3.4.11.7: glutamyl aminopeptidase
This is an abbreviated version!
For detailed information about glutamyl aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.7
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3.4.11.7
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apa
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aminopeptidases
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renin-angiotensin
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renin
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dipeptidyl
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hypertensive
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ras
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amastatin
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brush
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angiotensin-converting
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antihypertensive
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alanyl
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bestatin
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vasopressin
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pressor
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dipeptidylpeptidase
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losartan
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exopeptidase
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enpep
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arylamide
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intracerebroventricularly
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angiotensinogen
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medicine
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sucrase-isomaltase
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pyroglutamyl
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3.2.1.20
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puromycin-sensitive
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ras-regulating
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insulin-regulated
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oxytocinase
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kininase
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beta-naphthylamide
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microvillar
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synthesis
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diagnostics
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drug development
- 3.4.11.7
- apa
- aminopeptidases
-
renin-angiotensin
- renin
-
dipeptidyl
-
hypertensive
- ras
- amastatin
-
brush
-
angiotensin-converting
-
antihypertensive
-
alanyl
- bestatin
- vasopressin
-
pressor
-
dipeptidylpeptidase
- losartan
-
exopeptidase
- enpep
-
arylamide
-
intracerebroventricularly
- angiotensinogen
- medicine
- sucrase-isomaltase
-
pyroglutamyl
-
3.2.1.20
-
puromycin-sensitive
-
ras-regulating
-
insulin-regulated
- oxytocinase
-
kininase
- beta-naphthylamide
- microvillar
- synthesis
- diagnostics
- drug development
Reaction
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide =
Synonyms
acid aminopeptidase, acidic alpha-aminopeptidase, Aminopeptidase, aminopeptidase A, aminopeptidase A ectopeptidase, aminopeptidase, aspartate, aminopeptidase-A, angiotensinase, angiotensinase A, antigen BP-1/6C3 of mouse B lymphocytes, AP A, APA, Asp-AP, aspartate aminopeptidase, aspartyl aminopeptidase, aspartyl-aminopeptidase, BP-1, BP-1/6C3 antigen, BP1/6C3, Ca2+-activated glutamate aminopeptidase, Differentiation antigen gp160, EAP, ENPEP, GAP, GluAP, glutamyl (aspartyl)-specific aminopeptidase A, glutamyl aminopeptidase, glutamyl aminopeptidase (Lactococcus), glutamyl peptidase, glutamyl-aminopeptidase, glutamyl-AP, hAPA, L-alpha-aspartyl(L-alpha-glutamyl)-peptide hydrolase, L-aspartate aminopeptidase, LAP-A, Lb-PepA, Lc-PepA, leucine aminopeptidase A, M18 aspartyl aminopeptidase, mAPA, membrane aminopeptidase II, membrane-bound aspartyl-AP, MHJ_0125, More, N-terminal acidic amino acid-specific aminopeptidase, PepA, tricorn interacting factor F3, tricorn protease-interacting factor F3, type II Zn2+ membrane-bound aminopeptidase
ECTree
3.4.11.7 glutamyl aminopeptidaseAdvanced search results
results (
results (Source Tissue
Source Tissue on EC 3.4.11.7 - glutamyl aminopeptidase
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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GluAP is upregulated in osteogenic differentiated BMSC cells in vitro
activity is restricted to progenitor and precursor B cells. Enhanced BP-1 expression on virus-transformed pre-B cells and on normal pro-B cells stimulated by the interleukin 7 growth factor
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silver compounds tested show cytotoxicity against both U373-MG abd NB-69 cell lines. NB-69 cells need higher concentrations of silver complexes than U373-MG cells to obtain a 50% growth inhibition. The silver complexes tested also show a dose-dependent inhibitory effect on aminopeptidase A activity in NB-69 and U373-MG cells, although U373-MG cells are more sensitive
GAP activity in both the membrane-bound and soluble fractions is sharply decreased and its immunohistochemical expression shows mild staining in the histological types of renal tumours: clear-cell (CCRCC), papillary (PRCC) and chromophobe (ChRCC) renal cell carcinomas
GAP activity in both the membrane-bound and soluble fractions is sharply decreased and its immunohistochemical expression shows mild staining
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silver compounds tested show cytotoxicity against both U373-MG abd NB-69 cell lines. All compounds tested show apoptotic effects, with U373-MG cells being more susceptible. The silver complexes tested also show a dose-dependent inhibitory effect on aminopeptidase A activity in NB-69 and U373-MG cells, although U373-MG cells are more sensitive
additional information
while hyperthyroid rats exhibit lower levels of plasma AP A activity than controls, the kidney of hyperthyroid animals expresses significantly higher AP A than controls and hypothyroid animals. A discrepancy between the high expression of AP A in kidney of hyperthyroid rats and the low activity of AP A measured in plasma and kidney of hyperthyroid animals is found. The posttranslational influence of environmental biochemical factors may be in part responsible for that divergence
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while hyperthyroid rats exhibit lower levels of plasma AP A activity than controls, the kidney of hyperthyroid animals expresses significantly higher AP A than controls and hypothyroid animals. A discrepancy between the high expression of AP A in kidney of hyperthyroid rats and the low activity of AP A measured in plasma and kidney of hyperthyroid animals is found. The posttranslational influence of environmental biochemical factors may be in part responsible for that divergence
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bilateral distribution of aminopeptidases in stress-related areas, overview
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pericyte and almost all structures, hyperactive in RAS and SHR, distribution overview
immunoreactivity of APA in the medulla oblongata, the rostral ventrolateral medulla, and ambiguous nucleus
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immunoreactivity of APA in the medulla oblongata, the rostral ventrolateral medulla, and ambiguous nucleus
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the enzyme's ectodomain is cleaved in the kidney in to an N-terminal fragment, corresponding to the zinc metallopeptidase domain, and a C-terminal fragment
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urinary excretion of glutamyl aminopeptidase is increased in cisplatin-treated rats. Enzyme can be detected in urine samples with immunological methods, its excretion correlates with the extent of renal dysfunction in cisplatin-treated rats
additional information
immunohistochemic analysis and quantitative RT-PCR for detecting ENPEP mRNA in healthy and cancer cells, enzyme expression in the cancer cells is reduced compared to healthy cells
additional information
the Lb-PepA activity decreases during the stationary growth phase, which is caused by degradation of the enzyme
additional information
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the Lb-PepA activity decreases during the stationary growth phase, which is caused by degradation of the enzyme
additional information
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the Lb-PepA activity decreases during the stationary growth phase, which is caused by degradation of the enzyme
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additional information
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the enzyme is absent in the medulla and renal arterioles, distribution in renal tissues, overview
additional information
quantitative real-time PCR enzyme expression analysis
additional information
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the enzyme is absent in the medulla and renal arterioles, distribution in renal tissues, overview
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additional information
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tissue distribution of soluble and membrane enzyme activity, overview
additional information
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tissue distribution of soluble and membrane enzyme activity, overview
additional information
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tissue distribution of soluble and membrane enzyme activity, overview
