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

3.4.17.21

tomography

positron

metastases

psma-targeted

node

lncap

tracer

prostatectomy

castration-resistant

modal

radioligands

androgen

psma-positive

radiotherapy

radionuclide

68ga-psma

biodistribution

radiotracers

neovasculature

radiopharmaceutical

mcrpc

theranostic

pelvic

gleason

psma-expressing

suvmax

restaging

oligometastatic

68ga-labeled

multiparametric

urea-based

spect

dosimetry

scintigraphy

abiraterone

castrate-resistant

n-acetylaspartate

extraprostatic

mpmri

pet-ct

enzalutamide

18f-labeled

positron-emission

tomography-computed

radium-223

pharmacology

radioimmunotherapy

medicine

tumor-to-background

analysis

radiometals

postprostatectomy

per-patient

diagnostics

drug development

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

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
1	Activating Compound
189	AA Sequence
40	Application
1	CAS Registry Number
25	Cloned(Commentary)
12	Crystallization (Commentary)
7461	Disease/ Diagnostics
5	Expression
9	General Information
3	General Stability
121	IC50 Value
374	Inhibitors
4	kcat/KM [mM/s]
108	Ki Value [mM]
15	KM Value [mM]
83	Localization
41	Metals/Ions
8	Molecular Weight [Da]
62	Natural Substrates/ Products (Substrates)
128	Organism
2	Pathway
90	PDB ID
15	pH Optimum
2	pH Range
17	Posttranslational Modification
37	Protein Variants
14	Purification (Commentary)
4	Reaction
7	Reaction Type
126	Reference
230	Source Tissue
10	Specific Activity [micromol/min/mg]
144	Substrates and Products (Substrate)
10	Subunits
261	Synonyms
14	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Turnover Number [1/s]

Molecular Weight

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Molecular Weight on EC 3.4.17.21 - Glutamate carboxypeptidase II

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Molecular Weight Search

100000

2 entries

84000

Homo sapiens

calculation from sequence of cDNA, short intracellular domain, single transmembrane element, large glubular extracellular domain

137218

84490

Rattus norvegicus

sequence of cDNA, nonglycosylated enzyme form, the extracellular domain contains nine potential N- glycosylation sites

137215

85000

Rattus norvegicus

determined by SDS-PAGE and Western Blot analysis

94000

x * 94000, SDS-PAGE

97000

x * 97000, SDS-PAGE

additional information

Homo sapiens

domain structure, sequence alignment with transferrin receptor, the catalytic domain can be assigned to the peptidase family M28

137211