Information on EC 3.4.19.11 - gamma-D-glutamyl-meso-diaminopimelate peptidase

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The expected taxonomic range for this enzyme is: Lysinibacillus sphaericus

EC NUMBER
COMMENTARY
3.4.19.11
-
RECOMMENDED NAME
GeneOntology No.
gamma-D-glutamyl-meso-diaminopimelate peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hydrolysis of gamma-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted
show the reaction diagram
position 7
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-
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Endopeptidase I
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-
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gamma-D-Glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase
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-
-
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gamma-D-Glutamyl-meso-D-aminopimelic endopeptidase
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-
-
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gamma-D-Glutamyl-meso-diaminopimelate endopeptidase
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-
-
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gamma-D-Glutamyl-meso-diaminopimelic endopeptidase
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-
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gamma-D-Glutamyl-meso-diaminopimelic peptidoglycan hydrolase
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-
-
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gamma-Glutamyl-L-meso-diaminopimelyl endopeptidase
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-
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Hydrolase, gamma-D-glutamyl-(L)-meso-diaminopimelate peptidoglycan
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Peptidase, gamma-D-glutamyldiaminopimelate endo-
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-
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CAS REGISTRY NUMBER
COMMENTARY
62572-28-5
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-Acetylglucosamine-N-acetylmuramoyl-L-Ala-D-Glu-[-(L)-meso-diaminopimelic acid-D-Ala]NH2 + H2O
?
show the reaction diagram
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-
-
-
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N-Acetylmuramoyl-L-Ala-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala + H2O
N-Acetylmuramoyl-L-Ala-D-Glu + meso-diaminopimelic acid-(L)-D-Ala
show the reaction diagram
Lysinibacillus sphaericus, Lysinibacillus sphaericus 9602
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best substrate
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-
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N-Acetylmuramoyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala + H2O
N-Acetylmuramoyl-L-Ala-gamma-D-Glu + meso-diaminopimelic acid-(L)-D-Ala
show the reaction diagram
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-
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N-Acetylmuramoyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala + H2O
N-Acetylmuramoyl-L-Ala-gamma-D-Glu + meso-diaminopimelic acid-(L)-D-Ala
show the reaction diagram
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-
-
-
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additional information
?
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Lysinibacillus sphaericus, Lysinibacillus sphaericus 9602
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hydrolysis of substrates containing D-Glu-meso-diaminopimelic-acid with free omega-NH2 and omega-COOH groups, the presence or absence of an alpha-amide group on glutamic acid, the second residue of peptides, has no influence on the specificity. N-Substitution of N-terminal L-Ala does not modify the enzymic specificity. An amide group on glutamic acid gives an decrease of 80% of activity
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METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
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activates apoenzyme, maximal activation at 0.0002 mM
Mn2+
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activates apoenzyme, maximal activation at 0.0001 mM
Zn2+
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the enzyme contains one equivalent Zn2+ per mol of protein; zinc-binding triad His69-Glu72-His196; zinc enzyme
Zn2+
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activates apoenzyme; maximal activation at 0.0002 mM; zinc-binding triad His69-Glu72-His196; zinc enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
DD-Diaminopimelic acid isomers
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-
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Dicarboxylic D-amino acids
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inhibition is a function of length, maximum at n=4
EDTA
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reactivation by zinc, cobalt and manganese ions
meso-diaminopimelic acid isomers
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o-phenanthroline
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reactivation by zinc, cobalt and manganese ions
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Detergents
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enhance activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.99
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N-acetylglucosamine-N-acetylmuramoyl-L-Ala-D-Glu-[-(L)-meso-diaminopimelic acid-D-Ala]NH2
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immobilized enzyme
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4.34
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N-acetylglucosamine-N-acetylmuramoyl-L-Ala-D-Glu-[-(L)-meso-diaminopimelic acid-D-Ala]NH2
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native enzyme
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0.33
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N-Acetylmuramoyl-L-Ala-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala
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-
0.57
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N-Acetylmuramoyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala
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enzyme from sporulation medium
0.8
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N-Acetylmuramoyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala
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enzyme from spores
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
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enzyme from sporulation medium
13.9
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enzyme from spores
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-
native and immobilized enzyme
additional information
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-
pI: 5.4
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Lysinibacillus sphaericus 9602
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bound
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 45000, Bacillus sphaericus, SDS-PAGE
?
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in the absence of SDS, the enzyme aggregates to an enzymatically active dimer (MW 90000) which could be the native form of the enzyme
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
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stable for 45 days
55
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10 min, 2% loss of activity
65
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10 min, 3% loss of activity
75
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10 min, 13% loss of activity
75
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inactivation temperature of immobilized enzyme
80
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inactivation temperature of native enzyme
85
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10 min, 88% loss of activity
95
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10 min, 99% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, stable for months
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE