Information on EC 3.5.1.82 - N-acyl-D-glutamate deacylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.82
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RECOMMENDED NAME
GeneOntology No.
N-acyl-D-glutamate deacylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amides
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SYSTEMATIC NAME
IUBMB Comments
N-acyl-D-glutamate amidohydrolase
The enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.
CAS REGISTRY NUMBER
COMMENTARY hide
82249-69-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 5f-1
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Glycyl-D-Glu + H2O
Gly + D-Glu
show the reaction diagram
N-Acetyl-D-Glu + H2O
acetate + D-Glu
show the reaction diagram
N-acetyl-D-glutamate + H2O
acetate + D-glutamate
show the reaction diagram
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?
N-Butyl-D-Glu + H2O
Butanoate + D-Glu
show the reaction diagram
N-Chloroacetyl-D-Glu + H2O
Chloroacetate + D-Glu
show the reaction diagram
N-Formyl-D-Glu + H2O
Formate + D-Glu
show the reaction diagram
N-Propionyl-D-Glu + H2O
Propanoate + D-Glu
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-glutamate + H2O
acetate + D-glutamate
show the reaction diagram
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?
additional information
?
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the enzyme is inducibly produced by D-isomers of N-acetylglutamate, Glu, Asp, and Asn
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
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stabilizes partially at 1 mM
Co2+
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stabilizes, optimal at 1 mM, no activation of enzymic activity
Mg2+
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stabilizes partially at 1 mM
Zinc
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contains 2.06-2.61 gatom of Zn per mol of enzyme. The zinc atom is required for the catalytic activity and stability
Zn2+
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required, D-AGase is a zinc-metalloenzyme, stabilizes partially, no activation of enzymic activity
additional information
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effects on enzyme stability by metal ions, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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rapid inactivation even at an alkaline pH, 9.3
N-acetyl-DL-glutamate
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substrate inhibition at high concentration, 94% inhibition at 1 M, the inhibition is reduced by Co2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-Trinitrobenzene-1-sulfonate
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1 mM, 13% inhibition
2-oxoglutarate
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4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
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1 mM, 22% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
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1 mM, 10% inhibition
acetate
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diethyl dicarbonate
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1 mM, 86% inhibition. Protected by N-acetyl-D Glu or 2-oxo-ketoglutarate
diisopropyl fluorophosphate
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1 mM, 15% inhibition
glyoxylate
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N-Acetylimidazole
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1 mM, 21% inhibition
PCMB
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1 mM, 18% inhibition
Phenylglyoxal
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1 mM, 46% inhibition
phenylmethylsulfonyl fluoride
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1 mM, 40% inhibition
tosyl-L-lysine chloromethyl ketone
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1 mM, 30% inhibition
tosyl-L-phenylalanine chloromethyl ketone
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1 mM, 39% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.67
N-Acetyl-D-Glu
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38.1
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soluble recombinant enzyme from expression without chaperones and trigger factor
95.8
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soluble recombinant enzyme from co-expression with chaperones and trigger factor
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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gel filtration
49000
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gel filtration
51490
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x * 51490, calculation from nucleotide sequence
55000
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1 * 55000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 51490, calculation from nucleotide sequence; x * 59000, SDS-PAGE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 9.5
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45°C, quite stable, regardless of the presence or absence of MgCl2
31927
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
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10 min, in absence of a stabilizer, 50% loss of activity
45
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10 min, in absence of added metal ions, 60-70% loss of activity
48
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10 min, in presence of Mg2+, 50% loss of activity
additional information
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Zn2+ increases heat stability. Thermal stability increases about 10°C in the presence of Zn2+ or Co2+. The optimal concentration for Zn2+ at 45°C and pH 6.5 is 0.03-0.05 mM. The optimal concentration for Co2+ at 45°C, pH 6.5 is 1.0-2.0 mM
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Na+, K+, Mg2+, Ba2+ or glycerol stabilizes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression of active D-AGase in Escherichia coli strain JM109 or strain BL21 partially in inclusion bodies, co-expression of chaperones GroELS, DnaKJE, and trigger factor TF
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overexpression of D-AGase in Escherichia coli
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the deduced amino acid sequence of the cloned N-acyl-D-glutamate amidohydrolase shows high sequence homology with those of N-acyl-D-aspartate amidohydrolase, 46%, and D-aminoacylase, 47%, from Alcaligenes A-6
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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the enzyme is used for production of D-glutamate, Co2+ might be a useful additive for stabilization of the enzyme
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