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
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
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SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Endopeptidase I
-
-
-
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gamma-D-Glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase
-
-
-
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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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-
-
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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
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
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
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
COMMENTARY
LITERATURE
IMAGE
Detergents
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enhance activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.99
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
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
N-Acetylmuramoyl-L-Ala-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala
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-
0.57
N-Acetylmuramoyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala
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enzyme from sporulation medium
0.8
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]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
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enzyme from sporulation medium
13.9
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enzyme from spores
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
native and immobilized enzyme
additional information
-
pI: 5.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
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
COMMENTARY
LITERATURE
?
-
in the absence of SDS, the enzyme aggregates to an enzymatically active dimer (MW 90000) which could be the native form of the enzyme
?
-
x * 45000, Bacillus sphaericus, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
stable for 45 days
29020
55
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10 min, 2% loss of activity
29020
65
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10 min, 3% loss of activity
29020
75
-
10 min, 13% loss of activity
29020
75
-
inactivation temperature of immobilized enzyme
29022
80
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inactivation temperature of native enzyme
29022
85
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10 min, 88% loss of activity
29020
95
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10 min, 99% loss of activity
29020
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE