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Information on EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase and Organism(s) Escherichia coli and UniProt Accession P75820

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Escherichia coli
UNIPROT: P75820 not found.
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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-
-
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acetylmuramyl-alanine amidase
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-
-
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acetylmuramyl-L-alanine amidase
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-
-
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Autolysin
-
-
-
-
Cell wall hydrolase
-
-
-
-
Lytic amidase
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-
-
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Mucopeptide aminohydrolase
-
-
-
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murein hydrolase
-
-
-
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N-acetylmuramic acid L-alanine amidase
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-
-
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N-acetylmuramoyl-L-alanine amidase
-
-
-
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N-acetylmuramoyl-L-alanine amidase type I
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-
-
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N-acetylmuramoyl-L-alanine amidase type II
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-
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N-acetylmuramyl-L-alanine amidase
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-
-
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N-acetylmuramylalanine amidase
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-
-
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N-acylmuramyl-L-alanine amidase
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-
-
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ORFL3
-
-
-
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T3 lysozyme
-
-
-
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T7 lysozyme
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9013-25-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
?
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
show the reaction diagram
-
-
-
?
GlcNAc-anhydroMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O
GlcNAc-anhydroMurNAc + L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala
show the reaction diagram
biphasic behavior: rapid exponential phase preceding a linear phase (0.027 mM substrate, 0.000106 mM enzyme)
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
show the reaction diagram
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
?
L-alanine-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanine-gamma-D-glutamyl-mesodiaminopimelic acid + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-glutamine + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-gamma-D-glutaminyl-meso-diaminopimelic acid + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
phospho-N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelyl-D-alanyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
uridine diphospho-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
?
show the reaction diagram
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DD-diaminopimelic acid
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at 10 mM
L-alanyl-gamma-D-glutamyl-(L)-meso-diaminopimelic acid
-
at 5 mM
meso-diaminopimelic acid
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at 10 mM
Muramic acid
-
-
N-acetylglucosamine
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N-acetylmuramic acid
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-
phosphatidylglycerol
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cetyltrimethylammonium bromide
-
-
Dicetyl phosphate
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diheptanoylphosphatidylcholine
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-
glucosamine
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30% activation at 10 mM
lysophosphatidylcholine
-
-
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
-
-
sodium lauryl-N-sarcosinate
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Tetradecyltrimethylammonium bromide
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
x * 32000 Da, SDS-PAGE
39000
41000
-
SDS-PAGE, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 32000 Da, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
S-Sepharose column chromatography, Q-Sepharose column chromatography, and Sephacryl S100 gel filtration
7000-10000fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli LMG194 and B180 cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inactivation by treatment with 1.2 mM phosphatidylglycerol, complete recovery by adding K+, Mg2+, putrescine, spermidine or spermine
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team