Literature summary for 3.4.17.21 extracted from

Mesters, J.R.; Barinka, C.; Li, W.; Tsukamoto, T.; Majer, P.; Slusher, B.S.; Konvalinka, J.; Hilgenfeld, R.
Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer (2006), EMBO J., 25, 1375-1384.

Search for more literature for 3.4.17.21

Application

Application	Comment	Organism
pharmacology	the enzyme is a drug target in neuronal damage and prostate cancer	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
genetic structure, overview	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
2-(phosphonomethyl)-pentanedioic acid	i.e. 2-PMPA	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Homo sapiens	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	zinc-metalloenzyme, 2 Zn2+ bound per active site	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O	Homo sapiens	the essential enzyme is involved in prostate cancer, stroke, amyotrophic lateral sclerosis, and neuropathic pain	N-acetyl-alpha-L-aspartate + L-glutamate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q04609	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	10 possible N-glycosylation sites	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates	substrate recognition and induced-fit substrate binding mode, active site structure, catalytic mechanism involving Glu424	Homo sapiens	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	-	Homo sapiens	-
prostate cancer cell	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O	the essential enzyme is involved in prostate cancer, stroke, amyotrophic lateral sclerosis, and neuropathic pain	Homo sapiens	N-acetyl-alpha-L-aspartate + L-glutamate	-	?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O	i.e. NAAG, C-terminal glutamate recognition	Homo sapiens	N-acetyl-alpha-L-aspartate + L-glutamate	-	?

Subunits

Subunits	Comment	Organism
dimer	homodimer, the enzyme folds into three domains: a protease-like, an apical, and a C-terminal domain which are all involved in substrate binding, three-dimensional structure analysis, crystal structure	Homo sapiens

Synonyms

Synonyms	Comment	Organism
GCPII	-	Homo sapiens