3.5.1.28: N-acetylmuramoyl-L-alanine amidase
This is an abbreviated version!
For detailed information about N-acetylmuramoyl-L-alanine amidase, go to the full flat file.
Word Map on EC 3.5.1.28
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3.5.1.28
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endolysins
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staphylococcus
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aureus
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autolysins
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streptococcus
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listeria
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pneumococcal
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bacteriolytic
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murein
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autolytic
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holins
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prophage
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muropeptides
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pgrps
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wall-binding
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teichoic
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lysostaphin
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transglycosylase
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histidine-dependent
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n-acetylmuramidase
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choline-containing
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bacteriophage-encoded
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diaminopimelic
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muramidase
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siphoviridae
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phage-encoded
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n-acetylglucosaminidase
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endo-beta-n-acetylglucosaminidase
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lysodeikticus
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drug development
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agriculture
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diagnostics
- 3.5.1.28
- endolysins
- staphylococcus
- aureus
- autolysins
- streptococcus
- listeria
- pneumococcal
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bacteriolytic
- murein
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autolytic
-
holins
- prophage
- muropeptides
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pgrps
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wall-binding
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teichoic
- lysostaphin
- transglycosylase
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histidine-dependent
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n-acetylmuramidase
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choline-containing
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bacteriophage-encoded
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diaminopimelic
- muramidase
- siphoviridae
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phage-encoded
- n-acetylglucosaminidase
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endo-beta-n-acetylglucosaminidase
- lysodeikticus
- drug development
- agriculture
- diagnostics
Reaction
Synonyms
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, AMI1, AmiA, AmiB, AmiC, AmiC2, AmiD, amidase 3, amidase-hydrolase, AmiE, AmpD, anhydroMurNAc-L-Ala amidase, AtlE, Autolysin, autolysin E, bacteriophage phiGVE2 amidase, cell separation amidase, cell wall amidase, Cell wall hydrolase, CwhA, CwlB protein, cwlC, CwlJ1, EC 3.4.17.7, EC 3.4.19.10, endolysin, GC-AmiC, GRCS_0011, LysBPS13, lysostaphin, LysSA97, LytA, LytA-like N-acetylmuramoyl-L-alanine amidase, LytAB6, LytAHER, Lytic amidase, Lytmu1/6, LytN, More, MSMEG_6281, Mtb peptidoglycan amidase, Mucopeptide aminohydrolase, murein hydrolase, MurnAc-lAA, Nacetylmuramoyl-L-alanine amidase activity, N-acetyl muramyl-L-alanine amidase, N-acetyl-muramoyl-L-alanine amidase, N-acetylmuramic acid L-alanine amidase, N-acetylmuramoyl-L-alanine amidase, N-acetylmuramoyl-l-alanine amidase B, N-acetylmuramoyl-L-alanine amidase type I, N-acetylmuramoyl-L-alanine amidase type II, N-acetylmuramyl-L-alanine amidase, N-acetylmuramylalanine amidase, N-acylmuramyl-L-alanine amidase, NAM-amidase, NAMLA amidase, NAMLAA, Npun_F1846, ORFL3, peptidoglycan amidase, peptidoglycan aminohydrolase, Peptidoglycan hydrolase, peptidoglycan recognition protein 2, peptidoglycan recognition protein SC1a, peptidoglycan recognition protein-L, PG amidase, PGLYRP2, PGRP, PGRP-L, PGRP-S4, PGRP-SB1, phage endolysin, phi26F_gp22, phiCP26F endolysin, phiGVE2 endolysin, PlyCP26F, PlyCP39O, PlyCpAmi, PlyGRCS, PlyPl23, RC0497, RS15875, Rv3717, SA97_036, short peptidoglycan recognition protein 4, Skl, Sle1, SleC, spore cortex lytic enzyme, T3 lysozyme, T7 lysozyme
ECTree
3.5.1.28 N-acetylmuramoyl-L-alanine amidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H182A
site-directed mutagenesis, inactive active site mutant, quantitative analysis of localization of AmiCH182A during the cell cycle, overview
H182A
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site-directed mutagenesis, inactive active site mutant, quantitative analysis of localization of AmiCH182A during the cell cycle, overview
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H182A
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site-directed mutagenesis, inactive active site mutant, quantitative analysis of localization of AmiCH182A during the cell cycle, overview
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E116A
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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
H154N
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mutation of a zinc ligand residue, active mutant which can bind zinc, kinetics
K162H
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0.7% of wild-type activity, residue is probably involved in substrate binding, kinetics
K162Q
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0.2% of wild-type activity, residue is probably involved in substrate binding, kinetics
Y63F
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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
E200X
E229D
Q316K
E229D
Q316K
C29S
site-directed mutagenesis, catalytically inactive mutant
H92A
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
C116A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
C131A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
D128A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
D148A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
D186E
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
D21A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
D35A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
D70A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
E109D
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
E181A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
H184A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
H66A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
K27R
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
K87A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
L52P
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
N99A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
P71A
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
Q107A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
Q78A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
R100A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
R97A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
T33A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to wild-type
W140A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
W167A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
W5A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
additional information
E229D
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mutation alters peptidoglycan fragment release and causes a defect in cell separation
E229D
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site-directed mutagenesis, the mutation leads to reduced enzyme activity and causes a defect in cell separation. The amiCE229D mutant releases larger [3H]glucosamine-labeled peptidoglycan fragments relative to the wild-type and no disaccharide. The amiCE229D mutant does not release some [3H]DAP-labeled peptide fragments, similar to a DELTAamiC strain
Q316K
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mutation results in an AmiC with increased enzymatic activity on macromolecular peptidoglycan and on the synthetic peptidoglycan derivative GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide). The same mutation also results in cell separation and peptidoglycan fragment release defects
Q316K
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site-directed mutagenesis, mutation Q316K results in an AmiC with increased enzymatic activity on macromolecular peptidoglycan (PG) and on the synthetic PG derivative. The same Q316K mutation that increases AmiC activity also results in cell separation and PG fragment release defects. But amiCQ316K mutation has only intermediate effects on PG fragment release and causes a slight defect in cell separation. In addition, the mutation amiCQ316K causes increased activity on whole sacculi and lysis of Escherichia coli cells
E229D
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mutation alters peptidoglycan fragment release and causes a defect in cell separation
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E229D
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site-directed mutagenesis, the mutation leads to reduced enzyme activity and causes a defect in cell separation. The amiCE229D mutant releases larger [3H]glucosamine-labeled peptidoglycan fragments relative to the wild-type and no disaccharide. The amiCE229D mutant does not release some [3H]DAP-labeled peptide fragments, similar to a DELTAamiC strain
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Q316K
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mutation results in an AmiC with increased enzymatic activity on macromolecular peptidoglycan and on the synthetic peptidoglycan derivative GlcNAc-MurNAc(pentapeptide)-GlcNAc-MurNAc(pentapeptide). The same mutation also results in cell separation and peptidoglycan fragment release defects
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Q316K
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site-directed mutagenesis, mutation Q316K results in an AmiC with increased enzymatic activity on macromolecular peptidoglycan (PG) and on the synthetic PG derivative. The same Q316K mutation that increases AmiC activity also results in cell separation and PG fragment release defects. But amiCQ316K mutation has only intermediate effects on PG fragment release and causes a slight defect in cell separation. In addition, the mutation amiCQ316K causes increased activity on whole sacculi and lysis of Escherichia coli cells
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additional information
deletion of the C-terminal region completely abolishes the lytic activity
additional information
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gene cwlB and upstream gene cwlA form one transcriptional unit, construction of the cwlA, cwlB, and cwlAB deletion mutants and genetic complementation of the cwlB deletion mutant
additional information
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construction of a deletion by gene replacement in Bacillus thuringiensis strain HD73. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Engineered Bacillus thuringiensis strains targeting cwlC allow the crystal inclusion to remain encapsulated in the mother cell at the end of sporulation. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis
additional information
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construction of a deletion by gene replacement in Bacillus thuringiensis strain HD73. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Engineered Bacillus thuringiensis strains targeting cwlC allow the crystal inclusion to remain encapsulated in the mother cell at the end of sporulation. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis
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additional information
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gene cwlB and upstream gene cwlA form one transcriptional unit, construction of the cwlA, cwlB, and cwlAB deletion mutants and genetic complementation of the cwlB deletion mutant
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additional information
a thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability, overview. A codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) from Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F which is identical to the PlyCP39O endolysin CWB domain from Clostridium phage phiCP39-O. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures
additional information
a codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) of Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F which is identical to the PlyCP39O endolysin CWB domain. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures
additional information
a thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability, overview. A codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) from Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures
additional information
N-terminal DELTA1-343 deletion mutant of PGRP-L with reduced activity, inactive C-terminal DELTA344-576 deletion mutant of PGRP-L
additional information
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N-terminal DELTA1-343 deletion mutant of PGRP-L with reduced activity, inactive C-terminal DELTA344-576 deletion mutant of PGRP-L
additional information
construction of deletion mutants DELTA1-322, DELTA323-555, and DELTA474-555
additional information
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construction of deletion mutants DELTA1-322, DELTA323-555, and DELTA474-555
additional information
generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery
additional information
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generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery
additional information
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generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery
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additional information
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generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery
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additional information
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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
construction of enzyme AmiC residues 29-159 fused to GB1, the AmiC-NTD construct contains four beta strands, followed by a single alpha-helix and then a further four beta-strands
additional information
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construction of enzyme AmiC residues 29-159 fused to GB1, the AmiC-NTD construct contains four beta strands, followed by a single alpha-helix and then a further four beta-strands
additional information
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generation of an enzyme deletion mutant DELTAamiC
additional information
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construction of enzyme AmiC residues 29-159 fused to GB1, the AmiC-NTD construct contains four beta strands, followed by a single alpha-helix and then a further four beta-strands
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additional information
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construction of enzyme AmiC residues 29-159 fused to GB1, the AmiC-NTD construct contains four beta strands, followed by a single alpha-helix and then a further four beta-strands
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additional information
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generation of an enzyme deletion mutant DELTAamiC
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additional information
none of the Glu578-variants shows enzyme activity, suggesting that this residue is indispensable for catalysis
additional information
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none of the Glu578-variants shows enzyme activity, suggesting that this residue is indispensable for catalysis
additional information
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none of the Glu578-variants shows enzyme activity, suggesting that this residue is indispensable for catalysis
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additional information
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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
additional information
construction of diverse truncation mutants of endolysin. The mutants lacking more than 200 C-terminal amino acids or the cell wall-binding domain are inactive, while N-terminal truncation mutant, or C-terminal truncation mutants lacking less than 200 amino acids still show lytic activity, although less than the wild-type enzyme
