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

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.5.1.28
-
RECOMMENDED NAME
GeneOntology No.
N-acetylmuramoyl-L-alanine amidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
show the reaction diagram
-
-
-
-
Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
show the reaction diagram
catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
anhydromuropeptides recycling
-
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan amidohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,6-anhydro-N-acetylmuramic acid-L-alanine amidase
-
-
1,6-anhydro-N-acetylmuramyl-L-alanine amidase
-
-
acetylmuramoyl-alanine amidase
-
-
-
-
acetylmuramyl-alanine amidase
-
-
-
-
acetylmuramyl-L-alanine amidase
-
-
-
-
AmiB
Pseudomonas aeruginosa PA01
-
-
-
AmiD
P75820
-
AmiE
-
formerly YbbE
AmiE
Bacillus subtilis 168
-
formerly YbbE
-
AmpD
Q63AE6
-
AmpD
Q63AE6
-
-
anhydroMurNAc-L-Ala amidase
-
-
AtlE
-
148 kDa autolysin of Staphylococcus epidermidis
Autolysin
-
-
-
-
Autolysin
Pseudomonas aeruginosa PA01
-
-
-
Autolysin
Streptococcus pneumoniae P046
-
-
-
Cell wall hydrolase
-
-
-
-
CwhA
P81717
cell wall hydrolytic amidase
Endolysin
Bacillus cereus phage
-
-
Endolysin
Bacillus cereus phage BPS13
-
-
-
LysBPS13
Bacillus cereus phage
-
-
LysBPS13
Bacillus cereus phage BPS13
-
-
-
lysostaphin
-
activities: N-acetyl muramyl-L-alanine amidase, glycylglycine endopeptidase and endo-beta-N-acetyl glucosamidase
LytA
-
major autolysin of Streptococcus pneumoniae
LytA
Streptococcus pneumoniae P046
-
-
-
LytA-like N-acetylmuramoyl-L-alanine amidase
Q706F5, Q706F9
-
LytA-like N-acetylmuramoyl-L-alanine amidase
Q706F5
-
-
LytA-like N-acetylmuramoyl-L-alanine amidase
Streptococcus mitis HER1055
Q706F9
-
-
LytAB6
Q706F5
-
LytAB6
Q706F5
-
-
LytAHER
Q706F9
-
LytAHER
Streptococcus mitis HER1055
Q706F9
-
-
Lytic amidase
-
-
-
-
Mucopeptide aminohydrolase
-
-
-
-
murein hydrolase
-
-
-
-
Nacetylmuramoyl-L-alanine amidase activity
-
-
N-acetyl muramyl-L-alanine amidase
-
-
N-acetyl-muramoyl-L-alanine amidase
Q8LTE6
lysin PlyG
N-acetyl-muramoyl-L-alanine amidase
-
-
N-acetylmuramic acid L-alanine amidase
-
-
-
-
N-acetylmuramoyl-L-alanine amidase
-
-
-
-
N-acetylmuramoyl-L-alanine amidase
-
-
N-acetylmuramoyl-L-alanine amidase
-
-
N-acetylmuramoyl-L-alanine amidase
-
-
N-acetylmuramoyl-L-alanine amidase
-
-
N-acetylmuramoyl-L-alanine amidase
B5L7M5
activity of a bifunctional autolysin
N-acetylmuramoyl-l-alanine amidase B
-
-
N-acetylmuramoyl-l-alanine amidase B
Pseudomonas aeruginosa PA01
-
-
-
N-acetylmuramoyl-L-alanine amidase type I
-
-
-
-
N-acetylmuramoyl-L-alanine amidase type II
-
-
-
-
N-acetylmuramyl-L-alanine amidase
-
-
-
-
N-acetylmuramyl-L-alanine amidase
Bacillus cereus phage
-
-
N-acetylmuramyl-L-alanine amidase
Bacillus cereus phage BPS13
-
-
-
N-acetylmuramyl-L-alanine amidase
-
-
N-acetylmuramyl-L-alanine amidase
Bacillus subtilis 168
-
-
-
N-acetylmuramyl-L-alanine amidase
O51610
-
N-acetylmuramyl-L-alanine amidase
Borrelia burgdorferi B31A
O51610
-
-
N-acetylmuramylalanine amidase
-
-
-
-
N-acylmuramyl-L-alanine amidase
-
-
-
-
NAM-amidase
Streptococcus pneumoniae P046
-
-
-
NAMLAA
Q96PD5
-
ORFL3
-
-
-
-
peptidoglycan recognition protein 2
Q96PD5
-
peptidoglycan recognition protein SC1a
-
-
peptidoglycan recognition protein-L
Q96PD5
-
PGLYRP2
Q96PD5
-
PGRP-L
Q96PD5
-
Skl
Streptococcus mitis SK137
-
-
-
T3 lysozyme
-
-
-
-
T7 lysozyme
-
-
-
-
LytN
-
LytN harbors LysM and histidine-dependent amidohydrolase/peptidase domains, the latter of which functions as both an N-acetylmuramoyl-L-alanine amidase and D-alanyl-glycine endopeptidase
additional information
Q70PY2
the enzyme belongs to the peptidoglycan recognition protein, PGRP, family
additional information
-
the enzyme is a member of the choline-binding family, subfamily CHAP-containing enzymes, of proteins
additional information
Streptococcus mitis SK137
-
the enzyme is a member of the choline-binding family, subfamily CHAP-containing enzymes, of proteins
-
CAS REGISTRY NUMBER
COMMENTARY
9013-25-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Bacillus cereus phage
-
-
-
Manually annotated by BRENDA team
Bacillus cereus phage BPS13
-
-
-
Manually annotated by BRENDA team
-
Q8LTE6
UniProt
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
strain B31A
UniProt
Manually annotated by BRENDA team
Borrelia burgdorferi B31A
strain B31A
UniProt
Manually annotated by BRENDA team
strain ATCC6879
-
-
Manually annotated by BRENDA team
gene PGRP-SB1 or CG9681; gene PGRP-SB1 or CG9681
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
PGLYRP2; gene pglyrp2
SwissProt
Manually annotated by BRENDA team
reclassified as Listonella anguillarum
-
-
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
Pseudomonas aeruginosa PA01
strain PA01, gene amiB
-
-
Manually annotated by BRENDA team
strain ATCC 43809
UniProt
Manually annotated by BRENDA team
Streptococcus milleri NMSCC 061
NMSCC 061
-
-
Manually annotated by BRENDA team
strain SK137, gene skl
-
-
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
Streptococcus mitis bacteriophage PHIB6; isolated from Streptococcus mitis strain B6
SwissProt
Manually annotated by BRENDA team
Streptococcus mitis HER1055
Streptococcus mitis bacteriophage PHIHER; isolated from Streptococcus mitis strain HER1055
SwissProt
Manually annotated by BRENDA team
Streptococcus mitis SK137
strain SK137, gene skl
-
-
Manually annotated by BRENDA team
serotype 14 strain Tupelo
-
-
Manually annotated by BRENDA team
strains R6 and TIGR4 and clinical isolate 033806
-
-
Manually annotated by BRENDA team
strains SVMC28and R36A
-
-
Manually annotated by BRENDA team
Streptococcus pneumoniae P046
-
-
-
Manually annotated by BRENDA team
various strains
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
vancomycin tolerance in clinical and laboratory Streptococcus pneumoniae isolates depends on reduced enzyme activity of the major LytA autolysin
metabolism
-
AmiE and NagZ in conjunction liberate MurNAc by sequential hydrolysis of muropeptides
metabolism
Bacillus subtilis 168
-
AmiE and NagZ in conjunction liberate MurNAc by sequential hydrolysis of muropeptides
-
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
Bacillus cereus phage
-
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
Bacillus cereus phage BPS13
-
endolysin LysBPS13 demonstrates high lytic activity against Bacillus cereus
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Q96PD5
-
-
-
?
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
-
-
-
-
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
Q96PD5
-
-
-
?
cell walls
?
show the reaction diagram
Pneumococcal bacteriophage HB-3
-
pneumococcal cell walls, labeled with [methyl-3H]choline, L-[4,5-3H]lysine monohydrochloride, or [2-14C]ethanolamine
-
-
?
cell walls
?
show the reaction diagram
-
pneumococcal cell walls labeled with [methyl-3H] or [3H]lysine
-
-
?
cell walls
?
show the reaction diagram
-
from Bacillus polymyxa
-
-
-
cell walls
?
show the reaction diagram
-
from Bacillus megaterium, Bacillus subtilis
-
-
?
cell walls
?
show the reaction diagram
-
from Bacillus megaterium, Bacillus subtilis
-
-
?
cell walls
?
show the reaction diagram
-
cell wall anchor structures from staphylococcal surface proteins
-
-
?
cell walls
?
show the reaction diagram
-
from Bacillus subtilis, [14C] glucosamine-labeled
-
-
?
cell walls
?
show the reaction diagram
-
from Bacillus lentus
-
-
?
cell walls
?
show the reaction diagram
-
from Micrococcus luteus, Listeria monocytogenes
-
-
?
cell walls
?
show the reaction diagram
-
from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
-
-
?
cell walls
?
show the reaction diagram
-
from Diplococcus pneumoniae
-
-
?
cell walls
?
show the reaction diagram
-
from Bacillus subtilis
-
-
?
cell walls
?
show the reaction diagram
-
from Micrococcus luteus ATCC 46898
-
-
?
cell walls
?
show the reaction diagram
Bacillus subtilis 168
-
from Bacillus subtilis, [14C] glucosamine-labeled
-
-
?
cell walls
?
show the reaction diagram
Bacillus subtilis 168
-
from Micrococcus luteus, Staphylococcus aureus, Bacillus megaterium
-
-
?
cell walls
?
show the reaction diagram
Streptococcus milleri NMSCC 061
-
from Micrococcus luteus ATCC 46898
-
-
?
GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
show the reaction diagram
P75820
-
-
-
-
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
-
-
-
?
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-L-Lys + H2O
MurNAc + L-Ala-D-isoGln-L-Lys
show the reaction diagram
Q96PD5
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
Q96PD5
-
-
-
?
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 + H2O
N-acetylmuramate + L-alanine
show the reaction diagram
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
show the reaction diagram
Bacillus cereus phage
-
-
-
-
?
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
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
show the reaction diagram
Q96PD5
the enzyme hydrolyzes bacterial peptidoglycan
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
show the reaction diagram
Q70PY2
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
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, 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
show the reaction diagram
-
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-alanine + H2O
N-acetylmuramate + L-alanine
show the reaction diagram
Bacillus cereus phage BPS13
-
-
-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
show the reaction diagram
Bacillus subtilis 168
-
-
-
-
?
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-gamma-glutaminyl-meso-diaminopimelic 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-gamma-glutaminyl-meso-diamino [3,4,5-3H]pimelic acid (3H-MTP)
-
-
?
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
P06653
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
?
show the reaction diagram
-, P81717
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
?
show the reaction diagram
P06653
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
-
-
?
peptidoglucan + H2O
?
show the reaction diagram
Q96PD5
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
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
P75820
-
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
Bacillus cereus phage
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
enzyme is required for the recognition of peptidoglycan, a component of bacterial cell walls, and therefore critical for the immune response
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
Bacillus cereus phage BPS13
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
Pseudomonas aeruginosa PA01
-
-
-
-
?
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
-
-
-
-
?
L-alanine-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
AmpD is involved in both peptidoglycan recycling and beta-lactamase induction
-
-
-
additional information
?
-
-
AtlE is involved in the initial attachment of the cells to polymer surfaces and thus in biofilm formation
-
-
-
additional information
?
-
-, P81717
bacteriolytic/cell wall hydrolytic amidase
-
-
-
additional information
?
-
-
AtlE is a multifunctional, surface-associated protein having both enzymic, 60 kDa amidase and 52 kDa glucosaminidase, and adhesive functions, AtlE binds to vitronectin
-
-
-
additional information
?
-
-
not: L-Ala-p-nitroanilide, D-Ala-p-nitroanilide, Gly-p-nitroanilide
-
-
-
additional information
?
-
Q96PD5
PGRP-L has no direct bacteriolytic activity for intact bacteria, not: MurNAc-L-Ala-D-isoGln, GlcNAc-MurNAc-L-Ala-D-isoGln
-
-
-
additional information
?
-
Q706F5, Q706F9
the enzyme performs cell wall lysis
-
-
-
additional information
?
-
-
the enzyme performs cell wall lysis and is important in cell separation of Staphylococcus aureus
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Q70PY2
the enzyme performs cell wall lysis, and shows antibacterial activity against Bacillus megaterium
-
-
-
additional information
?
-
-
the activity of recombinant C-terminal and N-terminal enzyme fragments towards cell wall peptidoglycans is analyzed by MALDI-TOF MS
-
-
-
additional information
?
-
-
the enzyme does not show antibacterial activity
-
-
-
additional information
?
-
-
the enzyme performs lysis of pneumococcal, choline-containing cell walls
-
-
-
additional information
?
-
-
the enzyme cleaves the amide linkage between the stem peptides and the lactyl moiety of muramoyl residues in bacterial cell wall heteropolymer peptidoglycan
-
-
-
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
?
-
-
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
-
-
-
additional information
?
-
-, Q63AE6
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 has no activity on MurNAc-L-Ala-D-Glu
-
-
-
additional information
?
-
Bacillus subtilis 168
-
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
?
-
Streptococcus mitis HER1055
Q706F9
the enzyme performs cell wall lysis
-
-
-
additional information
?
-
Streptococcus mitis SK137
-
the enzyme performs lysis of pneumococcal, choline-containing cell walls
-
-
-
additional information
?
-
Streptococcus pneumoniae P046
-
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
-
-
-
additional information
?
-
Q706F5
the enzyme performs cell wall lysis
-
-
-
additional information
?
-
-, Q63AE6
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
?
-
Pseudomonas aeruginosa PA01
-
the enzyme cleaves the amide linkage between the stem peptides and the lactyl moiety of muramoyl residues in bacterial cell wall heteropolymer peptidoglycan
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
?
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
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
P75820
-
-
-
-
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
Bacillus cereus phage
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
-
enzyme is required for the recognition of peptidoglycan, a component of bacterial cell walls, and therefore critical for the immune response
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
Bacillus cereus phage BPS13
-
-
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
Pseudomonas aeruginosa PA01
-
-
-
-
?
bacterial peptidoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
AmpD is involved in both peptidoglycan recycling and beta-lactamase induction
-
-
-
additional information
?
-
-
AtlE is involved in the initial attachment of the cells to polymer surfaces and thus in biofilm formation
-
-
-
additional information
?
-
-, P81717
bacteriolytic/cell wall hydrolytic amidase
-
-
-
additional information
?
-
Q706F5, Q706F9
the enzyme performs cell wall lysis
-
-
-
additional information
?
-
-
the enzyme performs cell wall lysis and is important in cell separation of Staphylococcus aureus
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Q70PY2
the enzyme performs cell wall lysis, and shows antibacterial activity against Bacillus megaterium
-
-
-
additional information
?
-
-
the enzyme cleaves the amide linkage between the stem peptides and the lactyl moiety of muramoyl residues in bacterial cell wall heteropolymer peptidoglycan
-
-
-
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
?
-
-
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
-
-
-
additional information
?
-
-, Q63AE6
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
?
-
Bacillus subtilis 168
-
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
?
-
Streptococcus mitis HER1055
Q706F9
the enzyme performs cell wall lysis
-
-
-
additional information
?
-
Streptococcus pneumoniae P046
-
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
-
-
-
additional information
?
-
Q706F5
the enzyme performs cell wall lysis
-
-
-
additional information
?
-
-, Q63AE6
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
?
-
Pseudomonas aeruginosa PA01
-
the enzyme cleaves the amide linkage between the stem peptides and the lactyl moiety of muramoyl residues in bacterial cell wall heteropolymer peptidoglycan
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
enzyme activated by low concentrations of Mg2+
Mg2+
-
activates enzyme at concentrations up to 1 mM
Mg2+
-
absolute requirement for divalent cation, maximal activity with 0.02 M MgCl2
Zn2+
-
requirement, contains 0.7 mol of zinc/mol of enzyme with no zinc added to the buffer, His-34 and Asp-164 are presumed to act as zinc ligands, Glu-116 contributes to the correct orientation of His-34
Zn2+
Q96PD5
Zn2+-dependent
Zn2+
-
absolutely required for activity
Zn2+
-
absolutely required for activity, mutant PGRP-SC1B lacking a potential zinc ligand is enzymatically inactive but retains its peptidoglycan affinity
Zn2+
-
required for activity
Zn2+
Bacillus cereus phage
-
the enzyme contains three zinc-binding sites
Zn2+
-
contains zinc
additional information
-
enzyme requires divalent cations
additional information
-
not activated by Cu2+, Co2+, Ni2+, Cd2+ or Mn2+
additional information
-, P81717
probably a metalloenzyme, no effect on lytic activity by Zn2+, Ca2+ or Mg2+, each at 5 mM
additional information
Bacillus cereus phage
-
the enzyme needs no metal ions for its lytic activity, 1 mM MgCl2, CaCl2, ZnCl2, or MnCl2 does not affect lytic activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
0.005 mM, complete inhibition after 30 min, activity can be restored by 0.1 mM ZnSO4
1,10-phenanthroline
-, P81717
strong, 5 mM, 94% inhibition
1,10-phenanthroline
-
inactivation through depletion of zinc ions
1,10-phenanthroline
-
-
benzoyl-Arg-p-nitroanilide
-
inhibition: moderately at 1 mM, completely at 10 mM
beta-mercaptoethanol
-
-
choline
Pneumococcal bacteriophage HB-3
-
-
choline
Q706F5, Q706F9
IC50: 0.4 mM; IC50: 2 mM
CTAB
Bacillus cereus phage
-
almost complete inhibition at 0.1 (v/v)
Cu2+
-
57% inhibition
DD-diaminopimelic acid
-
at 10 mM
deoxycholate
Q706F5, Q706F9
at 1%; at 1%
dipicolinic acid
-
0.005 mM, complete inhibition after 30 min, activity can be restored by 0.1 mM ZnSO4
dithiothreitol
-
-
dithiothreitol
-, P81717
5 mM, 53% inhibition
EDTA
-
25 mM EDTA
EDTA
-
0.005 mM, complete inhibition after 30 min, activity can be restored by 0.1 mM ZnSO4
EDTA
-, P81717
less inhibitory than 1,10-phenanthroline, 10 mM, 25% inhibition
EDTA
Q96PD5
complete inhibition, restored by 1 mM Zn2+, partially restored by 10 mM Mg2+
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
-
-
-
lipoteichoic acid
Pneumococcal bacteriophage HB-3
-
-
-
meso-diaminopimelic acid
-
at 10 mM
Muramic acid
-
-
MurNAc-L-Ala-D-Gln
-
competitive inhibitor
-
N-acetylglucosamine
-
-
N-acetylmuramic acid
-
-
NaCl
-
at a concentration of 200 mM
NaCl
-, P81717
sensitive to salt concentration, loses its lytic activity in 10 mM Tris-HCl containing 100 mM NaCl
p-chloromercuribenzene sulfonate
-
-
p-chloromercuribenzene sulfonate
-
-
p-hydroxymercuribenzoic acid
-
-
phosphatidylglycerol
-
concentrations higher than 0.3 mM
phosphatidylglycerol
-
phosphatidylglycerol and cardiolipin
SDS
Bacillus cereus phage
-
almost complete inhibition at 0.1 (v/v)
Tris-HCl
-, P81717
lytic activity in 30 mM Tris-HCl is only 30% of that in 10 mM solution, almost inactive in 70 mM Tris-HCl
MgCl2
-
at a conecentration of 1 mM
additional information
-
not inhibited by 1,6-anhydro-beta-D-glucopyranose, 2-bromomethyl-1,3-dioxolane, anhydro-GlcNAc, L-Ala-p-nitroanilide, D-Ala-p-nitroanilide, Gly-p-nitroanilide
-
additional information
-, P81717
not inhibited by diisopropylfluorophosphate, iodoacetic acid, Zn2+, Ca2+, Mg2+, each at 5 mM
-
additional information
Bacillus cereus phage
-
the activity of the enzyme is not inhibited by 300 mM EDTA or CHAPS, Triton X-100 and Tween-20 (0.1% (v/v) each)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
Bacillus cereus phage
-
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
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
-
-
17
-
GlcNAc-MurNAc-L-Ala-D-isoglutaminyl-meso-diaminopimelyl-D-Ala-D-Ala
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Diplococcus pneumoniae cell wall, 0.025 g/liter
-
additional information
-
additional information
-
kinetic data
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
25
-
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP
-
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
-
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
-
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
-
-
0.00163
-
7-methoxycoumarin-4-yl-acetyl-Ala-D-isoGlu-Lys(2,4-dinitrophenyl)-D-Ala-Arg
-
-
additional information
-
additional information
-
kinetic data
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
69
-
1,6-anhydro-MurNAc-L-Ala-gamma-D-Glu-m-DAP
-
at pH 7.0, temperature not specified in the publication
308494
22
-
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
308495
0.23
-
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
308493
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.19
-
MurNAc-L-Ala-D-Gln
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
choline
Q706F5, Q706F9
IC50: 0.4 mM
2
-
choline
Q706F5, Q706F9
IC50: 2 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0000044
-
Q706F5, Q706F9
-
0.0000046
-
Q706F5, Q706F9
-
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
0.447
-
-
-
1.113
-
-
-
1.23
-
-
-
10.2
-
-
-
16.36
-
-
fraction II
23.62
-
-
fraction I
46
-
-
-
58
-
-
isoenzyme I
100
-
-
isoenzyme II
132
-
-
purified recombinant enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
the enzyme shows highest activity with peptidoglycan substrates from Staphylococcus aureus, and 34% and 23% of this activity with substrate from Micrococcus luteus and Bacillus megaterium, respectively, at pH 8.0
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
Q706F5, Q706F9
;
6
-
Pneumococcal bacteriophage HB-3
-
-
6.5
-
-
assay at
7
-
-
assay at
7.2
-
-
assay at
7.5
-
-
phosphate buffer
8
-
-
autolysis assay at
8.5
-
-, P81717
-
8.6
-
-
tetraborate/boric acid buffer
9.5
-
Bacillus cereus phage
-
-
9.7
10
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.7
9
-
>80% activity
7.5
10.5
Bacillus cereus phage
-
lytic activity significantly decreases at above pH 10.5 and below pH 7.5
7.6
-
-
inactive below pH 7.6
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
autolysis assay at room temperature
25
-
-
assay at
29
-
-
intracellular protein
30
-
-
assay at
37
-
-, P81717
assay at
37
-
Q96PD5
assay at
42
45
Bacillus cereus phage
-
-
65
-
-
extracellular protein
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
55
Bacillus cereus phage
-
about 50% activity at 35 and 55C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9.79
-
-
AmiB, sequence calculation
9.8
-
-
sequence calculation
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q96PD5
recombinant PGRP-L shows primarily intracellular and cell surface location
Manually annotated by BRENDA team
P06653
LytA is a surface-exposed enzyme
Manually annotated by BRENDA team
Bacillus subtilis 168
-
of mother cell
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
Streptococcus milleri NMSCC 061
-
-
-
-
Manually annotated by BRENDA team
Q96PD5
recombinant PGRP-L shows primarily intracellular and cell surface location
Manually annotated by BRENDA team
Q706F5, Q706F9
the enzyme posseses transmembrane segments; the enzyme possesses transmembrane segments
Manually annotated by BRENDA team
-
the enzyme posseses transmembrane segments
-
Manually annotated by BRENDA team
Streptococcus mitis HER1055
-
the enzyme possesses transmembrane segments
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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)
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)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
18500
-
-
gel filtration, SDS-PAGE
20000
-
-
SDS-PAGE
21000
-
-
gel filtration
21000
-
-
sucrose density gradient centrifugation
30000
40000
-
gel filtration
35000
-
-
SDS-PAGE, gel filtration
35000
-
-
SDS-PAGE
39000
-
-
gel filtration, SDS-PAGE
39000
-
-
SDS-PAGE, 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
-
B5L7M5, -
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 58000, SDS-PAGE, forms aggregates of high molecular mass at low salinity
?
-
x * 70000, SDS-PAGE
?
Pneumococcal bacteriophage HB-3
-
x * 36000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
?
-
x * 28000, SDS-PAGE
?
-
x * 70000, deglycosylated 60000, SDS-PAGE
?
-
x * 37500, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
-
x * 20847, wild-type AmpD, mass spectrometry
?
-
x * 148000, multifunctional AtlE
?
Q706F5, Q706F9
x * 36782, sequence calculation; x * 36919, sequence calculation
?
-
x * 32000, processed enzyme, SDS-PAGE x * 35800, unprocessed enzyme, sequence calculation
?
-
x * 32000 Da, SDS-PAGE
?
Q63AE6
x * 31130, calculated from amino acid sequence
?
Bacillus cereus phage
-
x * 35000, SDS-PAGE
?
-
x * 31130, calculated from amino acid sequence
-
?
Bacillus cereus phage BPS13
-
x * 35000, SDS-PAGE
-
?
Bacillus subtilis 168
-
x * 30000, SDS-PAGE
-
?
Streptococcus milleri NMSCC 061
-
x * 28000, SDS-PAGE
-
?
-
x * 36919, sequence calculation
-
?
Streptococcus mitis HER1055
-
x * 36782, sequence calculation
-
dimer
-
1 * 57000 + 1 * 70000, SDS-PAGE; 2 * 74000, SDS-PAGE
homodimer
P06653
2 * 36600, catalytically active homodimer, dimer interface
homodimer
-
-
monomer
-, P81717
1 * 19396, sequence calculation
monomer
P06653
monomeric LytA retains less than 10% of activity compared with the active homodimeric enzyme
additional information
Q96PD5
peptide mapping and immunospecificity analysis of enzyme proteins, overview
additional information
-
the enzyme contains a cysteine, histidine-dependent amidohydrolase/peptidase domain, i.e. CHAP domain
additional information
Streptococcus mitis SK137
-
the enzyme contains a cysteine, histidine-dependent amidohydrolase/peptidase domain, i.e. CHAP domain
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
Q96PD5
-
phosphoprotein
Q96PD5
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 ACCESSION NO.
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
-
two crystal forms of the C-terminal cell wall anchoring/choline-binding domain of LytA
P06653
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
half-life of staphylolytic activity: approximately 2 months (5C)
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
100
Bacillus cereus phage
-
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
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 ACCESSION NO.
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Triton X-100
Bacillus cereus phage
-
about 130% activity in the presence of 0.1 (v/v) Triton X-100
Triton X-100
Bacillus cereus phage BPS13
-
about 130% activity in the presence of 0.1 (v/v) Triton X-100
-
Tween 20
Bacillus cereus phage
-
about 115% activity in the presence of 0.1 (v/v) Tween 20
Tween 20
Bacillus cereus phage BPS13
-
about 115% activity in the presence of 0.1 (v/v) Tween 20
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 3 months, little change in activity
-
-20C, several months, no loss of activity
-
0C, activity decreases by 97% in the first 24 hours after preparation
-
-18C, several months, no loss of activity
-
-20C or 4C, overnight, in glass tubes, total loss of activity
-
-20C, crude cell extract, 2 years, 20% loss of activity
-
-20C, overnight, in polycarbonate tubes, 25-50% loss of activity
-
-20C, 1 month, no loss of activity
-
0C, enzyme-resin complex, several months, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
from achromopeptidase
-, P81717
Ni-nitrilotriacetate resin column chromatography
Q63AE6
Ni-NTA resin column chromatography
Bacillus cereus phage
-
HiTrap column chromatography, gel filtration
-
recombinant wild-type and mutant AmpD
-
gene PGRP-SB1, recombinant His6-tagged wild-type and mutant enzyme by nickel affinity chromatography
-
7000-10000fold
-
S-Sepharose column chromatography, Q-Sepharose column chromatography, and Sephacryl S100 gel filtration
-
10-15fold
-
354fold
-
56fold
-
739fold
-
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
Q96PD5
two methods
-
10-15fold
-
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
-
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
-
Ni-NTA Sepharose column chromatography, gel filtration
-
recombinant phage enzyme from Escherichia coli; recombinant phage enzyme from Escherichia coli
Q706F5, Q706F9
DEAE-cellulose column chromatography
-
recombinant LytA
P06653
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21 Star(DE3) cells
Bacillus cereus phage
-
expressed in Escherichia coli BL21(DE3) cells as a cytoplasmic N-terminal His10-tagged fusion protein
-
ampD gene, expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
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
-
expressed in Escherichia coli LMG194 and B180 cells
-
expression in COS-7 cells and in HepG2/C3A human hepatoblastoma cells
Q96PD5
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
Q96PD5
expression in Escherichia coli
-
Escherichia coli
Pneumococcal bacteriophage HB-3
-
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
-
Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
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
-
Escherichia coli
-
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
Q706F5, Q706F9
gene skl, expression in Escherichia coli strain DH10B
-
lytA gene, expression in Escherichia coli RB791
P06653
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
E90A
Q8LTE6
no bacteriolytic activity
H29N
Q8LTE6
no bacteriolytic activity
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
Q96PD5
inactive mutant
C530S
Q96PD5
inactive mutant
H411A
Q96PD5
mutant with full amidase activity
W442A
Q96PD5
mutant with reduced amidase activity
K135A
Q8LTE6
bacteriolytic activity similar to that of wild-type PlyG
additional information
Q8LTE6
deletion of the C-terminal region completely abolishes the lytic activity
H436A
Q96PD5
mutant with full amidase activity
additional information
Q96PD5
N-terminal DELTA1-343 deletion mutant of PGRP-L with reduced activity, inactive C-terminal DELTA344-576 deletion mutant of PGRP-L
additional information
Q96PD5
construction of deletion mutants DELTA1-322, DELTA323-555, and DELTA474-555
Y447A
Q96PD5
inactive mutant
additional information
-
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
-
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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q96PD5
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
-
detection of Vibrio anguillarum, a fish pathogen via PCR-detection of the gene for N-acetylmuramoyl-L-alanine amidase