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3.4.17.21: Glutamate carboxypeptidase II

This is an abbreviated version!
For detailed information about Glutamate carboxypeptidase II, go to the full flat file.

Word Map on EC 3.4.17.21

Reaction

release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates =

Synonyms

100 kDa ileum brush border membrane protein, Acetylaspartylglutamate dipeptidase, altered meristem program1, AMP1, Dipeptidase, acetylaspartylglutamate, EC 3.4.19.8, FGCP, folate hydrolase, folate hydrolase 1, FOLH1, Folylpoly-gamma-glutamate carboxypeptidase, folylpoly-gamma-glutamate carboxypeptidase II, GCP II, GCPII, GCPIII, glutamate carboxypeptidase, glutamate carboxypeptidase II, glutamate carboxypeptidase III, GPCPII, I100, Ileal dipeptidylpeptidase, Membrane glutamate carboxypeptidase, mGCP, More, N-acetyl-alpha-linked acidic dipeptidase, N-acetyl-alpha-linked acidic dipeptidase I, N-acetylaspartylglutamate peptidase, N-acetylated alpha-linked acid dipeptidase, N-Acetylated alpha-linked acidic dipeptidase, N-Acetylated-alpha-linked acidic dipeptidase, N-acetylated-alpha-linked acidic dipeptidase 2, N-acetylated-alpha-linked acidic dipeptidase II, N-Acetylated-alpha-linked-acidic dipeptidase, N-acetylated-alpha-linked-acidic-dipeptidase, N-Acetylated-alpha-linked-amino dipeptidase, NAADLADase, NAADLADse, NAAG degradation enzyme, NAAG peptidase, NAAG peptidase II, NAAG-hydrolyzing activity, NAALA dipeptidase, NAALADase, Naaladase I, NAALADase II, NLD I, PMSA, prostate specific membrane antigen, Prostate-specific membrane antigen, Prostate-specific membrane antigen homolog, prostate-specificmembrane antigen, Prostrate-specific membrane antigen, PSM, PSM antigen, PSMA, Pteroylpoly-gamma-glutamate carboxypeptidase, Rat NAAG peptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.21 Glutamate carboxypeptidase II

Crystallization

Crystallization on EC 3.4.17.21 - Glutamate carboxypeptidase II

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GCPIII ectodomain in a pseudo-unliganded state and in a complex with product L-glutamate, or the phosphapeptide transition state mimetic (2S,3'S)-[[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl]-pentanedioic acid, or quisqualic acid, a glutamate biostere, X-ray diffraction structure determination and analysis at 1.29-1.56 A resolution, modelling
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hanging-drop vapor-diffusion method, crystal structures of human glutamate carboxypeptidase II in complex with a series of phosphoramidate-based inhibitors harboring effector functions of diverse physicochemical characteristics
in complex with inhibitors N-2-([(1S)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine, N-2-([(1S)-1-carboxybut-3-yn-1-yl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine, and N-([(1S)-1-carboxy-5-([(4-iodophenyl)carbonyl]amino)pentyl]carbamoyl)-L-glutamic acid, PDB entries 4OC2, 4OC3, and 3D7H, respectively
prostate-specific membrane antigen crystal structure analysis
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purified recombinant extracellular portion of the enzyme, comprising residues 44-750, in complex with GPI-18431, a iodobenzyl derivative of inhibitor 2-PMPA, hanging drop vapour diffusion method, room temperature, 0.002 ml protein solution, containing 0.2 mM GPI-18431, is mixed with 0.002 ml well solution containing 20 mM HEPES, pH 7.5, 0.2 M NaCl, 5% w/v PEG 400, and 15%w/v PEG 1500, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution
purified recombinant His6-tagged extracellular portion, which contains bound Zn2+, hanging drop vapour diffusion method, 0.0008 ml of 10 mg/ml protein in 20 mM Tris, pH 7.5, is mixed with an equal volume of reservoir solution containing 18% PEG 3350, 0.2 M sodium thiocyanate, 4°C, cryoprotection by 20% glycerol, X-ray diffrcation structure determination and analysis at 3.5 A resolution
the crystal structure of GCPII(E424A) in complex with N-acetyl-L-aspartyl-L-glutamate is determined at 1.70 A resolution
the structures of human GCPII in complex with (S)-2-(3-((R)-1-carboxy-(2-methylthio)ethyl)ureido)pentanedioic acid, (S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid, (S)-2-(3-((R)-1-carboxy-2-(4-fluorobenzylthio)ethyl)ureido)pentanedioic acid and (S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid are solved to a resolution of 1.75, 1.54, 1.69 and 1.55 A, respectively
X-ray crystal structure of glutamate carboxypeptidase II in complex with (S)-2-(3-((S)-1-carboxy-5-(1,2-dicarba-closo-dodecarboranylamido) pentyl)ureido)pentanedioic acid at 1.79 A resolution. The X-ray analysis reveals that the bulky closo-carborane cluster is located in the spacious entrance funnel region of the enzyme, indicating that the carborane cluster can be further structurally modified to identify promising lead structures of novel glutamate carboxypeptidase II inhibitors
X-ray structure of human glutamate carboxypeptidase II in complex with hydroxamate-based inhibitors
X-ray structure of the inactive enzyme with the engineered mutation E424A in complex with beta-citrylglutamate, hanging drop vapour diffusion method
X-ray structures of seven complexes of the hydrolytically inactive recombinant E424A mutant and polyglutamylated folates substrates, refined at resolutions of between 1.65 and 2.00 A, and mutant H475Y, in complex with substrate N-acetyl-L-aspartyl-L-glutamate to 1.83 A resolution