Information on EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.28
-
RECOMMENDED NAME
GeneOntology No.
N-acetylmuramoyl-L-alanine amidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anhydromuropeptides recycling
-
-
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9013-25-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bacillus cereus phage BPS13
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
subsp. kurstaki, orf bt2494, gene cwlB
-
-
Manually annotated by BRENDA team
subsp. kurstaki, orf bt2494, gene cwlB
-
-
Manually annotated by BRENDA team
Borrelia burgdorferi
strain B31A
UniProt
Manually annotated by BRENDA team
Borrelia burgdorferi B31A
strain B31A
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene amiC, several strains, overview
-
-
Manually annotated by BRENDA team
Pneumococcal bacteriophage HB-3
-
-
-
Manually annotated by BRENDA team
strain PA01, gene amiB
-
-
Manually annotated by BRENDA team
strain ATCC 43809
UniProt
Manually annotated by BRENDA team
NMSCC 061
-
-
Manually annotated by BRENDA team
NMSCC 061
-
-
Manually annotated by BRENDA team
Streptococcus mitis bacteriophage PHIB6; isolated from Streptococcus mitis strain B6
SwissProt
Manually annotated by BRENDA team
Streptococcus mitis bacteriophage PHIHER; isolated from Streptococcus mitis strain HER1055
SwissProt
Manually annotated by BRENDA team
strain SK137, gene skl
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
various strains
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(GlcNAc-MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala)2 + H2O
?
show the reaction diagram
-
-
-
?
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP + H2O
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
1,6-anhydromuropeptide + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
bacterial peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
bacterial spore peptidoglycan
?
show the reaction diagram
-
-
-
-
-
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
?
show the reaction diagram
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
show the reaction diagram
-
-
-
-
?
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
biotin-peptidoglucan + H2O
?
show the reaction diagram
-
-
-
?
cell walls
?
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)
-
-
?
GlcNAc-MurNAc-anhydro-L-Ala-D-gluc-meso-diaminopimelyl-D-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoGIn-meso-diaminopimelyl-(D)-amide-(L)-D-Ala-D-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
GlcNAc-MurNAc-L-Ala-D-isoGln-meso-diaminopimelyl-D-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
L-alanine-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
murein + H2O
?
show the reaction diagram
-
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
show the reaction diagram
MurNAc-L-Ala-D-isoGln-L-Lys + H2O
MurNAc + L-Ala-D-isoGln-L-Lys
show the reaction diagram
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
show the reaction diagram
-
-
-
?
N-(beta-1,4-N-acetylglucosaminyl-N-acetylmuramoyl-L-alanyl-gamma-D-isoglutaminyl)-L-lysyl-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-glucosaminyl(beta1-4)N-acetylmuramoyl-tetrapeptide + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-glucosaminyl(beta1-4)N-acetylmuramoyl-tripeptide + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylglucosaminyl-1,6-anhydro-N-acetylmuramyl-tripeptide + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
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-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine + 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
-
-
-
-
?
peptidoglucan + H2O
?
show the reaction diagram
peptidoglycan + 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 SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP + H2O
1,6-anhydro-MurNAc + L-Ala-gamma-D-Glu-m-DAP
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
?
show the reaction diagram
P75820
-
-
-
-
4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala + H2O
?
show the reaction diagram
-
the substrate is likely not turned over in vitro by AmpD
-
-
?
bacterial peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
show the reaction diagram
-
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
-
-
?
peptidoglucan + H2O
?
show the reaction diagram
P06653
cell autolysis, LytA rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone, LytA is an important pneumococcal virulence factor
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
benzoyl-Arg-p-nitroanilide
-
inhibition: moderately at 1 mM, completely at 10 mM
beta-mercaptoethanol
-
-
choline
CTAB
-
almost complete inhibition at 0.1 (v/v)
DD-diaminopimelic acid
-
at 10 mM
deoxycholate
at 1%; at 1%
dipicolinic acid
-
0.005 mM, complete inhibition after 30 min, activity can be restored by 0.1 mM ZnSO4
dithiothreitol
EGTA
-
0.2 mM EGTA
glutathione
-
-
iodoacetamide
-
-
iodoacetate
-
-
KCl
-
at a concentration of 200 mM
L-alanyl-gamma-D-glutamyl-(L)-meso-diaminopimelic acid
-
at 5 mM
LiCl
-
at a concentration of 200 mM
lipoteichoic acid
meso-diaminopimelic acid
-
at 10 mM
MgCl2
-
at a conecentration of 1 mM
Muramic acid
-
-
MurNAc-L-Ala-D-Gln
-
competitive inhibitor
-
N-acetylglucosamine
-
-
N-acetylmuramic acid
-
-
p-chloromercuribenzene sulfonate
p-hydroxymercuribenzoic acid
-
-
phosphatidylglycerol
SDS
-
almost complete inhibition at 0.1 (v/v)
teichoic acid
-
-
Tris-HCl
lytic activity in 30 mM Tris-HCl is only 30% of that in 10 mM solution, almost inactive in 70 mM Tris-HCl
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ammonium acetate
-
18% activation at 0.15 M
ammonium sulfate
-
20% activation at 0.15 M
Cetyltrimethylammonium bromide
-
-
Dicetyl phosphate
-
-
diheptanoylphosphatidylcholine
-
-
glucosamine
-
30% activation at 10 mM
lysophosphatidylcholine
-
-
lysophosphatidylethanolamine
-
-
NaCl
-
the highest lytic activity is observed in the presences of 250 mM NaCl
NH4Cl
-
8% activation at 0.15 M
phosphatidylglycerol
-
concentrations of 0.002-0.05 mM
polyoxyethylene lauryl ether
-
-
-
polyoxyethylene p-t-octylphenol
-
-
-
polyoxyethylene sorbitol oleate
-
-
-
Sodium dodecyl sulfate
-
-
sodium lauryl-N-sarcosinate
-
-
Tetradecyltrimethylammonium bromide
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP
-
at pH 7.0, temperature not specified in the publication
0.5
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala
-
at pH 7.0, temperature not specified in the publication
1.76
4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala
-
at pH 7.0, temperature not specified in the publication
0.2849
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGln-Lys(2,4-dinitrophenyl)-D-Ala-Arg
-
-
0.3601
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg
-
-
4
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide
-
-
-
1.8
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
-
-
-
2.5
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-(beta-N-acetyl-glucasaminyl-(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
-
-
-
4
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide
-
-
-
2
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
-
-
-
2.5
GlcNAc-MurNAc-L-Ala-D-isoGIn-meso-diaminopimelyl-(D)-amide-(L)-D-Ala-D-Ala
-
-
8 - 17
GlcNAc-MurNAc-L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala
0.04
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid
-
-
0.5
N-acetylmuramoyl-L-alanyl-gamma-D-glutaminyl-meso-diaminopimelic acid
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP
Citrobacter freundii
-
at pH 7.0, temperature not specified in the publication
11
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala
Citrobacter freundii
-
at pH 7.0, temperature not specified in the publication
0.4
4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala
Citrobacter freundii
-
at pH 7.0, temperature not specified in the publication
0.00159
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGln-Lys(2,4-dinitrophenyl)-D-Ala-Arg
Staphylococcus epidermidis
-
-
0.00163
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg
Staphylococcus epidermidis
-
-
additional information
additional information
Citrobacter freundii
-
kinetic data
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
69
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP
Citrobacter freundii
-
at pH 7.0, temperature not specified in the publication
41096
22
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala
Citrobacter freundii
-
at pH 7.0, temperature not specified in the publication
41097
0.23
4-O-beta-D-GlcNAc-1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP-D-Ala-D-Ala
Citrobacter freundii
-
at pH 7.0, temperature not specified in the publication
41095
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
MurNAc-L-Ala-D-Gln
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 2
choline
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
Skl, substrate are choline-containing cell walls of Streptococcus mitis
0.03
-
Skl, substrate are choline-containing cell walls of Streptococcus pneumoniae
0.144
-
-
0.301
-
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
0.325
-
beta-N-acetylglucosaminyl-(1-4)-N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide
0.385
-
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
0.402
-
beta-N-acetylglucosaminyl-(1-4)-N,6-O-diacetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide-(L)-D-alanine
0.408
-
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
0.41
-
-
0.425
-
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-(L)-meso-2,6-diaminopimelic acid-(D)-amide
1.113
-
-
1.23
-
-
10.2
-
-
16.36
-
fraction II
23.62
-
fraction I
58
-
isoenzyme I
100
-
isoenzyme II
132
-
purified recombinant enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9
-
-
5.7 - 9
-
>80% activity
7.5 - 10.5
-
lytic activity significantly decreases at above pH 10.5 and below pH 7.5
7.6
-
inactive below pH 7.6
9 - 11
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29
-
intracellular protein
42 - 45
-
-
65
-
extracellular protein
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 55
-
about 50% activity at 35 and 55C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
sequence calculation
9.79
-
AmiB, sequence calculation
9.8
-
sequence calculation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in granulocytes
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus thuringiensis subsp. konkukian (strain 97-27)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Peptoclostridium difficile (strain 630)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18500
-
gel filtration, SDS-PAGE
20000
-
SDS-PAGE
30000 - 40000
-
gel filtration
41000
-
SDS-PAGE, gel filtration
47000
-
sucrose density gradient centrifugation
51000
-
SDS-PAGE
58000
-
SDS-PAGE
62000
-
sucrose density gradient centrifugation
62920
-
calculated from amino acid sequence
65000
N-acetylmuramoyl-L-alanine amidase domain of the bifunctional autolysin AtlL
75000
-
SDS-PAGE
82000
-
gel filtration
110000
-
gel filtration, fraction I
120000
-
gel filtration, (Sephadex)
130000
-
gel filtration, (Sephacryl)
135000
-
native gradient PAGE, gel filtration
220000
-
gel filtration, fraction II
800000 - 1000000
-
sucrose density gradient centrifugation, gel filtration
additional information
-
the gene encodes a protein of 137 kDa which is exported and processed in the multiple autolysin bands seen
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 57000 + 1 * 70000, SDS-PAGE; 2 * 74000, SDS-PAGE
homodimer
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
phosphoprotein
the enzyme contains a phosphorylation site at S218
additional information
-
the enzyme possesses a signal peptide for secretion from the cell
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
-
purified enzyme Rv3717 free, or in complex with L-Ala-iso-D-Gln product or Zn2+, hanging drop vapor diffusion method, from 200 mM NaCl, 100 mM Tris, pH 8.5, 25% PEG 3350, X-ray diffraction structure determination and analysis at 2.1-2.67 A resolution, molecular replacement method using Bartonella henselae AmiB as the search model, PDB code 3NE8
two crystal forms of the C-terminal cell wall anchoring/choline-binding domain of LytA
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
half-life of staphylolytic activity: approximately 2 months (5C)
695804
5 - 7
-
-
172000
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 100
-
the enzyme demonstrates remarkable thermostability in the presence of 30% (v/v) glycerol, and it retains its lytic activity after incubation between 4 and 100C for 30 min
5
-
half-life of staphylolytic activity: approximately 2 months (pH 4)
25
-
10 min at 25C result in 25% loss of inactivation
30 - 50
-
-
35
-
Tm, H34A mutant AmpD + Zn2+
37
-
recombinant lysostaphin: stable for 72 h
39
-
Tm, D164A mutant AmpD + Zn2+
46
-
Tm, D164A mutant AmpD
50
-
stable below 50C
51
-
Tm, H34A mutant AmpD
52
-
Tm, H154A mutant AmpD + Zn2+
55
-
Tm, Y63F mutant AmpD + Zn2+
56
-
Tm, H154A mutant AmpD, K162H mutant AmpD + Zn2+
57
-
Tm, H154N mutant AmpD + Zn2+
59
-
Tm, K162Q mutant AmpD + Zn2+
60
-
Tm, wild-type AmpD, wild-type AmpD + Zn2+, H154N and K162Q mutant AmpD
61
-
Tm, Y63F mutant AmpD
62
-
Tm, E116A mutant AmpD + Zn2+, K162H mutant AmpD
66
-
Tm, E116A mutant AmpD
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
Tween 20
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, several months, no loss of activity
-20C or 4C, overnight, in glass tubes, total loss of activity
-
-20C, 1 month, no loss of activity
-
-20C, 3 months, little change in activity
-
-20C, crude cell extract, 2 years, 20% loss of activity
-
-20C, overnight, in polycarbonate tubes, 25-50% loss of activity
-
-20C, several months, no loss of activity
-
0C, activity decreases by 97% in the first 24 hours after preparation
-
0C, enzyme-resin complex, several months, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10-15fold
354fold
-
56fold
-
7000-10000fold
-
739fold
-
combination of affinity and cation-exchange chromatographies; recombinant C-terminally His-tagged enzyme 38fold from Escherichia coli by nickel affinity and cation exchange chromatography to 98% homogeneity
-
DEAE-cellulose column chromatography
-
from achromopeptidase
gene PGRP-SB1, recombinant His6-tagged wild-type and mutant enzyme by nickel affinity chromatography
-
HiTrap column chromatography, gel filtration
-
native enzyme 307.7fold from cell culture medium by dye-ligand affinity chromatography, the flow through of the step is used in hydrophobic interaction chromatography
-
native enzyme from liver by gel filtration, and immunoaffinity chromatography, native serum enzyme by immunoaffinity chromatography solubilization and purification of recombinant wild-type and truncated mutant enzymes from Escherichia coli inclusion bodies by treatment with 6 M urea and nickel affinity chromatography under denaturing conditions
Ni-nitrilotriacetate resin column chromatography
Ni-NTA resin column chromatography
-
Ni-NTA Sepharose column chromatography, gel filtration
-
recombinant GST-tagged enzyme from Escherichia coli strain BL-21 Codon Plus by glutathione affinity chromatography and tag cleavage, followed by a combined glutathione affinity/anion exchange chromatography step, and a gel filtration step
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) cell walls by sonication and nickel affinity chromatography
-
recombinant phage enzyme from Escherichia coli; recombinant phage enzyme from Escherichia coli
recombinant wild-type and mutant AmpD
-
S-Sepharose column chromatography, Q-Sepharose column chromatography, and Sephacryl S100 gel filtration
-
two methods
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ampD gene, expression in Escherichia coli
-
Escherichia coli
expressed in Escherichia coli BL21 Star(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells as a cytoplasmic N-terminal His10-tagged fusion protein
-
expressed in Escherichia coli LMG194 and B180 cells
-
expression in COS-7 cells and in HepG2/C3A human hepatoblastoma cells
expression in Escherichia coli
gene amiB, DNA and amino acid sequence determination and analysis, overexpression of the C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha; overexpression in Escherichia coli
-
gene cwlB, the gene and upstream gene cwlA form one transcriptional unit, DNA and amino acid sequence determination and analysis, sequence comparison. Transcription of the operon is directed by a promoter, PcwlA, which is located upstream from the cwlA gene and that the transcription start site is a single 5'-end nucleotide residue T located 25 nucleotides upstream from the cwlA translational start codon. The activity of PcwlA is controlled by sigmaK. Subcloning and gene modifications in Escherichia coli strains TG1 and SCS110, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene cwlD, DNA and amino acid sequence determination and analysis from strains CP26, CP39, CP509, CP297, CP697, CP726, CP776, CP1036, and CP1113, genotyping, recombinant expression in Escherichia coli strain Rosetta 2 (DE3), cloning in Escherichia coli strain DH5alpha
gene lytAB6, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression of the phage enzyme in Escherichia coli strain DH10B; gene lytAHER, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression of the phage enzyme in Escherichia coli strain DH10B
gene pglyrp2, DNA and amino acid sequence determination and analysis, no alternative splice forms, transient expression in COS-7 and HEK-293 cells, expression of wild-type and truncated mutant enzymes in Escherichia coli as inclusion bodies
gene PGRP-SB1, DNA and amino acid sequence determination and analysis, expression of His6-tagged 128 C-terminal residues and of his6-tagged 180 N-terminal residues in Escherichia coli strain XL-1I Blue
-
gene PGRP-SB1, expression of His6-tagged wild-type and mutant enzyme
-
gene Rv3717, expression of recombinant GST-tagged enzyme in Escherichia coli strain BL-21 Codon Plus
gene skl, expression in Escherichia coli strain DH10B
-
gene sle1, DNA and amino acid sequence determination and analysis, expression of His6-tagged 128 C-terminal residues and of His6-tagged 180 N-terminal residues in Escherichia coli strain XL-1I Blue
-
lytA gene, expression in Escherichia coli RB791
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after 1 h of exposure to DC-159a and sitafloxacin, there is no significant increase in the expression of LytA
-
after 2 h of exposure to twice the minimum inhibitory concentration, DC-159a increases the expression level of LytA by up to 3.6fold relative to the no drug control. Sitafloxacin induces expression of LytA by up to 4.6fold in S. pneumoniae strain R6 with 2 h of exposure to the minimum inhibitory concentration. Garenoxacin causes a less significant increase in LytA (up to 2.7fold at 2 h) than DC-159a and sitafloxacin
-
LytA is activated at the end of the lytic cycle, LytA is activated by the holing-induced membrane disruption
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E90A
no bacteriolytic activity
H29N
no bacteriolytic activity
K135A
bacteriolytic activity similar to that of wild-type PlyG
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
C419A
inactive mutant
C530S
inactive mutant
H411A
mutant with full amidase activity
H436A
mutant with full amidase activity
W442A
mutant with reduced amidase activity
Y447A
inactive mutant
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inactivation by treatment with 1.2 mM phosphatidylglycerol, complete recovery by adding K+, Mg2+, putrescine, spermidine or spermine
-
solubilization and purification of recombinant wild-type and truncated mutant enzymes from Escherichia coli inclusion bodies by treatment with 6 M urea and nickel affinity chromatography under denaturing conditions
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
detection of Vibrio anguillarum, a fish pathogen via PCR-detection of the gene for N-acetylmuramoyl-L-alanine amidase
drug development
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