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EC Tree
The taxonomic range for the selected organisms is: Escherichia coli The enzyme appears in selected viruses and cellular organisms
Synonyms
n-acetylmuramoyl-l-alanine amidase, pglyrp2, cell wall hydrolase, t7 lysozyme, n-acetylmuramyl-l-alanine amidase, phage endolysin, namlaa, pgrp-l, cwlj1, amic2,
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1,6-anhydro-N-acetylmuramic acid-L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase
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acetylmuramoyl-alanine amidase
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acetylmuramyl-alanine amidase
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acetylmuramyl-L-alanine amidase
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Cell wall hydrolase
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Mucopeptide aminohydrolase
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N-acetylmuramic acid L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase type I
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N-acetylmuramoyl-L-alanine amidase type II
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N-acetylmuramyl-L-alanine amidase
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N-acetylmuramylalanine amidase
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N-acylmuramyl-L-alanine amidase
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hydrolysis of peptide bond
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peptidoglycan amidohydrolase
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1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
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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
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?
GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
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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
biphasic behavior: rapid exponential phase preceding a linear phase (0.027 mM substrate, 0.000106 mM enzyme)
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N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
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peptidoglycan + H2O
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L-alanine-p-nitroanilide + H2O
?
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N-acetylmuramoyl-L-alanine + H2O
?
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N-acetylmuramoyl-L-alanine-gamma-D-glutamyl-mesodiaminopimelic acid + H2O
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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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N-acetylmuramoyl-L-alanyl-gamma-D-glutaminyl-meso-diaminopimelic acid + H2O
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N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
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phospho-N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
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uridine diphospho-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid + H2O
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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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1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
?
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?
peptidoglycan + H2O
?
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?
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Zn2+
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Zn2+
required for activity
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DD-diaminopimelic acid
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at 10 mM
L-alanyl-gamma-D-glutamyl-(L)-meso-diaminopimelic acid
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at 5 mM
meso-diaminopimelic acid
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at 10 mM
phosphatidylglycerol
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concentrations higher than 0.3 mM
phosphatidylglycerol
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phosphatidylglycerol and cardiolipin
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cetyltrimethylammonium bromide
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diheptanoylphosphatidylcholine
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glucosamine
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30% activation at 10 mM
lysophosphatidylcholine
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lysophosphatidylethanolamine
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phosphatidylglycerol
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concentrations of 0.002-0.05 mM
polyoxyethylene lauryl ether
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polyoxyethylene p-t-octylphenol
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polyoxyethylene sorbitol oleate
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Sodium dodecyl sulfate
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sodium lauryl-N-sarcosinate
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Tetradecyltrimethylammonium bromide
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0.04
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid
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0.5
N-acetylmuramoyl-L-alanyl-gamma-D-glutaminyl-meso-diaminopimelic acid
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additional information
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Uniprot
brenda
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brenda
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brenda
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brenda
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32000
x * 32000 Da, SDS-PAGE
41000
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SDS-PAGE, gel filtration
39000
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gel filtration, SDS-PAGE
39000
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SDS-PAGE, gel filtration
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hanging drop vapor diffusion method, using 1 M LiCl, 10% (w/v) polyethylene glycol 6000 in a 0.1 M sodium citrate buffer (pH 4) for the native structure, and 1 M MgSO4 in a 0.1 M sodium acetate buffer (pH 4.6) for the Se-Met structure. The apoenzyme in complex with the substrate anhydro-N-acetylmuramic-acid-L-Ala-gamma-D-Glu-L-Lys is crystallized using 50% (w/v) polyethylene glycol 6000, 0.1 M sodium citrate buffer (pH 4), and 5 mM EDTA. The holoenzyme in complex with the product L-Ala-gamma-D-Glu-L-Lys is crystallized using 1 M MgCl2 in a 0.1 M sodium acetate buffer, pH 4.6
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S-Sepharose column chromatography, Q-Sepharose column chromatography, and Sephacryl S100 gel filtration
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expressed in Escherichia coli LMG194 and B180 cells
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inactivation by treatment with 1.2 mM phosphatidylglycerol, complete recovery by adding K+, Mg2+, putrescine, spermidine or spermine
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Vanderwinkel, E.; De Vlieghere, M.; Charles, P.; Baptist, V.
Nature of the interactions involved in the lipid-protein complexes of the Escherichia coli N-acetylmuramoyl-L-alanine amidase
Biochim. Biophys. Acta
913
238-244
1987
Escherichia coli
brenda
Vanderwinkel, E.; De Vlieghere, M.
Modulation of Escherichia coli N-acetylmuramoyl-L-alanine amidase activity by phosphatidylglycerol
Biochim. Biophys. Acta
838
54-59
1985
Escherichia coli
brenda
Parquet, C.; Flouret, B.; Leduc, M.; Hirota, Y.; van Heijenoort, J.
N-Acetylmuramoyl-L-alanine amidase of Escherichia coli K12. Possible physiological functions
Eur. J. Biochem.
133
371-377
1983
Escherichia coli
brenda
Vanderwinkel, E.; De Vlieghere, M.; De Tanhoffer De Volcsey, L.
Activity of N-acetylmuramoyl-L-alanine amidase in phospholipidic enviroments
Biochim. Biophys. Acta
663
46-57
1984
Escherichia coli
brenda
Van Heijenoort, J.; Parquet, C.; Flouret, B.; Van Heijenoort, Y.
Envelope-bound N-acetylmuramyl-L-alanine amidase of Escherichia coli K 12. Purification and properties of the enzyme
Eur. J. Biochem.
58
611-619
1975
Escherichia coli
brenda
Uehara, T.; Park, J.T.
An anhydro-N-acetylmuramyl-L-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coli
J. Bacteriol.
189
5634-5641
2007
Escherichia coli (P75820)
brenda
Pennartz, A.; Genereux, C.; Parquet, C.; Mengin-Lecreulx, D.; Joris, B.
Substrate-induced inactivation of the Escherichia coli AmiD N-acetylmuramoyl-L-alanine amidase highlights a new strategy to inhibit this class of enzyme
Antimicrob. Agents Chemother.
53
2991-2997
2009
Escherichia coli (P75820), Escherichia coli
brenda
Kerff, F.; Petrella, S.; Mercier, F.; Sauvage, E.; Herman, R.; Pennartz, A.; Zervosen, A.; Luxen, A.; Frre, J.; Joris, B.; Charlier, P.
Specific structural features of the N-acetylmuramoyl-L-alanine amidase amid from Escherichia coli and mechanistic implications for enzymes of this family
J. Mol. Biol.
397
249-259
2010
Escherichia coli (P75820), Escherichia coli
brenda