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

RECOMMENDED NAMEGeneOntology No.
N-acyl-D-glutamate deacylaseGO:0047421

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysis of linear amides----

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
N-acyl-D-glutamate amidohydrolaseThe enzyme from Alcaligenes xylosoxydans subsp. xylosoxydans and Pseudomonas sp. is specific for N-acyl-D-glutamate. Requires zinc.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Amidase, long-chain acylglutamate----
D-AGase----
D-AGaseAchromobacter xylosoxidans--668056, 669735
Deacylase, long-chain-fatty-acyl-glutamate----
Deacylase, N-acyl-D-glutamate----
EC 3.5.1.55--related-
Long chain acyl aminoacylase----
N-acyl-D-glutamate amidohydrolase----
N-acyl-D-glutamate amidohydrolaseAchromobacter xylosoxidans--668056, 669735

CAS REGISTRY NUMBERCOMMENTARY
82249-69-2-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Achromobacter xylosoxidans-668056, 669735--Manually annotated by BRENDA team
Achromobacter xylosoxidanssubsp. xylosoxydans A-631924--Manually annotated by BRENDA team
Pseudomonas sp.-31927, 31928--Manually annotated by BRENDA team
Pseudomonas sp.strain 5f-131925, 31926--Manually annotated by BRENDA team
Pseudomonas sp. 5f-1strain 5f-131925--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
Glycyl-D-Glu + H2OGly + D-Glu
show the reaction diagram		Pseudomonas sp.--31928---
N-Acetyl-D-Glu + H2Oacetate + D-Glu
show the reaction diagram		Pseudomonas sp.--31925-31925-
N-Acetyl-D-Glu + H2Oacetate + D-Glu
show the reaction diagram		Pseudomonas sp.--31926-31926-
N-Acetyl-D-Glu + H2Oacetate + D-Glu
show the reaction diagram		Pseudomonas sp.--31928---
N-Acetyl-D-Glu + H2Oacetate + D-Glu
show the reaction diagram		Achromobacter xylosoxidans--31924-31924-
N-Acetyl-D-Glu + H2Oacetate + D-Glu
show the reaction diagram		Pseudomonas sp.-58% of the activity with N-formyl-D-Glu31927---
N-acetyl-D-glutamate + H2Oacetate + D-glutamate
show the reaction diagram		Achromobacter xylosoxidans--668056--?
N-Butyl-D-Glu + H2OButanoate + D-Glu
show the reaction diagram		Pseudomonas sp.--31928---
N-Butyl-D-Glu + H2OButanoate + D-Glu
show the reaction diagram		Pseudomonas sp.-21% of the activity with N-formyl-D-Glu31927---
N-Chloroacetyl-D-Glu + H2OChloroacetate + D-Glu
show the reaction diagram		Pseudomonas sp.--31928---
N-Chloroacetyl-D-Glu + H2OChloroacetate + D-Glu
show the reaction diagram		Pseudomonas sp.-7.5% of the activity with N-formyl-D-Glu31927---
N-Formyl-D-Glu + H2OFormate + D-Glu
show the reaction diagram		Pseudomonas sp.--31927---
N-Formyl-D-Glu + H2OFormate + D-Glu
show the reaction diagram		Pseudomonas sp.-most preferred substrate31928---
N-Propionyl-D-Glu + H2OPropanoate + D-Glu
show the reaction diagram		Pseudomonas sp.--31928---
N-Propionyl-D-Glu + H2OPropanoate + D-Glu
show the reaction diagram		Pseudomonas sp.-16% of the activity with N-formyl-D-Glu31927---
Glycyl-D-Glu + H2OGly + D-Glu
show the reaction diagram		Pseudomonas sp.-0.79% of the activity with N-formyl-D-Glu31927---
additional information?-Pseudomonas sp.-the enzyme is inducibly produced by D-isomers of N-acetylglutamate, Glu, Asp, and Asn31927---
additional information?-Achromobacter xylosoxidans-the enzyme is specific for N-acyl-D-glutamate669735---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
N-acetyl-D-glutamate + H2Oacetate + D-glutamate
show the reaction diagram		Achromobacter xylosoxidans--668056--
additional information?-Pseudomonas sp.-the enzyme is inducibly produced by D-isomers of N-acetylglutamate, Glu, Asp, and Asn31927--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ba2+Achromobacter xylosoxidans-stabilizes partially at 1 mM668056
Co2+Achromobacter xylosoxidans-stabilizes, optimal at 1 mM, no activation of enzymic activity668056
ZincPseudomonas sp.-contains 2.06-2.61 gatom of Zn per mol of enzyme. The zinc atom is required for the catalytic activity and stability31925
Zn2+Achromobacter xylosoxidans-required, D-AGase is a zinc-metalloenzyme, stabilizes partially, no activation of enzymic activity668056
Mg2+Achromobacter xylosoxidans-stabilizes partially at 1 mM668056
additional informationAchromobacter xylosoxidans-effects on enzyme stability by metal ions, overview668056

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1,10-phenanthrolinePseudomonas sp.-rapid inactivation even at an alkaline pH, 9.331925 2D-image
Cu2+Pseudomonas sp.--31925, 31927 2D-image
EDTAPseudomonas sp.-reactivation: Zn2+, 66%, Co2+, 40%, or Mn2+ 9%31925 2D-image
EDTAPseudomonas sp.--31927 2D-image
Fe2+Pseudomonas sp.--31925 2D-image
Fe3+Pseudomonas sp.--31927 2D-image
Hg2+Pseudomonas sp.--31927 2D-image
N-acetyl-DL-glutamateAchromobacter xylosoxidans-substrate inhibition at high concentration, 94% inhibition at 1 M, the inhibition is reduced by Co2+668056 2D-image
Zn2+Pseudomonas sp.--31925, 31927 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2,4,6-Trinitrobenzene-1-sulfonatePseudomonas sp.-1 mM, 13% inhibition31926 2D-image
2-oxoglutaratePseudomonas sp.--31926 2D-image
4-(2-Aminoethyl)benzenesulfonyl fluoride hydrochloridePseudomonas sp.-1 mM, 22% inhibition31926 2D-image
5,5'-dithiobis(2-nitrobenzoic acid)Pseudomonas sp.-1 mM, 10% inhibition31926 2D-image
acetatePseudomonas sp.--31927 2D-image
diethyl dicarbonatePseudomonas sp.-1 mM, 86% inhibition. Protected by N-acetyl-D Glu or 2-oxo-ketoglutarate31926 2D-image
diisopropyl fluorophosphatePseudomonas sp.-1 mM, 15% inhibition31926 2D-image
glyoxylatePseudomonas sp.--31926 2D-image
N-AcetylimidazolePseudomonas sp.-1 mM, 21% inhibition31926 2D-image
PCMBPseudomonas sp.-1 mM, 18% inhibition31926 2D-image
PhenylglyoxalPseudomonas sp.-1 mM, 46% inhibition31926 2D-image
phenylmethylsulfonyl fluoridePseudomonas sp.-1 mM, 40% inhibition31926 2D-image
tosyl-L-lysine chloromethyl ketonePseudomonas sp.-1 mM, 30% inhibition31926 2D-image
tosyl-L-phenylalanine chloromethyl ketonePseudomonas sp.-1 mM, 39% inhibition31926 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
6.67-N-Acetyl-D-GluPseudomonas sp.--31927 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
38.1-Achromobacter xylosoxidans-soluble recombinant enzyme from expression without chaperones and trigger factor669735
95.8-Achromobacter xylosoxidans-soluble recombinant enzyme from co-expression with chaperones and trigger factor669735
589-Pseudomonas sp.--31927
1100-Pseudomonas sp.--31928
additional information-Achromobacter xylosoxidans--668056

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6.57.5Pseudomonas sp.--31927
7-Achromobacter xylosoxidans-assay at668056

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
30-Achromobacter xylosoxidans-assay at668056
45-Pseudomonas sp.--31927

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
3gip, downloadSCOP (3gip)CATH (3gip)Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
3giq, downloadSCOP (3giq)CATH (3giq)Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
44000-Pseudomonas sp.-gel filtration31925, 31927
49000-Pseudomonas sp.-gel filtration31928

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Achromobacter xylosoxidans-x * 51490, calculation from nucleotide sequence; x * 59000, SDS-PAGE31924
monomerPseudomonas sp.-1 * 55000, SDS-PAGE31925, 31927
monomerPseudomonas sp.-1 * 59000, SDS-PAGE31928

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
99.5Pseudomonas sp.-45°C, quite stable, regardless of the presence or absence of MgCl231927

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
41-Pseudomonas sp.-10 min, in absence of a stabilizer, 50% loss of activity31927
45-Pseudomonas sp.-10 min, in absence of added metal ions, 60-70% loss of activity31925
48-Pseudomonas sp.-10 min, in presence of Mg2+, 50% loss of activity31927
additional information-Pseudomonas sp.-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 mM31925

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
Co2+ stabilizesAchromobacter xylosoxidans-668056
Na+, K+, Mg2+, Ba2+ or glycerol stabilizesPseudomonas sp.-31927

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Pseudomonas sp.-31925, 31927, 31928

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. 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 TFAchromobacter xylosoxidans-669735
overexpression of D-AGase in Escherichia coliAchromobacter xylosoxidans-668056
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-6Achromobacter xylosoxidans-31924

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisAchromobacter xylosoxidans-the enzyme is used for production of D-glutamate, Co2+ might be a useful additive for stabilization of the enzyme668056

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
31924Wakayama, M.; Ashika, T.; Miyamoto, Y.; Yoshikawa, T.; Sonoda, Y.; Sakai, K.; Moriguchi, M.Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6J. Biochem.118204-2091995Achromobacter xylosoxidans PubMed
31925Wakayama, M.; Miura, Y.; Oshima, K.; Sakai, K.; Moriguchi, M.Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1Biosci. Biotechnol. Biochem.591489-14921995Pseudomonas sp. PubMed
31926Wakayama, M.; Tsutsumi, T.; Yada, H.; Sakai, K.; Moriguchi, M.Chemical modification of histidine residue of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. 5f-1Biosci. Biotechnol. Biochem.60650-6531996Pseudomonas sp. PubMed
31927Sakai, K.; Oshima, K.; Moriguchi, M.Purification and characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1Appl. Environ. Microbiol.572540-25431991Pseudomonas sp. PubMed
31928Sakai, K.; Imamura, K.; Sonoda, Y.; Kido, H.; Moriguchi, M.Purification and characterization of N-acyl-D-glutamate deacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6FEBS Lett.28944-461991Pseudomonas sp. PubMed
668056Yoshimune, K.; Hirayama, A.; Moriguchi, M.A metal ion as a cofactor attenuates substrate inhibition in the enzymatic production of a high concentration of D-glutamate using N-acyl-D-glutamate amidohydrolaseBiotechnol. Lett.271325-13282005Achromobacter xylosoxidans PubMed
669735Yoshimune, K.; Ninomiya, Y.; Wakayama, M.; Moriguchi, M.Molecular chaperones facilitate the soluble expression of N-acyl-D-amino acid amidohydrolases in Escherichia coliJ. Ind. Microbiol. Biotechnol.31421-4262004Achromobacter xylosoxidans PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 3.5.1.82)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)