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(GlcNAc-MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala)2 + H2O
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Substrates: -
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1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP + H2O
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP
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Substrates: -
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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
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Substrates: -
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1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
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Substrates: -
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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
Substrates: -
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1,6-anhydromuropeptide + H2O
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Substrates: 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
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4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O
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Substrates: the substrate is likely not turned over in vitro by AmpD
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7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGln-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
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Substrates: -
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7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
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Substrates: -
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bacterial peptidoglycan + H2O
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Substrates: -
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bacterial spore peptidoglycan
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Substrates: -
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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
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Substrates: -
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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
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Substrates: -
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beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
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Substrates: -
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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
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Substrates: -
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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
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Substrates: -
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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
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Substrates: -
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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
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Substrates: -
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beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
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Substrates: -
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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
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Substrates: -
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biotin-peptidoglucan + H2O
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Substrates: -
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GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
Substrates: -
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GlcNAc-anhydroMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
GlcNAc-anhydroMurNAc + L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala
Substrates: biphasic behavior: rapid exponential phase preceding a linear phase (0.027 mM substrate, 0.000106 mM enzyme)
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GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
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GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
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GlcNAc-MurNAc-anhydro-L-Ala-D-gluc-meso-diaminopimelyl-D-Ala + H2O
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Substrates: -
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GlcNAc-MurNAc-L-Ala-D-isoGIn-meso-diaminopimelyl-(D)-amide-(L)-D-Ala-D-Ala + H2O
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Substrates: -
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GlcNAc-MurNAc-L-Ala-D-isoGln-meso-diaminopimelyl-D-Ala + H2O
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Substrates: -
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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
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Substrates: -
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murein + H2O
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Substrates: also murein extracted from cells grown in the presence of penicillin, N-acetylated murein
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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
Substrates: MurNAc-tripeptide, minimum peptidoglycan fragment hydrolyzed by PGRP-L
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MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala + H2O
MurNAc + L-Ala-D-isoGln-L-Lys-D-Ala
Substrates: -
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N-(beta-1,4-N-acetylglucosaminyl-N-acetylmuramoyl-L-alanyl-gamma-D-isoglutaminyl)-L-lysyl-D-alanine + H2O
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Substrates: -
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N-acetyl-glucosaminyl(beta1-4)N-acetylmuramoyl-tetrapeptide + H2O
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Substrates: -
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N-acetyl-glucosaminyl(beta1-4)N-acetylmuramoyl-tripeptide + H2O
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Substrates: -
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N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-tripeptide + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanine + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
N-acetylmuramoyl-L-alanine-gamma-D-glutamyl-mesodiaminopimelic acid + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
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N-acetylmuramoyl-L-alanyl-D-glutamine + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanyl-gamma-D-glutaminyl-meso-diaminopimelic acid + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
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Substrates: -
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peptidoglycan + H2O
peptidoglycan-derived fragment peptides
phospho-N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
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Substrates: -
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uridine diphospho-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid + H2O
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Substrates: -
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additional information
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cell walls
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Substrates: from Bacillus megaterium, Bacillus subtilis
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cell walls
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Substrates: from Bacillus subtilis, [14C] glucosamine-labeled
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cell walls
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Substrates: from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
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cell walls
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Substrates: from Bacillus subtilis
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cell walls
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Substrates: from Bacillus subtilis, [14C] glucosamine-labeled
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cell walls
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Substrates: from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
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cell walls
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Dubowvirus dv11
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Substrates: cell wall anchor structures from staphylococcal surface proteins
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cell walls
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Substrates: from Bacillus lentus
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cell walls
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Substrates: from Micrococcus luteus, Listeria monocytogenes
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cell walls
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Substrates: from Bacillus polymyxa
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cell walls
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Pneumococcal bacteriophage HB-3
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Substrates: pneumococcal cell walls, labeled with [methyl-3H]choline, L-[4,5-3H]lysine monohydrochloride, or [2-14C]ethanolamine
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cell walls
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Substrates: from Bacillus megaterium, Bacillus subtilis
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cell walls
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Substrates: from Micrococcus luteus ATCC 46898
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cell walls
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Substrates: from Micrococcus luteus ATCC 46898
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cell walls
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Substrates: pneumococcal cell walls labeled with [methyl-3H] or [3H]lysine
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cell walls
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Substrates: from Diplococcus pneumoniae
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GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
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Substrates: 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
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GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc + H2O
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Substrates: 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
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GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
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Substrates: small synthetic peptidoglycan fragment
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GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide) + H2O
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Substrates: small synthetic peptidoglycan fragment
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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
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Substrates: -
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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
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Substrates: -
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MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
Substrates: -
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MurNAc-L-Ala-D-isoGln + H2O
N-acetylmuramic acid + L-alanyl-iso-D-glutamine
Substrates: -
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
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Substrates: -
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Bacillus cereus phage BPS13
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Substrates: -
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
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Substrates: -
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
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Substrates: -
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Substrates: 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
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Substrates: 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
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Substrates: 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
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Substrates: -
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
Substrates: the enzyme hydrolyzes bacterial peptidoglycan
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
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Substrates: 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
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N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
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Substrates: -
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N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
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Substrates: N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diamino [3,4,5-3H]pimelic acid (3H-MTP)
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peptidoglucan + H2O
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Substrates: 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
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peptidoglucan + H2O
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Substrates: 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
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peptidoglucan + H2O
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Substrates: cell autolysis, LytA rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone, LytA is an important pneumococcal virulence factor
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peptidoglucan + H2O
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Substrates: 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
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peptidoglycan + H2O
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Substrates: -
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peptidoglycan + H2O
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Bacillus cereus phage BPS13
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Substrates: -
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peptidoglycan + H2O
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Substrates: enzyme is required for the recognition of peptidoglycan, a component of bacterial cell walls, and therefore critical for the immune response
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peptidoglycan + H2O
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Substrates: -
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peptidoglycan + H2O
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Substrates: -
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peptidoglycan + H2O
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Substrates: the enzyme can act on macromolecular peptidoglycan to liberate cross-linked and non-cross-linked peptides
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peptidoglycan + H2O
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Substrates: the enzyme can act on macromolecular peptidoglycan to liberate cross-linked and non-cross-linked peptides
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peptidoglycan + H2O
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Substrates: -
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peptidoglycan + H2O
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Substrates: -
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peptidoglycan + H2O
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Substrates: -
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peptidoglycan + H2O
peptidoglycan-derived fragment peptides
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Substrates: 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
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peptidoglycan + H2O
peptidoglycan-derived fragment peptides
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Substrates: 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
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additional information
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Substrates: bacteriolytic/cell wall hydrolytic amidase
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additional information
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Substrates: bacteriolytic/cell wall hydrolytic amidase
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additional information
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A0A1J9W3F9
Substrates: 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
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additional information
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Substrates: 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
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additional information
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A0A1J9W3F9
Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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