, A.
Characterization of the N-terminal catalytic domain of Lytmu1/6, an endolysin from Streptomyces aureofaciens Phage mu1/6
Curr. Microbiol.
73
602-610
2016
Streptomyces phage mu1/6 (Q7Y4H8)
brenda
Buettner, F.M.; Faulhaber, K.; Forchhammer, K.; Maldener, I.; Stehle, T.
Enabling cell-cell communication via nanopore formation structure, function and localization of the unique cell wall amidase AmiC2 of Nostoc punctiforme
FEBS J.
283
1336-1350
2016
Nostoc punctiforme (B2J2S4), Nostoc punctiforme, Nostoc punctiforme ATCC 29133 (B2J2S4)
brenda
Yang, P.J.; Zhan, M.Y.; Ye, C.; Yu, X.Q.; Rao, X.J.
Molecular cloning and characterization of a short peptidoglycan recognition protein from silkworm Bombyx mori
Insect Mol. Biol.
26
665-676
2017
Bombyx mori
brenda
Lenz, J.D.; Stohl, E.A.; Robertson, R.M.; Hackett, K.T.; Fisher, K.; Xiong, K.; Lee, M.; Hesek, D.; Mobashery, S.; Seifert, H.S.; Davies, C.; Dillard, J.P.
Amidase activity of AmiC controls cell separation and stem peptide release and is enhanced by NlpD in Neisseria gonorrhoeae
J. Biol. Chem.
291
10916-10933
2016
Neisseria gonorrhoeae, Neisseria gonorrhoeae MS11
brenda
Chaput, C.; Ecobichon, C.; Pouradier, N.; Rousselle, J.C.; Namane, A.; Boneca, I.G.
Role of the N-acetylmuramoyl-L-alanyl amidase, AmiA, of Helicobacter pylori in peptidoglycan metabolism, daughter cell separation, and virulence
Microb. Drug Resist.
22
477-486
2016
Helicobacter pylori (O25464), Helicobacter pylori ATCC 700392 (O25464), Helicobacter pylori 26695 (O25464)
brenda
Oliveira, A.; Leite, M.; Kluskens, L.D.; Santos, S.B.; Melo, L.D.; Azeredo, J.
The first Paenibacillus larvae bacteriophage endolysin (PlyPl23) with high potential to control american foulbrood
PLoS ONE
10
e0132095
2015
Paenibacillus phage phiIBB_P123 (R9VY83)
brenda
Senzani, S.; Li, D.; Bhaskar, A.; Ealand, C.; Chang, J.; Rimal, B.; Liu, C.; Joon Kim, S.; Dhar, N.; Kana, B.
An Amidase_3 domain-containing N-acetylmuramyl-L-alanine amidase is required for mycobacterial cell division
Sci. Rep.
7
1140
2017
Mycolicibacterium smegmatis (A0R5R2), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0R5R2), Mycolicibacterium smegmatis mc(2)155 (A0R5R2)
brenda
Swift, S.M.; Seal, B.S.; Garrish, J.K.; Oakley, B.B.; Hiett, K.; Yeh, H.Y.; Woolsey, R.; Schegg, K.M.; Line, J.E.; Donovan, D.M.
A thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability
Viruses
7
3019-3034
2015
Geobacillus virus E2 (A6M970), Clostridium phage phiCP39-O (B6CXF7), Clostridium phage phiCP26F (F2VHX9)
brenda