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Information on EC 3.5.1.28 - N-acetylmuramoyl-L-alanine amidase and Organism(s) Homo sapiens and UniProt Accession Q96PD5
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3.5.1.28 N-acetylmuramoyl-L-alanine amidaseSpecify your search results
Word Map
- 3.5.1.28
- endolysins
- staphylococcus
- aureus
- autolysins
- streptococcus
- listeria
- pneumococcal
-
bacteriolytic
- murein
-
autolytic
-
holins
- prophage
- muropeptides
-
pgrps
-
wall-binding
-
teichoic
- lysostaphin
- transglycosylase
-
histidine-dependent
-
n-acetylmuramidase
-
choline-containing
-
bacteriophage-encoded
-
diaminopimelic
- muramidase
- siphoviridae
-
phage-encoded
- n-acetylglucosaminidase
-
endo-beta-n-acetylglucosaminidase
- lysodeikticus
- drug development
- agriculture
- diagnostics
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
n-acetylmuramoyl-l-alanine amidase, pglyrp2, cell wall hydrolase, t7 lysozyme, n-acetylmuramyl-l-alanine amidase, phage endolysin, namlaa, pgrp-l, cwlj1, peptidoglycan amidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylmuramoyl-alanine amidase
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-
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acetylmuramyl-alanine amidase
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acetylmuramyl-L-alanine amidase
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-
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Autolysin
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-
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Cell wall hydrolase
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-
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Lytic amidase
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-
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Mucopeptide aminohydrolase
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murein hydrolase
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N-acetylmuramic acid L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase type I
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N-acetylmuramoyl-L-alanine amidase type II
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N-acetylmuramyl-L-alanine amidase
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N-acetylmuramylalanine amidase
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N-acylmuramyl-L-alanine amidase
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ORFL3
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-
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T3 lysozyme
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T7 lysozyme
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9013-25-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
MurNAc-L-Ala-D-isoGln-L-Lys + H2O
MurNAc + L-Ala-D-isoGln-L-Lys
MurNAc-tripeptide, minimum peptidoglycan fragment hydrolyzed by PGRP-L
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-
?
MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala + H2O
MurNAc + L-Ala-D-isoGln-L-Lys-D-Ala
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-
-
?
N-acetylmuramoyl-L-alanine + H2O
N-acetylmuramate + L-alanine
the enzyme hydrolyzes bacterial peptidoglycan
-
-
?
peptidoglucan + H2O
?
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
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-
?
GlcNAc-MurNAc-L-Ala-D-isoGIn-meso-diaminopimelyl-(D)-amide-(L)-D-Ala-D-Ala + H2O
?
-
-
-
-
?
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
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-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
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-
-
-
?
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diaminopimelic acid + H2O
?
-
N-acetylmuramoyl-L-alanyl-D-gamma-glutaminyl-meso-diamino [3,4,5-3H]pimelic acid (3H-MTP)
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-
?
additional information
?
-
PGRP-L has no direct bacteriolytic activity for intact bacteria, not: MurNAc-L-Ala-D-isoGln, GlcNAc-MurNAc-L-Ala-D-isoGln
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-
?
additional information
?
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PGRP-L has no direct bacteriolytic activity for intact bacteria, not: MurNAc-L-Ala-D-isoGln, GlcNAc-MurNAc-L-Ala-D-isoGln
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
complete inhibition, restored by 1 mM Zn2+, partially restored by 10 mM Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
GlcNAc-MurNAc-L-Ala-D-isoGIn-meso-diaminopimelyl-(D)-amide-(L)-D-Ala-D-Ala
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
recombinant PGRP-L shows primarily intracellular and cell surface location
recombinant PGRP-L shows primarily intracellular and cell surface location
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PGRP2_HUMAN
576
0
62217
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
peptide mapping and immunospecificity analysis of enzyme proteins, overview
additional information
-
peptide mapping and immunospecificity analysis of enzyme proteins, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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
-
construction of deletion mutants DELTA1-322, DELTA323-555, and DELTA474-555
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mollner, S.; Braun, V.
Murein hydrolase (N-acetyl-muramyl-L-alanine amidase) in human serum
Arch. Microbiol.
140
171-177
1984
Homo sapiens
Valinger, Z.; Ladesic, B.; Tomasic, J.
Partial purification and characterization of N-acetylmuramyl-L-alanine amidase from human and mouse serum
Biochim. Biophys. Acta
701
63-71
1982
Homo sapiens, Mus musculus
Hoijer, M.A.; Melief, M.J.; Calafat, J.; Roos, D.; van den Beemd, R.W.M.; van Dongen, J.J.M.; Hazenberg, M.P.
Expression and intracellular localization of the human N-acetylmuramyl-L-alanine amidase, a bacertial cell wall-degrading enzyme
Blood
90
1246-1254
1997
Homo sapiens
Hoijer, M.A.; Melief, M-J.; Keck, W.; Hazenberg, M.P.
Purification and characterization of N-acetylmuramyl-L-alanine amidase from human plasma using monoclonal antibodies
Biochim. Biophys. Acta
1289
57-64
1996
Homo sapiens
Vanderwinkel, E.; De Vlieghere, M.; De Pauw, P.; Cattalini, N.; Ledoux, V.; Gigot, D.; Ten Have, J.P.
Purification and characterization of N-acetylmuramoyl-L-alanine amidase from human serum
Biochim. Biophys. Acta
1039
331-338
1990
Homo sapiens
De Pauw, P; Neyt, C.; Vanderwinkel, E.; Wattiez, R.; Falmagne, P.
Characterization of human serum N-acetylmuramyl-L-alanine amidase purified by affinity chromatography
Protein Expr. Purif.
6
371-378
1995
Homo sapiens
Wang, Z.M.; Li, X.; Cocklin, R.R.; Wang, M.; Fukase, K.; Inamura, S.; Kusumoto, S.; Gupta, D.; Dziarski, R.
Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-L-alanine amidase
J. Biol. Chem.
278
49044-49052
2003
Homo sapiens (Q96PD5), Homo sapiens
Zhang, Y.; Van der Fits, L.; Voerman, J.S.; Melief, M.; Laman, J.D.; Wang, M.; Wang, H.; Wang, M.; Li, X.; Walls, C.D.; Gupta, D.; Dziarski, R.
Identification of serum N-acetylmuramoyl-L-alanine amidase as liver peptidoglycan recognition protein 2
Biochim. Biophys. Acta
1752
34-46
2005
Homo sapiens (Q96PD5), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 3.5.1.28)
Transporter Classification Database (TCDB): 1.C.105.2.7, 1.C.105.2.6
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