Aminopeptidases: A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.Methionyl Aminopeptidases: Aminopeptidases that remove METHIONINE from the amino-terminus of a peptide chain, such as the initiator METHIONINE found on nascent peptide chains.Leucyl Aminopeptidase: A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.Glutamyl Aminopeptidase: A ZINC-dependent membrane-bound aminopeptidase that catalyzes the N-terminal peptide cleavage of GLUTAMATE (and to a lesser extent ASPARTATE). The enzyme appears to play a role in the catabolic pathway of the RENIN-ANGIOTENSIN SYSTEM.Antigens, CD13: Zinc-binding metalloproteases that are members of the type II integral membrane metalloproteases. They are expressed by GRANULOCYTES; MONOCYTES; and their precursors as well as by various non-hematopoietic cells. They release an N-terminal amino acid from a peptide, amide or arylamide.Cystinyl Aminopeptidase: A zinc-containing sialoglycoprotein that is used to study aminopeptidase activity in the pathogenesis of hypertension. EC 3.4.11.3.Dipeptidyl-Peptidases and Tripeptidyl-Peptidases: A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Dipeptidases: EXOPEPTIDASES that specifically act on dipeptides. EC 3.4.13.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Pyroglutamyl-Peptidase I: An enzyme that catalyzes the release of a N-terminal pyroglutamyl group from a polypeptide provided the next residue is not proline. It is inhibited by thiol-blocking reagents and occurs in mammalian tissues, microorganisms, and plants. (From Enzyme Nomenclature, 1992) EC 3.4.19.3.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Metalloproteases: Proteases which use a metal, normally ZINC, in the catalytic mechanism. This group of enzymes is inactivated by metal CHELATORS.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Enkephalin, Leucine: One of the endogenous pentapeptides with morphine-like activity. It differs from MET-ENKEPHALIN in the LEUCINE at position 5. Its first four amino acid sequence is identical to the tetrapeptide sequence at the N-terminal of BETA-ENDORPHIN.Digestive System: A group of organs stretching from the MOUTH to the ANUS, serving to breakdown foods, assimilate nutrients, and eliminate waste. In humans, the digestive system includes the GASTROINTESTINAL TRACT and the accessory glands (LIVER; BILIARY TRACT; PANCREAS).Aeromonas: A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that occurs singly, in pairs, or in short chains. Its organisms are found in fresh water and sewage and are pathogenic to humans, frogs, and fish.Neprilysin: Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Dipeptidyl Peptidase 4: A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation.Dipeptides: Peptides composed of two amino acid units.Microvilli: Minute projections of cell membranes which greatly increase the surface area of the cell.Lepidoptera: A large order of insects comprising the butterflies and moths.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Oligopeptides: Peptides composed of between two and twelve amino acids.Hemolysin Proteins: Proteins from BACTERIA and FUNGI that are soluble enough to be secreted to target ERYTHROCYTES and insert into the membrane to form beta-barrel pores. Biosynthesis may be regulated by HEMOLYSIN FACTORS.Antigen Presentation: The process by which antigen is presented to lymphocytes in a form they can recognize. This is performed by antigen presenting cells (APCs). Some antigens require processing before they can be recognized. Antigen processing consists of ingestion and partial digestion of the antigen by the APC, followed by presentation of fragments on the cell surface. (From Rosen et al., Dictionary of Immunology, 1989)Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Metals: Electropositive chemical elements characterized by ductility, malleability, luster, and conductance of heat and electricity. They can replace the hydrogen of an acid and form bases with hydroxyl radicals. (Grant & Hackh's Chemical Dictionary, 5th ed)Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Drug Design: The molecular designing of drugs for specific purposes (such as DNA-binding, enzyme inhibition, anti-cancer efficacy, etc.) based on knowledge of molecular properties such as activity of functional groups, molecular geometry, and electronic structure, and also on information cataloged on analogous molecules. Drug design is generally computer-assisted molecular modeling and does not include pharmacokinetics, dosage analysis, or drug administration analysis.Kinetics: The rate dynamics in chemical or physical systems.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Endotoxins: Toxins closely associated with the living cytoplasm or cell wall of certain microorganisms, which do not readily diffuse into the culture medium, but are released upon lysis of the cells.Zinc: A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.Bacterial Proteins: Proteins found in any species of bacterium.Histocompatibility Antigens Class I: Membrane glycoproteins consisting of an alpha subunit and a BETA 2-MICROGLOBULIN beta subunit. In humans, highly polymorphic genes on CHROMOSOME 6 encode the alpha subunits of class I antigens and play an important role in determining the serological specificity of the surface antigen. Class I antigens are found on most nucleated cells and are generally detected by their reactivity with alloantisera. These antigens are recognized during GRAFT REJECTION and restrict cell-mediated lysis of virus-infected cells.Cations, Divalent: Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

Kidney aminopeptidase A and hypertension, part I: spontaneously hypertensive rats. (1/1462)

Tissue and plasma levels of aminopeptidase A (APA), the principal enzyme that hydrolyzes angiotensin II (Ang II) to angiotensin III, were measured in spontaneously hypertensive rats (SHR) and their normotensive control strain at 3 different ages corresponding to prehypertensive (4 weeks), developing (8 weeks), and established (16 weeks) phases of hypertension. Plasma APA activity was significantly but modestly elevated in SHR at all 3 ages compared with normotensive Wistar-Kyoto rats. Likewise, levels of APA in brain, heart, and adrenal gland were generally, but again only moderately, elevated in SHR at all ages. However, a large increase in APA activity was seen within the kidney in which APA levels were elevated 41%, 51%, and 68% in SHR at 4, 8, and 16 weeks of age, respectively. Kidney APA levels were also significantly increased in immunoblots from 8- and 16-week-old SHR. Glomeruli isolated from 16-week-old SHR had 57% higher APA activity and increased immunoreactivity compared with Wistar-Kyoto rats. To determine whether the increase in kidney APA activity in SHR was related to Ang II levels, SHR were treated for 2 weeks with the angiotensin-converting enzyme inhibitor captopril. Captopril treatment reduced blood pressure to normotensive values and resulted in a 25% reduction in kidney APA activity. These results suggest that APA expression in the kidney may be regulated by activity of the renin-angiotensin system. If so, this would further suggest that upregulation of APA during conditions in which Ang II levels were elevated would have a protective effect against Ang II-mediated cardiovascular diseases, whereas a decrease in APA expression or a failure to upregulate would exacerbate such conditions.  (+info)

Kidney aminopeptidase A and hypertension, part II: effects of angiotensin II. (2/1462)

Aminopeptidase A (APA) is the principal enzyme that metabolizes angiotensin II (Ang II) to angiotensin III. Previously, we showed that kidney APA was elevated in spontaneously hypertensive rats and was reduced after angiotensin-converting enzyme inhibition. In the present study, we sought to determine whether kidney APA expression was altered after chronically elevated Ang II, either exogenously delivered via osmotic minipumps or endogenously produced in two-kidney, one clip (2K1C) hypertensive rats. Ang II (200 ng. kg-1. min-1) was infused subcutaneously for 1 or 2 weeks by osmotic minipumps, and 2K1C rats were tested 4 weeks after unilateral renal artery clipping. Blood pressure was not significantly elevated in the Ang II-infused animals but was significantly increased at 3 and 4 weeks in the 2K1C animals. APA was significantly elevated approximately 2-fold in kidney cortical membranes from Ang II-infused animals but was decreased 45% in the clipped kidney and 18% in the nonclipped kidneys from 2K1C animals. Isolated glomeruli from Ang II-infused animals and the nonclipped kidneys from 2K1C animals had markedly higher APA activity and immunoreactivity. Likewise, histochemical and immunohistochemical studies indicated that APA levels were increased in glomeruli from angiotensin-infused animals and in both nonclipped and clipped kidneys from 2K1C animals. In contrast, tubular APA was decreased in tubular elements from 2K1C animals, most markedly in the clipped kidneys. Thus, despite the increase in glomerular APA expression in kidneys from 2K1C animals, the decrease in tubular APA expression is more extensive and accounts for the measured reduction in total APA in cortical homogenates. Because clipped kidneys are not exposed to high blood pressure, these results suggest that glomerular APA expression is positively regulated and tubular APA negatively regulated by Ang II. These results further suggest that changes in kidney APA expression could influence the progression of angiotensin-dependent hypertension.  (+info)

Co-expression of glutathione S-transferase with methionine aminopeptidase: a system of producing enriched N-terminal processed proteins in Escherichia coli. (3/1462)

We describe here an Escherichia coli expression system that produces recombinant proteins enriched in the N-terminal processed form, by using glutathione S-transferase cGSTM1-1 and rGSTT1-1 as models, where c and r refer to chick and rat respectively. Approximately 90% of the cGSTM1-1 or rGSTT1-1 overexpressed in E. coli under the control of a phoA promoter retained the initiator methionine residue that was absent from the mature isoenzymes isolated from tissues. The amount of initiator methionine was decreased to 40% of the expressed cGSTM1-1 when the isoenzyme was co-expressed with an exogenous methionine aminopeptidase gene under the control of a separate phoA promoter. The recombinant proteins expressed were mainly methionine aminopeptidase. The yield of cGSTM1-1 was decreased to 10% of that expressed in the absence of the exogenous methionine aminopeptidase gene. By replacing the phoA with its natural promoter, the expression of methionine aminopeptidase decreased drastically. The yield of the co-expressed cGSTM1-1 was approx. 60% of that in the absence of the exogenous methionine aminopeptidase gene; approx. 65% of the initiator methionine residues were removed from the enzyme. Under similar conditions, N-terminal processing was observed in approx. 70% of the recombinant rGSTT1-1 expressed. By increasing the concentration of phosphate in the growth medium, the amount of initiator methionine on cGSTM1-1 was decreased to 14% of the overexpressed isoenzymes, whereas no further improvement could be observed for rGSTT1-1. The initiator methionine residue does not affect the enzymic activities of either cGSTM1-1 or rGSTT1-1. However, the epoxidase activity and the 4-nitrobenzyl chloride-conjugating activity of the purified recombinant rGSTT1-1 are markedly higher that those reported recently for the same isoenzyme isolated from rat livers.  (+info)

Endothelin stimulates glucose uptake and GLUT4 translocation via activation of endothelin ETA receptor in 3T3-L1 adipocytes. (4/1462)

Endothelin-1 (ET-1) is a 21-amino acid peptide that binds to G-protein-coupled receptors to evoke biological responses. This report studies the effect of ET-1 on regulating glucose transport in 3T3-L1 adipocytes. ET-1, but not angiotensin II, stimulated glucose uptake in a dose-dependent manner with an EC50 value of 0.29 nM and a 2.47-fold stimulation at 100 nM. ET-1 stimulated glucose uptake in differentiated 3T3-L1 cells but had no effect in undifferentiated cells, although ET-1 stimulated phosphatidylinositol hydrolysis to a similar degree in both. The 3T3-L1 cells expressed approximately 560,000 sites/cell of ETA receptor, which was not altered during differentiation. Western blot analysis and immunofluorescence staining show that ET-1 stimulated the translocation of insulin-responsive aminopeptidase and GLUT4 to the plasma membrane. The effect of ET-1 on glucose uptake was blocked by A-216546, an antagonist selective for the ETA receptor. ET-1 treatment did not induce phosphorylation of insulin receptor beta-subunit, insulin receptor substrate-1, or Akt but stimulated the tyrosyl phosphorylation of a 75-kDa protein. Genistein (100 microM), an inhibitor of tyrosine kinases, inhibited ET-1-stimulated glucose uptake. Our results show that ET-1 stimulates GLUT4 translocation and glucose uptake in 3T3-L1 adipocytes via activation of ETA receptor.  (+info)

Identification of kallidin degrading enzymes in the isolated perfused rat heart. (5/1462)

Kallidin (KD) is an important vasoactive kinin whose physiological effects are strongly dependent on its degradation through local kininases. In the present study, we examined the spectrum of these enzymes and their contribution to KD degradation in isolated perfused rat hearts. By inhibiting angiotensin-converting enzyme (ACE), aminopeptidase M (APM) and neutral endopeptidase (NEP) with ramiprilat (0.25 microM), amastatin (40 microM) and phosphoramidon (1 microM), respectively, relative kininase activities were obtained. APM (44%) and ACE (35%) are the main KD degrading enzymes in rat heart; NEP (7%) plays a minor role. A participation of carboxypeptidase N (CPN) could not be found.  (+info)

Hydrolysis of alphas1- and beta-casein-derived peptides with a broad specificity aminopeptidase and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2. (6/1462)

Aminopeptidase hydrolysis of alpha(s)1 - and beta-casein-derived synthetic peptides containing non-consecutive and consecutive proline residues was characterised. Aminopeptidase P (Pep P) (EC 3.4.11.9) or post-proline dipeptidyl aminopeptidase (PPDA) (EC 3.4.14.5) along with lysine-paranitroanilide hydrolase (KpNA-H) (EC 3.4.11.1) activities are required in the degradation of peptides containing non-consecutive proline residues. However, both Pep P and PPDA along with KpNA-H are required for hydrolysis of peptides containing consecutive proline residues. The results demonstrate the mechanism by which combinations of purified general and proline specific aminopeptidases from Lactococcus lactis subsp. cremoris AM2 hydrolyse peptides containing proline residues.  (+info)

Cloning and functional expression of the cytoplasmic form of rat aminopeptidase P. (7/1462)

A rat cytoplasmic aminopeptidase P was purified from liver cytosol with a procedure including an affinity elution step with 3 microM inositol 1,3,4-trisphosphate. Proteolytic fragments were generated, sequenced and the enzyme was cloned from a rat liver cDNA library. The structure shows high (87.8% and 95.5%, respectively) sequence identity at the nucleotide and amino acid levels with the previously described human putative cytoplasmic aminopeptidase P. The cloned rat enzyme was functionally expressed in Escherichia coli and also in COS-1 cells. Western blot analysis, using an antibody generated against the recombinant protein, and Northern blot hybridization showed ubiquitous expression of the protein in different tissues with the highest expression level in the testis.  (+info)

Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. (8/1462)

Vp10p is a receptor that sorts several different vacuolar proteins by cycling between a late Golgi compartment and the endosome. The cytoplasmic tail of Vps10p is necessary for the recycling, whereas the lumenal domain is predicted to interact with the soluble ligands. We have studied ligand binding to Vps10p by introducing deletions in the lumenal region. This region contains two domains with homology to each other. Domain 2 binds carboxypeptidase Y (CPY), proteinase A (PrA) and hybrids of these proteases with invertase. Moreover, we show that aminopeptidase Y (APY) is a ligand of Vps10p. The native proteases compete for binding to domain 2. Binding of CPY(156)-invertase or PrA(137)-invertase, on the other hand, do not interfere with binding of CPY to Vps10p. Furthermore, the Q24RPL27 sequence known to be important for vacuolar sorting of CPY, is of little importance in the Vps10p-dependent sorting of CPY-invertase. Apparently, domain 2 contains two different binding sites; one for APY, CPY and PrA, and one for CPY-invertase and PrA-invertase. The latter interaction seems not to be sequence specific, and we suggest that an unfolded structure in these ligands is recognized by Vps10p.  (+info)

*Leucyl/cystinyl aminopeptidase

... , also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human ... end and chromosomal assignment of human placental leucine aminopeptidase/insulin-regulated membrane aminopeptidase gene". ... Leucine aminopeptidase". Acta genetica et statistica medica. 16 (2): 122-31. doi:10.1159/000151957. PMID 5953194. Itoh C, ... Mutations in this gene have been associated to psoriasis risk.(doi:10.1038/jid.2013.317) Cystinyl aminopeptidase has been shown ...

*Alanine aminopeptidase

... aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)". Yeager CL, Ashmun RA, Williams RK ... Membrane alanyl aminopeptidase (EC 3.4.11.2) also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme ... "Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N". Biological Chemistry ... Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract ...

*PEPD

However, biochemical and structural analyses of aminopeptidase (APPro), methionine aminopeptidase (MetAP), and prolidase, all ... enzyme with residue numbering corresponding to those found in methionine aminopeptidase from E. coli. As shown in Intermediate ... "Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the ...

*ARTS-1

ARTS1 is also known as: ER aminopeptidase 1 (ERAP1) the name accepted by the Hugo Gene Nomenclature Committee ER aminopeptidase ... Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator, also known as endoplasmic reticulum aminopeptidase 1 ( ... "Shedding of the Type II IL-1 Decoy Receptor Requires a Multifunctional Aminopeptidase, Aminopeptidase Regulator of TNF Receptor ... "Distribution of Adipocyte-derived Leucine Aminopeptidase (A-LAP)/ER-aminopeptidase (ERAP)-1 in Human Uterine Endometrium". ...

*DPP3

Vitale L, Zubanović M, Abramić M (1982). "Properties and distribution of aminopeptidase and dipeptidyl aminopeptidase III of ... Grdisa M, Vitale L (1991). "Types and localization of aminopeptidases in different human blood cells". Int. J. Biochem. 23 (3 ... Jones TH, Kapralou A (1982). "A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes". Anal. Biochem. 119 (2): ... Vanha-Perttula T (1989). "Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and ...

*Aminopeptidase

One important aminopeptidase is a zinc-dependent enzyme produced and secreted by glands of the small intestine. It helps the ... Aminopeptidases are enzymes that catalyze the cleavage of amino acids from the amino terminus (N-terminus) of proteins or ... Aminopeptidases are used in essential cellular functions. Many, but not all, of these peptidases are zinc metalloenzymes. Some ... Alanine aminopeptidase Carboxypeptidase PDB: 3QNF​: Vollmar, M.; Kochan, G.; Krojer, T.; Harvey, D.; Chaikuad, A.; Allerston, C ...

*Aminopeptidase Y

... (EC 3.4.11.15, aminopeptidase Co, aminopeptidase (cobalt-activated), lysyl aminopeptidase) is an enzyme. This ... Sequence analysis and gene disruption of a new aminopeptidase". J. Biol. Chem. 269: 13651-13655. PMID 8175800. Aminopeptidase Y ... Yasuhara, T.; Nakai, T.; Ohashi, A. (1994). "Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. Purification ... Nishizawa, M.; Yasuhara, T.; Nakai, T.; Fujiki, Y.; Ohashi, A. (1994). "Molecular cloning of the aminopeptidase Y gene of ...

*Prolyl aminopeptidase

... (EC 3.4.11.5, proline aminopeptidase, Pro-X aminopeptidase, cytosol aminopeptidase V, proline ... Prolyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Turzynski, A.; Mentlein, R. (1990). "Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as ... leucyl aminopeptidase". Eur. J. Biochem. 190: 509-515. doi:10.1111/j.1432-1033.1990.tb15603.x. PMID 2373079. ...

*Methionyl aminopeptidase

... (EC 3.4.11.18, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme ... Methionyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Roderick SL, Matthews BW (1988). "Crystallization of methionine aminopeptidase from Escherichia coli". J. Biol. Chem. 263: ... Freitas JO, Termignoni C, Guimarães JA (1985). "Methionine aminopeptidase associated with liver mitochondria and microsomes". ...

*Tripeptide aminopeptidase

... at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Doumeng, C.; Maroux, S. (1979). "Aminopeptidase, a cytosol enzyme from rabbit intestinal mucosa". Biochem. J. 177: 801-808. PMC ... Tripeptide aminopeptidase (EC 3.4.11.4, tripeptidase, aminotripeptidase, aminoexotripeptidase, lymphopeptidase, ...

*Aminopeptidase Ey

... (EC 3.4.11.20) is an enzyme. This enzyme catalyses differs from other aminopeptidases in broad specificity ... Aminopeptidase Ey at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal ... Ichishima, E.; Yamagata, Y.; Chiba, H.; Sawaguchi, K.; Tanaka, T. (1989). "Soluble and bound forms of aminopeptidase in hens ... Tanaka, T.; Ichishima, E. (1993). "Substrate specificity of aminopeptidase Ey from hen's egg yolk". Comp. Biochem. Physiol. [B ...

*Aspartyl aminopeptidase

... (EC 3.4.11.21) is an enzyme. This enzyme catalyses the following chemical reaction Release of an N- ... Aspartyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Kelly, J.A.; Neidle, E.L.; Neidle, A. (1983). "An aminopeptidase from mouse brain cytosol that cleaves N-terminal acidic amino ... characterization and cloning of a cytosolic aspartyl aminopeptidase". J. Biol. Chem. 273: 15961-15970. doi:10.1074/jbc.273.26. ...

*Aminopeptidase S

... aminopeptidase (Streptomyces griseus), Streptomyces griseus aminopeptidase, S. griseus AP, double-zinc aminopeptidase) is an ... Aminopeptidase S at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Arima, J.; Uesugi, Y.; Iwabuchi, M.; Hatanaka, T. (2006). "Study on peptide hydrolysis by aminopeptidases from Streptomyces ... Ben-Meir, D.; Spungin, A.; Ashkenazi, R.; Blumberg, S. (1993). "Specificity of Streptomyces griseus aminopeptidase and ...

*Tryptophanyl aminopeptidase

... (EC 3.4.11.17, tryptophan aminopeptidase, L-tryptophan aminopeptidase) is an enzyme. This enzyme ... Tryptophanyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Iwayama, A.; Kimura, T.; Adachi, O.; Ameyama, M. (1983). "Crystallization and characterization of a novel aminopeptidase from ...

*Clostridial aminopeptidase

... (EC 3.4.11.13, Clostridium histolyticum aminopeptidase) is an enzyme. This enzyme catalyses the ... Clostridial aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Kessler, E.; Yaron, A. (1973). "A novel aminopeptidase from Clostridium histolyticum". Biochem. Biophys. Res. Commun. 50: 405- ... Kessler, E.; Yaron, A. (1976). "An extracellular aminopeptidase from Clostridium histolyticum". Eur. J. Biochem. 63: 271-287. ...

*Aminopeptidase B

... arginyl aminopeptidase, Cl-activated arginine aminopeptidase, cytosol aminopeptidase IV, L-arginine aminopeptidase) is an ... Aminopeptidase B (EC 3.4.11.6, arylamidase II, arginine aminopeptidase, ... Aminopeptidase B at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Cadel, S.; Pierotti, A.R.; Foulon, T.; Créminon, C.; Barré, N.; Segrétain, D.; Cohen, P. (1995). "Aminopeptidase-B in the rat ...

*Leucyl aminopeptidase

... leucinamide aminopeptidase, FTBL proteins, proteinates FTBL, aminopeptidase II, aminopeptidase III, aminopeptidase I) are ... Leucyl aminopeptidases (EC 3.4.11.1, leucine aminopeptidase, LAPs, leucyl peptidase, peptidase S, cytosol aminopeptidase, ... Leucyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... LAP-A is the first plant aminopeptidase shown to have a regulatory role in signal transduction pathway. LAP proteins and ...

*Pyroglutamate aminopeptidase

... may be used to cleave the cyclical lactam and will therefore leave the next amino acid with a free ... Pyroglutamate aminopeptidase is a type of enzyme that cleaves the peptide bond linking the N-terminal end of a polypeptide ... "High-Yield Deblocking of Amino Termini of Recombinant Immunoglobulins with Pyroglutamate Aminopeptidase". Analytical ...

*PepB aminopeptidase

... (EC 3.4.11.23, Salmonella enterica serovar Typhimurium peptidase B) is an enzyme which catalyses the ... PepB aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Mathew, Z.; Knox, T.M.; Miller, C.G. (2000). "Salmonella enterica serovar typhimurium peptidase B is a leucyl aminopeptidase ...

*Aminopeptidase I

... (EC 3.4.11.22, aminopeptidase III, aminopeptidase yscI, leucine aminopeptidase IV, yeast aminopeptidase I) is ... Aminopeptidase I at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Chang, Y-H.; Smith, J.A. (1989). "Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces ... Metz, G.; Rohm, K.-H. (1976). "Yeast aminopeptidase I. Chemical composition and catalytic properties". Biochim. Biophys. Acta. ...

*Glutamyl aminopeptidase

... (EC 3.4.11.7, aminopeptidase A, aspartate aminopeptidase, angiotensinase A, glutamyl peptidase, Ca2+- ... Glutamyl aminopeptidase has also recently been designated CD249 (cluster of differentiation 249). Glutamyl aminopeptidase is a ... membrane aminopeptidase II, antigen BP-1/6C3 of mouse B lymphocytes, L-aspartate aminopeptidase, angiotensinase A2) is an ... Reaux A, Iturrioz X, Vazeux G, Fournie-Zaluski MC, David C, Roques BP, Corvol P, Llorens-Cortes C (2000). "Aminopeptidase A, ...

*Bacterial leucyl aminopeptidase

... (EC 3.4.11.10, Aeromonas proteolytica aminopeptidase) is an enzyme. This enzyme catalyses the ... Bacterial leucyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Dick, A.J.; Matheson, A.T.; Wang, J.H. (1970). "A ribosomal-bound aminopeptidase in Escherichia coli B: purification and ... Prescott, J.M.; Wilkes, S.H. (1966). "Aeromonas aminopeptidase: purification and some general properties". Arch. Biochem. ...

*X-Trp aminopeptidase

Xaa-Trp aminopeptidase (EC 3.4.11.16, aminopeptidase W, aminopeptidase X-Trp) is an enzyme. This enzyme catalyses the following ... Xaa-Trp aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... The 130kDa protein in pig kidney, recognised by monoclonal antibody GK5C1, is an ectoenzyme with aminopeptidase activity". ... Enzymic and molecular properties of aminopeptidase W". Biochem. J. 246: 97-102. doi:10.1042/bj2460097. PMC 1148244 . PMID ...

*Beta-peptidyl aminopeptidase

... (EC 3.4.11.25, BapA) is an enzyme. This enzyme catalyses the following chemical reaction Cleaves N ... Beta-peptidyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... Geueke, B.; Namoto, K.; Seebach, D.; Kohler, H.P. (2005). "A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves ... Geueke, B.; Heck, T.; Limbach, M.; Nesatyy, V.; Seebach, D.; Kohler, H.P. (2006). "Bacterial β-peptidyl aminopeptidases with ...

*Xaa-Pro aminopeptidase

... (EC 3.4.11.9, X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, aminoacylproline ... Xaa-Pro aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Hooper, N.M.; Hryszko, J.; Turner, A.J. (1990). "Purification and characterization of pig kidney aminopeptidase P". Biochem. J ... Orawski, A.T.; Susz, J.P.; Simmons, W.H. (1987). "Aminopeptidase-P from bovine lung - solubilization, properties, potential ...
Puromycin-sensitive aminopeptidase Lysates from Novus Biologicals. Browse our Puromycin-sensitive aminopeptidase Overexpression Lysates.
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EC 3.4.11.6 Recommended name: Aminopeptidase B. Reaction: Release of N-terminal Arg and Lys from oligopeptides when P1 is not Pro. Also acts on arylamides of Arg and Lys. Other names: Arylamidase II; Arginine aminopeptidase; Arginyl aminopeptidase; Cl--Activated arginine aminopeptidase; Cytosol aminopeptidase IV. Comments: Cytosolic or membrane-associated enzyme from mammalian tissues, activated by 0.15 M Cl- and low concentrations of thiol compounds. Hydrolyses a non-peptide (epoxide) bond in leukotriene A4, but is distinct from leukotriene-A4 hydrolase (EC 3.3.2.6) [5]. Potently inhibited by arphamenine B, and also inhibited by chelating agents, N-ethylmaleimide, arphamenine A, amastatin and bestatin. A zinc metallopeptidase in family M1 [4,5]. References 1. Gainer, H., Russell, J.T. & Loh, Y.P. (1984) An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin(60-65). FEBS Lett. 175, 135-139. 2. Belhacène, N., Mari, B., Rossi, ...
Compare arginyl aminopeptidase (aminopeptidase B)-like 1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
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Salt sensitivity of blood pressure (SSBP) and hypertension are common, but the underlying mechanisms remain unclear. Endoplasmic reticulum aminopeptidase 1 (ERAP1) degrades angiotensin II (ANGII). We hypothesized that decreasing ERAP1 increases BP via ANGII-mediated effects on aldosterone (ALDO) production and/or renovascular function. Compared with WT littermate mice, ERAP1-deficient (ERAP1+/-) mice had increased tissue ANGII, systolic and diastolic BP, and SSBP, indicating that ERAP1 deficiency leads to volume expansion. However, the mechanisms underlying the volume expansion differed according to sex. Male ERAP1+/- mice had increased ALDO levels and normal renovascular responses to volume expansion (decreased resistive and pulsatility indices and increased glomerular volume). In contrast, female ERAP1+/- mice had normal ALDO levels but lacked normal renovascular responses. In humans, ERAP1 rs30187, a loss-of-function gene variant that reduces ANGII degradation in vitro, is associated with ...
APP (aminopeptidase P) has the unique ability to cleave the N-terminal amino acid residue from peptides exhibiting a proline at P1′. Despite its putative involvement in the processing of bioactive peptides, among them the kinins, little is known about the physiological roles of both human forms of APP. The purpose of the present study is first to engineer and characterize a secreted form of hmAPP (human membrane-bound APP). Our biochemical analysis has shown that the expressed glycosylated protein is fully functional, and exhibits enzymic parameters similar to those described previously for mAPP purified from porcine or bovine lungs or expressed from a porcine clone. This soluble form of hmAPP cross-reacts with a polyclonal antiserum raised against a 469-amino-acid hmAPP fragment produced in Escherichia coli. Secondly, we synthesized three internally quenched fluorescent peptide substrates that exhibit a similar affinity for the enzyme than its natural substrates, the kinins, and a higher ...
XPNPEP1 (do inglês, X-prolyl aminopeptidase (aminopeptidase P) 1, soluble), é um gene humano. XPNPEP1 (EC 3.4.11.9) é uma metaloaminopeptidase específica de prolina que catalisa especificamente a remoção de qualquer aminoácido N-terminal não-substituído que seja adjacente a penúltimo resíduo de prolina. Devido à sua especificidade em relação à prolina, tem sido sugerido que XPNPEP1 é importante na maturação e degradação de hormonas peptídicas, de neuropéptidos e de taquininas, como também na digestão de outros fragmentos proteicos resistentes, da dieta, desta forma complementando as peptidases pancreáticas. A deficiência em XPNPEP1 resulta na excreção de grandes quantidades de imino-oligopéptidos na urina. «Entrez Gene: XPNPEP1 X-prolyl aminopeptidase (aminopeptidase P) 1, soluble» Vanhoof G, De Meester I, Goossens F; et al. (1992). «Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P.». Biochem. Pharmacol. 44 ...
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The present invention relates to isolated polypeptides having aminopeptidase activity and isolated nucleic acid sequences encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing and using the polypeptides.
3QNF: Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
3QNF: Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
Erap1 - Erap1 (GFP-tagged) - Mouse endoplasmic reticulum aminopeptidase 1 (Erap1), (10ug) available for purchase from OriGene - Your Gene Company.
This agent and others like it have already been in clinical trials as treatments for other tumors, so if we find that fumagillin inhibits brain tumor growth in preclinical studies, it will be a much smaller leap to using these compounds in patients with NF1," says senior investigator David H. Gutmann, M.D., Ph.D., the Donald O. Schnuck Family Professor of Neurology at Washington University School of Medicine in St. Louis and co-director of the neuro-oncology program at the Siteman Cancer Center ...
Reaktivität: Rind (Kuh), Hund, Human and more. 39 verschiedene XPNPEP1 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Background Inflammatory bowel disease (IBD) is connected with a defective intestinal hurdle and improved adaptive immune system replies against commensal microbiota. of IBD sufferers. Fecal Ab amounts towards meals and microbial antigens present distinctive patterns in handles, UC and CD patients. Launch Inflammatory bowel illnesses (IBD) add a selection of chronic, immune-mediated inflammatory disorders from the gastrointestinal program with fluctuating activity, most regularly symbolized by Crohns disease (Compact disc) or ulcerative colitis (UC). IBD includes a multifactorial etiology with hereditary and environmental sets off and its been associated with adjustments from the intestinal microflora, defects in the gastrointestinal barrier with increased transport of luminal contents into the tissue and a loss of immune tolerance [1], [2]. Consequently, specific adaptive immune responses towards luminal antigens, in particular antigens of the commensal microflora, are altered in IBD patients. ...
Xpnpep3 - Xpnpep3 (Myc-DDK-tagged) - Mouse X-prolyl aminopeptidase (aminopeptidase P) 3, putative (Xpnpep3), nuclear gene encoding mitochondrial protein available for purchase from OriGene - Your Gene Company.
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RNPEPL1 antibody (arginyl aminopeptidase (aminopeptidase B)-like 1) for IHC-P, WB. Anti-RNPEPL1 pAb (GTX111563) is tested in Human, Mouse samples. 100% Ab-Assurance.
The discovery of CHR-2797 stemmed from the observation that certain membrane-permeant compounds within a metalloenzyme inhibitor-focused chemical library inhibited the proliferation of a subset of tumor cell lines. The belief that the target enzyme is located intracellularly is substantiated by the findings that only esters that drive the accumulation of an acid inside the cell exert a powerful antiproliferative action. In contrast, related compounds which are poorly lipophilic are only weakly active in cell proliferation assays despite good activity against the same class of aminopeptidases, e.g., CHR-79888. The evidence that the target for these effects lay within the cell focused attention on aminopeptidases, histone deacetylases, MetAP-2, or peptide deformylase as intracellular metalloenzyme targets ( 2, 10, 24- 26). CHR-2797 has been shown to be inactive against a number of these targets (histone deacetylase, MetAP-2) and/or to affect the proliferation of a different spectrum of tumor cell ...
In living organisms, enzymes work in complicated networks to perform various biological functions. To analyse such functions, specific enzyme inhibitors are needed. Such inhibitors would be of great...
There is an urgent need for novel compounds and treatment strategies for elderly patients with AML, particularly those with refractory or relapsed disease for whom there are few effective treatment options. Treatment options for elderly patients are further limited by co-morbidity and tolerability constraints.. Tosedostat is a new aminopeptidase inhibitor, which in preclinical experiments has shown potent activity in both in vitro and in vivo cancer models as a single agent. In early clinical studies particularly good results have been observed in refractory and relapsed AML in older patients and these observations form the basis for the current study.. This multi-center, open label phase II study will enrol approximately 70 subjects in Part A and 130 subjects in Part B. ...
There is an urgent need for novel compounds and treatment strategies for elderly patients with AML, particularly those with refractory or relapsed disease for whom there are few effective treatment options. Treatment options for elderly patients are further limited by co-morbidity and tolerability constraints.. Tosedostat is a new aminopeptidase inhibitor, which in preclinical experiments has shown potent activity in both in vitro and in vivo cancer models as a single agent. In early clinical studies particularly good results have been observed in refractory and relapsed AML in older patients and these observations form the basis for the current study.. This multi-center, open label phase II study will enrol approximately 70 subjects in Part A and 130 subjects in Part B. ...
List of words make out of Aminopeptidase. Anagrams of word Aminopeptidase. Words made after scrabbling Aminopeptidase. Word Creation helps in Anagrams and Puzzles.
Endoplasmatic reticulum aminopeptidase 1 (ERAP1) is a multifunctional enzyme involved in trimming of peptides to an optimal length for presentation by major histocompatibility complex (MHC) class I molecules. Polymorphisms in ERAP1 have been associated with chronic inflammatory diseases, including ankylosing spondylitis (AS) and psoriasis, and subsequent in vitro enzyme studies suggest distinct catalytic properties of ERAP1 variants. To understand structure-activity relationships of this enzyme we determined crystal structures in open and closed states of human ERAP1, which provide the first snapshots along a catalytic path. ERAP1 is a zinc-metallopeptidase with typical H-E-X-X-H-(X)(18)-E zinc binding and G-A-M-E-N motifs characteristic for members of the gluzincin protease family. The structures reveal extensive domain movements, including an active site closure as well as three different open conformations, thus providing insights into the catalytic cycle. A K(528)R mutant strongly associated ...
The identity of the physiologically relevant metal ions for the methionyl aminopeptidase (MetAP) from Escherichia coli was investigated and is suggested to be Fe(II). The metal content of whole cells in the absence and presence of expression of the type I MetAP from E. coli was determined by inductively coupled plasma (ICP) emission analysis. The observed change in whole cell concentrations of cobalt, cadmium, copper, nickel, strontium, titanium, and vanadium upon expression of MetAP was negligible. On the other hand, significant increases in the cellular metal ion concentrations of chromium, zinc, manganese, and iron were observed with the increase in iron concentration being 4.4 and 6.2 times greater than that of manganese and zinc, respectively. Activity assays of freshly lysed BL21(DE3) cells containing the pMetAAP plasmid revealed detectable levels (|2 units/mg) of MetAP activity. Control experiments with BL21(DE3) without the MetAP plasmid showed no detectable enzymatic activity. Since MetAP is
Xpnpep1 - mouse gene knockout kit via CRISPR, 1 kit. |dl||dt|Kit Component:|/dt||dd|- |strong|KN319510G1|/strong|, Xpnpep1 gRNA vector 1 in |a href=http://www.origene.com/CRISPR-CAS9/Detail.
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Complete information for XPNPEP1 gene (Protein Coding), X-Prolyl Aminopeptidase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
The protein encoded by this gene is a zinc metalloprotease that displays some activity against angiotensin-3. The encoded protein is inhibited by the aminopeptidase inhibitor amastatin, as well as by the general inhibitors o-phenanthroline and batimastat. Defects in this gene may be associated with lung tumorigenesis. [provided by RefSeq, Oct 2016 ...
Anti-Methionine Aminopeptidase 2 antibody [EPR6886(B)] (ab124953) has been cited in 1 publications. Find out more about the references
Peak concentrations are achieved after 60 min. Biotransformation develops through the action of aminopeptidases and angiotensin-converting enzyme to individual amino acids. Its half-life (t 1/2) is 4 min; The therapeutic effect, after the application of a single dose, is maintained up to 20 hours. It is very rapidly excreted in urine via kidneys . Its half-life is : 0.4-5 minutes.. ...
Analysis of Antimalarial Synergy between Bestatin and Endoprotease Inhibitors Using Statistical Response-Surface Modelling: The pathway of hemoglobin degradatio
since using bestatin, i cough a lot more and when in bed i feel some irragular heartbeat. somewhere ... which were nog good. so many bad side effects.
Tripeptidyl-peptidase 2 is an enzyme that in humans is encoded by the TPP2 gene. Among other things it is heavily implicated in MHC (HLA) class-I processing, as it has both endopeptidase and exopeptidase activity. GRCh38: Ensembl release 89: ENSG00000134900 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000041763 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Tomkinson B, Jonsson AK (Feb 1991). "Characterization of cDNA for human tripeptidyl peptidase II: the N-terminal part of the enzyme is similar to subtilisin". Biochemistry. 30 (1): 168-74. doi:10.1021/bi00215a025. PMID 1670990. "Entrez Gene: TPP2 tripeptidyl peptidase II". Reits E, Neijssen J, Herberts C, et al. (April 2004). "A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation". Immunity. 20 (4): 495-506. doi:10.1016/S1074-7613(04)00074-3. PMID 15084277. The MEROPS online database for peptidases and their inhibitors: S08.090 Tomkinson B, Zetterqvist O ...
Tripeptidyl peptidase II (TPPII) is an exopeptidase which cleaves tripeptides from theN-terminus of peptides. The exact functional role of TPPII is still a matter of investigation. Itis believed that the enzyme is primarily involved in intracellular protein degradation, where itcooperates with the proteasome and other peptidases to degrade proteins into free aminoacids. These amino acids can subsequently be used in the production of new proteins. The aimof this work was to express murine wild type TPPII using E. coli and thereafter purify theenzyme from the bacterial lysate. Methods used for the purification included protein andnucleic acid precipitation, anion exchange chromatography, hydrophobic interactionchromatography and gel filtration. The presence of TPPII was determined using activityassay, western blot and SDS-PAGE. Despite the fact that some modification is still needed,the purification yielded a total of 34μg TPPII with a purity of approximately 60%. Thispurified enzyme can be used ...
Aminopeptidase N (Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or Microsomal Aminopeptidase or gp150 or CD13 or ANPEP or EC 3.4.11.2) - Market research report and industry analysis - 11296626
Title: Alpha-1-Adrenergic Receptor Blockade Modifies Insulin-Regulated Aminopeptidase (IRAP) Activity in Rat Prostate and Modulates Oxytocin Functions. VOLUME: 5 ISSUE: 3. Author(s):Marcela Arrazola Saniger, Maria Jesus Ramirez-Exposito, Susana de la Chica, Maria Pilar Carrera-Gonzalez, Maria Dolores Mayas and Jose Manuel Martinez-Martos. Affiliation:Experimental and Clinical Physiopathology Research Group, Department of Health Sciences, Faculty of Experimental and Health Sciences, University of Jaen, Campus Universitario Las Lagunillas, E-23071, Jaen, Spain.. Keywords:Oxytocin, Prostate, Insulin-regulated aminopeptidase, Adrenergic receptors, Doxazosin, Wistar rat, alpha1-adrenergic receptor antagonist, hyperplasia. Abstract: Background: Oxytocin (OT) is one of the important paracrine factors that prostate synthesizes. OT maintains its resting tone and stimulates its contractile activity. However, the involvement of OT in modulating cell proliferation of the prostate is being investigated. In ...
The protein degradation process is of vital importance for the cell to maintain cellular functions. An important enzyme in this process is the multimeric tripeptidyl-peptidase II (TPP II). It removes tripeptides from a free N-terminus of the substrates. TPP II has broad substrate specificity and wide-spread distribution, suggesting that the TPP II gene is a house-keeping gene. However, the levels of both mRNA and TPP II protein varies during different conditions and the TPP II gene promoter was therefore identified and characterized. It is a 215 bp fragment just upstream of the coding sequence. This fragment lacks a TATA-box but contains an initiator, two inverted CCAAT-boxes and an E-box. The CCAAT-boxes and the E-box were found to bind the nuclear factor Y (NF-Y) and upstream stimulatory factor-1 (USF-1) respectively. The CCAAT-boxes appear to be most important for the transcriptional activation. Furthermore, several silencer element were identified further upstream of the 215 bp promoter and ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Sodium atom in PDB 2gg5: Novel Bacterial Methionine Aminopeptidase Inhibitors
In this study, we determined serum aminopeptidase N/CD13 concentrations in patients with NSCLC using an aminopeptidase N/CD13-specific mAb (MH8-11), which inhibits cell motility and angiogenesis in vitro (10). Serum aminopeptidase N/CD13 concentrations were significantly elevated in patients with advanced-stage NSCLC. When the serum aminopeptidase N/CD13 values corresponding to the best diagnostic accuracy to separate the healthy controls and the patients with NSCLC were used as the cutoff value, the sensitivity of aminopeptidase N/CD13 was poorer than that of serum carcinoembryonic antigen; this suggests that serum aminopeptidase N/CD13 is not valuable as a diagnostic marker. However, a high serum aminopeptidase N/CD13 was significantly associated with established adverse prognostic factors in NSCLC, such as advanced stage, poor performance status, and poor response to chemotherapy. Serum aminopeptidase N/CD13 levels were also associated with overall survival in univariate analyses and had an ...
The property of solutions of Triton X-114 to separate into detergent-rich and detergent-poor phases at 30 degrees C has been exploited to investigate the identities of the aminopeptidases in synaptic membrane preparations from pig striatum. When titrated with an antiserum to aminopeptidase N (EC 3.4.11.2), synaptic membranes solubilized with Triton X-100 revealed that this enzyme apparently comprises no more than 5% of the activity releasing tyrosine from [Leu]enkephalin. When assayed in the presence of puromycin, this proportion increased to 20%. Three integral membrane proteins were fractionated by phase separation in Triton X-114. Aminopeptidase activity, endopeptidase-24.11 and peptidyl dipeptidase A partitioned predominantly into the detergent-rich phase when kidney microvillar membranes were so treated. However, only 5.5% of synaptic membrane aminopeptidase activity partitioned into this phase, although the other peptidases behaved predictably. About half of the aminopeptidase activity in ...
Angiotensin IV (Ang IV) and related peptide analogues, as well as non-peptide inhibitors of insulin-regulated aminopeptidase (IRAP), have previously been shown to enhance memory and cognition in animal models. Furthermore, the endogenous IRAP substrates oxytocin and vasopressin are known to facilitate learning and memory. In this study, the two recently synthesized 13-membered macrocylic competitive IRAP inhibitors HA08 and HA09, which were designed to mimic the N-terminal of oxytocin and vasopressin, were assessed and compared based on their ability to bind to the IRAP active site, and alter dendritic spine density in rat hippocampal primary cultures. The binding modes of the IRAP inhibitors HA08, HA09 and of Ang IV in either the extended or γ-turn conformation at the C-terminal to human IRAP were predicted by docking and molecular dynamics (MD) simulations. The binding free energies calculated with the linear interaction energy (LIE) method, which are in excellent agreement with experimental ...
The hexapeptide angiotensin IV (Ang IV) is a metabolite of angiotensin II (Ang II) and plays a central role in the brain. It was reported more than two decades ago that intracerebroventricular injection of Ang IV improved memory and learning in the rat. Several hypotheses have been put forward to explain the positive effects of Ang IV and related analogues on cognition. It has been proposed that the insulin-regulated aminopeptidase (IRAP) is the main target of Ang IV. This paper discusses progress in the discovery of inhibitors of IRAP as potential enhancers of cognitive functions. Very potent inhibitors of the protease have been synthesised, but pharmacokinetic issues (including problems associated with crossing the blood-brain barrier) remain to be solved. The paper also briefly presents an overview of the status in the discovery of inhibitors of ACE and renin, and of AT1R antagonists and AT2R agonists, in order to enable other discovery processes within the RAS system to be compared. The paper
Strain JC140T exhibited a catalase activity but no oxidase activity. Using the API Rapid ID 32A system, positive reactions were observed for arginine arylimidase, tyrosine arylamidase, histidine arylamidase and indole production. Weak reactions were observed for leucyl glycine arylamidase and glycine arylamidase. All other assays were negative. P. senegalensis is susceptible to penicillin G, amoxicillin + clavulanic acid, imipeneme, vancomycin, clindamycin and metronidazole. By comparison with other phylogenetically closely related Peptoniphilus species, P. senegalensis differed in leucine arylamidase, phenylalanine arylamidase and serine arylamidase activities with P. gorbachii [22], in tyrosine arylamidase activity with P. harei [18] and in α-galactosidase, serine arylamidase, leucine arylamidase, phenylalanine arylamidase, glycine arylamidase and glycine arylamidase activities with P. timonensis [10].. Matrix-assisted laser-desorption/ionization time-of-flight (MALDI-TOF) MS protein analysis ...
Membrane alanyl aminopeptidase (EC 3.4.11.2) also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme that in humans is encoded by the ANPEP gene. Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. In the small intestine aminopeptidase N plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Its function in proximal tubular epithelial cells and other cell types is less clear. The large extracellular carboxyterminal domain contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloproteinase superfamily. Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. The latter enzyme was thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, ...
Alanine aminopeptidase membranaire Lalanine aminopeptidase est une peptidase qui catalyse lhydrolyse de la liaison peptidique liant le résidu N-terminal dun peptide. Cet acide aminé est de préférence lalanine, mais lenzyme est active sur la plupart des autres acides aminés également, y compris la proline - la réaction est cependant plus lente - ainsi que sur les amides et arylamides de cet acide aminé. Lors quun résidu hydrophobe N-terminal est suivi par un résidu de proline, lenzyme peut alors cliver ces deux résidus du reste du peptide en libérant un dipeptide Xaa-Pro. Lalanine aminopeptidase est utilisée comme marqueur biologique pour détecter les dommages aux reins, et qui peut être utilisée pour aider à diagnostiquer certaines maladies rénales. En cas de problèmes rénaux, on en trouve en concentration élevée dans lurine. Son gène est ANPEP situé sur le chromosome 15 humain. Cette section est vide, insuffisamment détaillée ou incomplète. Votre aide est la ...
Title: The Development of MetAP-2 Inhibitors in Cancer Treatment. VOLUME: 19 ISSUE: 7. Author(s):S.-Q. Yin, J.-J. Wang, C.-M. Zhang and Z.-P. Liu. Affiliation:Department of Organic Chemistry,School of Pharmaceutical Sciences, Shandong University, Jinan 250012, P. R. China.. Keywords:Angiogenesis inhibitor, antiangiogenesis, endothelial cells, methionine, metastasis, migration, MetAP-2, cancer, MetAP-2 inhibitors, fumagillin, structure-activity relationship, vascular endothelial growth factor. Abstract: Methionine aminopeptidases (MetAPs), which remove methionine residue from newly synthesized polypeptide chains, are a class of metalloproteases ubiquitously distributed in both eukaryotes and prokaryotes. MetAP-2 inhibition can induce G1 cell cycle arrest, cytostasis in tumor cells in vitro and inhibition of tumor growth in vivo. The discovery of fumagillin with potent antiangiogenic and antiproliferative activities promoted the development of fumagillin analogues as a novel class of anticancer ...
Definition of leucine aminopeptidase in the Legal Dictionary - by Free online English dictionary and encyclopedia. What is leucine aminopeptidase? Meaning of leucine aminopeptidase as a legal term. What does leucine aminopeptidase mean in law?
The SCOP classification for the Methionine aminopeptidase, insert domain family. Additional information, provided for both this family and the superfamily it belongs to, includes SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
The IUPHAR/BPS Guide to Pharmacology. Monoacylglycerol lipase - S33: Prolyl aminopeptidase. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of drug targets.
Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. In the small intestine aminopeptidase N plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Its function in proximal tubular epithelial cells and other cell types is less clear. The large extracellular carboxyterminal domain contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloproteinase superfamily. Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. The latter enzyme was thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, granulocytes, and synaptic membranes from the CNS. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract ...
A case-control study of 1103 Chilean maternal-fetal dyads and 1637 unpaired African American samples (836 maternal, 837 fetal) concluded that the fetal minor allele rs2549782(G) was associated with 1.3x increased risk (CI: 1.075-1.619) for pre-eclampsia in the African American population (p = 0.009), but not in the Chilean population. }} [PMID 20843824] Genetic diversity at endoplasmic reticulum aminopeptidases is maintained by balancing selection and is associated with natural resistance to HIV-1 infection. [PMID 20595269] Serum cytokine receptors in ankylosing spondylitis: relationship to inflammatory markers and endoplasmic reticulum aminopeptidase polymorphisms. [PMID 19578876 ...
Looking for online definition of aminopeptidase microsomal in the Medical Dictionary? aminopeptidase microsomal explanation free. What is aminopeptidase microsomal? Meaning of aminopeptidase microsomal medical term. What does aminopeptidase microsomal mean?
Serum cystyl aminopeptidase (CAS) activity was estimated at 36 weeks gestation in 209 normotensive pregnancies. The highest activity was found in 31 women who had spontaneous deliveries before 38 weeks gestation and the lowest in 76 women who were induced after term. The enzyme levels in 117 women who developed hypertension of pregnancy were higher than for normotensives; the highest levels were found in 32 women with pre-eclampsia. A correlation was found between serum CAS activity at 36 weeks gestation and the birth weight of babies of women who went into spontaneous labour at term (277 to 283 days gestation).. ...
Dipeptidyl Aminopeptidases exert a potent modulatory role at an interface between immune mechanisms, metabolic responses, and neuroendocrine pathways. Experimental models and clinical studies addressi
To detect viral infections and tumors, CD8+ T lymphocytes monitor cells for the presence of antigenic peptides bound to MHC class I molecules. The majority of MHC class I-presented peptides are generated from the cleavage of cellular and viral proteins by the ubiquitin-proteasome pathway. Many of the oligopeptides produced by this process are too long to stably bind to MHC class I molecules and require further trimming for presentation. Leucine aminopeptidase (LAP) is an IFN-inducible cytosolic aminopeptidase that can trim precursor peptides to mature epitopes and has been thought to play an important role in Ag presentation. To examine the role of LAP in generating MHC class I peptides in vivo, we generated LAP-deficient mice and LAP-deficient cell lines. These mutant mice and cells are viable and grow normally. The trimming of peptides in LAP-deficient cells is not reduced under basal conditions or after stimulation with IFN. Similarly, there is no reduction in presentation of peptides from precursor
Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily (297 aa ...
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle ...
GT:ID BAD55641.1 GT:GENE BAD55641.1 GT:PRODUCT putative methionine aminopeptidase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 860331..861131 GB:FROM 860331 GB:TO 861131 GB:DIRECTION + GB:PRODUCT putative methionine aminopeptidase GB:PROTEIN_ID BAD55641.1 LENGTH 266 SQ:AASEQ MVFGRKNKKVVPFRTAGELDAMAAAGAVVGRALVAVRAAAKPGVSTLELDEVAEQTIREAGAVPSFKGYHGFPGSICSSVNDRVVHGIPSAEEILAEGDLVSIDCGAILDGWHGDSAWTFGVGSIIEADRLLSEATRISMEAGIAAMVPGNRLTDVSHAIELGTRAAEQEHGRAYGIVDGYGGHGIGREMHMDPFLANEGEPGRGPQLVVGSVLAIEPMLTLGTTQTKVLDDDWTVVTVDGSRAAHWEHTVAVTEDGPRILTPRPE GT:EXON 1,1-266:0, BL:SWS:NREP 1 BL:SWS:REP 41-,262,AMPM_CLOAB,5e-54,48.1,216/250, SEG 21-,40,amaaagavvgralvavraaa, SEG 175-,187,ygivdgygghgig, SEG 227-,240,tkvldddwtvvtvd, BL:PDB:NREP 1 BL:PDB:REP 42-,262,1o0xA,1e-37,38.1,215/249, RP:PDB:NREP 1 RP:PDB:REP 41-,266,2bb7A,5e-42,32.7,220/258, RP:PFM:NREP 1 RP:PFM:REP 41-,159,PF00557,2e-13,44.2,113/203,Peptidase_M24, HM:PFM:NREP 1 HM:PFM:REP ...
Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). Specificity related to, but distinct from, those of thermolysin and bacillolysin [1]. A zinc metallopeptidase in family M4 (thermolysin family). Formerly included in EC 3.4.24.4 ...
TET aminopeptidases are dodecameric particles shared in the three life domains involved in various biological processes, from carbon source provider in archaea to eye-pressure regulation in humans. Each subunit contains a dinuclear metal site (M1 and M2) responsible for the enzyme catalytic activity. However, the role of each metal ion is still uncharacterized. Noteworthy, while mesophilic TETs are activated by Mn(2+), hyperthermophilic TETs prefers Co(2+). Here, by means of anomalous x-ray crystallography and enzyme kinetics measurements of the TET3 aminopeptidase from the hyperthermophilic organism Pyrococcus furiosus (PfTET3), we show that M2 hosts the catalytic activity of the enzyme, while M1 stabilizes the TET3 quaternary structure and controls the active site flexibility in a temperature dependent manner. A new third metal site (M3) was found in the substrate binding pocket, modulating the PfTET3 substrate preferences. These data show that TET activity is tuned by the molecular interplay among
Neuromedin N (NN) induced a concentration-dependent contraction (ED50 = 2.3 +/- 0.2 microM) of the isolated longitudinal smooth muscle from guinea pig ileum. This effect was drastically enhanced (ED50 = 0.06 microM) by the aminopeptidases M and B inhibitor bestatin (10 microM), which elicited a 40-fold increase in NN potency. HPLC analysis indicated that the main NN catabolite generated by membranes from guinea pig longitudinal smooth muscle homogenate corresponded to des-Lys1-NN, which results from removal of the N-terminal lysyl residue of NN. The fact that the formation of des-Lys1-NN was fully prevented by bestatin (10 microM) further supports the involvement of aminopeptidases in NN degradation. We examined the catabolic fate of NN in vivo in the vascularly perfused dog ileum. Bolus administration or continuous infusion of the peptide led to rapid disappearance of NN. This was prevented by prior treatment of ileal segments with bestatin (10 microM) but not with arphamenine B (0.5 microM), ...
The LAP disk is a rapid test for the detection of enzyme lucine amino peptidase.. Leucine-beta-naphthylamide impregnated disk serve as a substrate for the detection of lucine aminopeptidase. Following hydrolysis of the substrate by enzyme, the resulting beta- naphthylamineprodeces a red color upon the addition of cinnamaldehyde reagent ...
Staphylococcus aureus is a remarkably successful pathogen, accounting for an estimated 95,000 invasive infections annually in the U.S. alone. The burden of MRSA infections on public healthcare continues to rise, particularly with the continued spread of antibiotic resistant strains and the hyper-virulent CA-MRSA strains. The pathogenic nature of S. aureus can be attributed to the cache of virulence factors encoded within the genome of this organism. Typically, these are secreted toxins which directly interact with the host during infection, and facilitate pathogenesis. A previous screen in our laboratory investigating proteases in S. aureus identified a mutant in aminopeptidase Z as being attenuated in disease causation. Classically aminopeptidases function in the bioactivation/inactivation of proteins; and/or the utilization of imported peptides for cellular nutrition. We therefore hypothesize that cells deficient in one of these two processes would have decreased fitness levels, resulting in reduced
Complete information for TPP2 gene (Protein Coding), Tripeptidyl Peptidase 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Malarial aminopeptidase molecule. Computer model showing the structure of the M18 aspartyl aminopeptidase with a dodecameric assembly arranged via dimer and trimer units forming a tetrahedron shape. From Plasmodium falciparum. - Stock Image C035/8499
Aminopeptidase definition, any of several intestinal hydrolytic enzymes that remove an amino acid from the end of a peptide chain having a free amino group. See more.
How to detect leucine arylamidase - posted in Microbiology: Dear all, I want to detect leucine arylamidase in brush border membrane vesicle from mosquito larvae but I have no idea about it. Could you guys tell me more about this enzyme and how to detect it ? I tried searching in google and yahoo but there was no provided kit or method. Thank you.
Identification of peptides presented in human leukocyte antigen (HLA) class I molecules after viral infection is of strategic importance for immunology and vaccine development
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Mammalian sera contain enzymes that catalyze the hydrolytic degradation of peptidoglycans and molecules of related structure and are relevant for the metabolism of peptidoglycans. We now report on a novel L,(L/D)-aminopeptidase found in human and mam
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
The graphic displays domains and Protease cut sites on the protein sequence. Drag your mouse right/left over the graphic. Use the selection boxes on the right to select which annotations to view simultaneously. Combine annotation with multiple checkmarks.. ...
Shop Tricorn protease ELISA Kit, Recombinant Protein and Tricorn protease Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Węglarz-Tomczak, Ewelina; Berlicki, Šukasz; Pawełczak, Małgorzata et al. (2016) A structural insight into the P1S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases. Eur J Med Chem 117:187-96 ...
This chapter describes the approaches used to identify Gram-negative rods, with emphasis on the greater difficulty in identifying non-glucose-fermenting organisms. We amplify what was presented in the 9th edition of this Manual by presenting a scheme to identify these organisms that is centered around three enzymatic activities, i.e., oxidase, trypsin (benzyl-arginine arylamidase or benzyl-arginine aminopeptidase), and pyrrolidonyl aminopeptidase. These enzymatic reactions are fast and easy to interpret, and they are stable markers in almost all taxa discussed; i.e., there are few species for which these tests yield variable intraspecies results.
Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.
Also known as ARTS1. The ERAP1 gene encodes a protein involved both in immune regulation and in the processing of cell surface receptors for pro-inflammatory cytokines. SNPs in ERAP1 have been reported in association with increased (or decreased) risk for the following conditions: ...
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TY - JOUR. T1 - Methionine aminopeptidase-2 regulates human mesothelioma cell survival. T2 - Role of Bcl-2 expression and telomerase activity. AU - Catalano, A.. AU - Romano, M.. AU - Robuffo, I.. AU - Strizzi, L.. AU - Procopio, A.. PY - 2001. Y1 - 2001. N2 - Methionine aminopeptidase-2 (MetAP2) is the molecular target of the angiogenesis inhibitors, fumagillin and ovalacin. Fumagillin can also inhibit cancer cell proliferation, implying that MetAP2 may play a quite complex role in tumor progression. Here, we examined the expression and function of MetAP2 in an in vitro model of human mesothelioma. We found that mesothelioma cells expressed higher MetAP2 mRNA levels than primary normal mesothelial cells. Consistently, fumagillin induced apoptosis, owing to early mitochondrial damage, in malignant, but not in normal mesothelial cells. Transfection of mesothelioma cells with a MetAP2 anti-sense oligonucleotide determined a time-dependent inhibition of cell survival and induced nucleosome ...
Tripeptidyl peptidase 1 (TPP1) enzymes are lysosomal peptidases that have a tripeptidyl exopeptidase activity with an optimal pH of 4-5. They belong to the group of sedolisins, serine peptidases that are present in organisms ranging from bacteria to mammals (Wlodawer et al., 2001; Comellas-Bigler et al., 2002). In eukaryotes, they are synthesized as precursors with an N-terminal signal sequence, a prodomain and a catalytic domain (peptidases S53 domain) (Vines and Warburton, 1999). Furthermore, they are N-glycosylated and become mannosylated during passage through the Golgi complex (Kollmann et al., 2013). TPP1 removes tripeptides from the N-terminus of proteins, but the in vivo substrates are not well characterized. However, synthetic peptides have been developed for enzyme analysis (Tian et al., 2006).. In humans, TPP1 is encoded by the TPP1 (CLN2) gene. Mutations in this gene cause an autosomal recessive neurodegenerative disease of childhood called late infantile neuronal ceroid ...
Catechols are known to coordinate divalent metal ions by virtue of their acidic ortho-hydroxyl groups. A recent HTS screening campaign to develop inhibitors against Pfm18AAP, a potential drug target for the treatment of malaria, identified a number of catechol-containing inhibitory molecules (Schoenen et al., 2010). In fact, the best-in-class probe identified in that screen, ML369 (Supplemental Fig. 5A), features a catechol moiety linked to a piperidine-tetrahydroquinoline ring system. Catechols have also been identified as inhibitors of methionine aminopeptidase, which, like DNPEP, also contains a binuclear zinc center. A structure of E. coli methionine aminopeptidase in complex with a catechol-containing compound revealed the mode of interaction of the catechol ring with the binuclear zinc center (Wang et al., 2008). In this structure, one of the hydroxyl groups of the catechol replaced water as a bridging ligand, whereas the other interacted with one of the zinc ions enforced by the active ...
ID H6RB75_NOCCG Unreviewed; 320 AA. AC H6RB75; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 22-NOV-2017, entry version 33. DE RecName: Full=Proline iminopeptidase {ECO:0000256,PIRNR:PIRNR006431, ECO:0000256,RuleBase:RU003421}; DE Short=PIP {ECO:0000256,PIRNR:PIRNR006431}; DE EC=3.4.11.5 {ECO:0000256,PIRNR:PIRNR006431, ECO:0000256,RuleBase:RU003421}; DE AltName: Full=Prolyl aminopeptidase {ECO:0000256,PIRNR:PIRNR006431}; GN Name=pip {ECO:0000313,EMBL:CCF62509.1}; GN OrderedLocusNames=NOCYR_1723 {ECO:0000313,EMBL:CCF62509.1}; OS Nocardia cyriacigeorgica (strain GUH-2). OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=1127134 {ECO:0000313,EMBL:CCF62509.1, ECO:0000313,Proteomes:UP000008190}; RN [1] {ECO:0000313,EMBL:CCF62509.1, ECO:0000313,Proteomes:UP000008190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GUH-2 {ECO:0000313,EMBL:CCF62509.1, RC ECO:0000313,Proteomes:UP000008190}; RX PubMed=22461543; ...
Crystallization trials were performed by sitting drop vapor diffusion in 96-well plates (Greiner Bio-One, Stonehouse, U.K.), using a Cartesian Technologies Microsys MIC4000 liquid-handling robot, incubated at 21°C and periodically inspected using a TAP Biosystems storage vault (TAP, Royston, U.K.).. Purified IRAP at a concentration of 10 mg/ml in 150 mM NaCl and 10 mM HEPES buffer (pH 7.4) was screened for crystallization against various commercially available screens. The protein stock and reservoir solution was mixed at a 1:1 ratio to form a drop of volume 200 nL. Usable crystals were obtained at several conditions of the Morpheus Screen (Molecular Dimensions) (32). In all cases, data were collected at the I03 beamline at the Diamond Light Source UK, equipped with a Pilatus3 6M pixel detector, at a wavelength of 0.976 Å. Data were merged and scaled using the xia2 package (33).. The best dataset collected from an unsoaked IRAP crystal was from the following Morpheus screen condition: 10% ...
Numerous significant hits in gapped BLAST to methionine aminopeptidases, e.g. residues 1-248 are 42% similar to (AF036708) of Mycoplasma gallisepticum, and residues 10-248 are 30% similar to AMP1_YEAST ...
Vibrio proteolyticus vibriolysin protein: a proteolytic enzyme secreted by the marine microorganism Vibrio proteolyticus; amino acid sequence given in first source
article{4bacc912-41d5-4b5a-8bf5-28fce4e1ba74, abstract = {Cancer is responsible for many deaths and is a major source of healthcare expenditures. The identification of new, non-invasive biomarkers might allow improvement of the direct diagnostic or prognostic ability of already available tools. Here, we took the innovative approach of interrogating the activity of exopeptidases in the serum of cancer patients with the aim of establishing a distinction based on enzymatic function, instead of simple protein levels, as a means to biomarker discovery. We first analyzed two well-characterized mouse models of prostate cancer, each with a distinct genetic lesion, and established that broad exopeptidase and targeted aminopeptidase activity tests reveal proteolytic changes associated with tumor development. We also describe new peptide-based freeze-frame reagents uniquely suited to probe the altered balance of selected aminopeptidases, as opposed to the full array of exopeptidases, and/or their ...
Cummins, P., M.; O'connor, B., 1996: Bovine brain pyroglutamyl aminopeptidase (type-1): Purification and characterisation of a neuropeptide-inactivating peptidase
This invention relates to the crystal structure of a plant peptide deformylase polypeptide and methods of using the structure to design compounds that modulate the activity of the polypeptide.
At least 115 mutations in the TPP1 gene have been found to cause CLN2 disease. This condition impairs motor and mental development, typically starting in early childhood, causing gradually worsening movement disorders and a decline in intellectual function. In addition, affected children often develop recurrent seizures (epilepsy) and vision impairment. In some cases, signs and symptoms of CLN2 disease do not appear until later in childhood, usually after age 4.. Most of the TPP1 gene mutations that cause CLN2 disease change single amino acids in tripeptidyl peptidase 1, resulting in a severe decrease in enzyme activity. A reduction in functional enzyme results in the incomplete breakdown of certain peptides. CLN2 disease is characterized by the accumulation of proteins or peptides and other substances in lysosomes. These accumulations occur in cells throughout the body; however, nerve cells seem to be particularly vulnerable to their effects. The accumulations can cause cell damage leading to ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
MicroRNA (miRNA) disorder is associated with a variety of human being illnesses, including malignancy. miR-671-5p lead in a change from epithelial-to-mesenchymal changeover (EMT) to mesenchymal-to-epithelial changeover (MET) phenotypes in MDA-MB-231 breasts malignancy cells and caused S-phase police arrest. Furthermore, miR-671-5p sensitive breasts malignancy cells to cisplatin, 5-fluorouracil (5-FU) and epirubicin publicity. Host cell reactivation (HCR) assays demonstrated that miR-671-5p decreases DNA restoration ability in post-drug revealed breasts malignancy cells. cDNA microarray data exposed that differentially indicated genetics when miR-671-5p was transfected are linked with cell growth, breach, cell routine, and EMT. These data suggest that miR-671-5p features as a growth suppressor miRNA in breasts cancer tumor by straight concentrating on FOXM1. Therefore, miR-671-5p might serve as a new therapeutic focus on for breasts cancer tumor administration. (DCIS), and culminates in the ...
MicroRNA (miRNA) disorder is associated with a variety of human being illnesses, including malignancy. miR-671-5p lead in a change from epithelial-to-mesenchymal changeover (EMT) to mesenchymal-to-epithelial changeover (MET) phenotypes in MDA-MB-231 breasts malignancy cells and caused S-phase police arrest. Furthermore, miR-671-5p sensitive breasts malignancy cells to cisplatin, 5-fluorouracil (5-FU) and epirubicin publicity. Host cell reactivation (HCR) assays demonstrated that miR-671-5p decreases DNA restoration ability in post-drug revealed breasts malignancy cells. cDNA microarray data exposed that differentially indicated genetics when miR-671-5p was transfected are linked with cell growth, breach, cell routine, and EMT. These data suggest that miR-671-5p features as a growth suppressor miRNA in breasts cancer tumor by straight concentrating on FOXM1. Therefore, miR-671-5p might serve as a new therapeutic focus on for breasts cancer tumor administration. (DCIS), and culminates in the ...
Methionine aminopeptidase (map) is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. The role of this protein in general is to produce the mature amino end of cytosolic proteins by removing the N-terminal methionine. This model describes type II, among which the eukaryotic members typically have an N-terminal extension not present in archaeal members. It can act cotranslationally. The enzyme from rat has been shown to associate with translation initiation factor 2 (IF-2) and may have a role in translational regulation ...
The neuronal ceroid lipofuscinoses (NCLs) are a group of inherited neurodegenerative disorders with pathological phenotypes that auto fluorescent lipopigments present in neurons and other cell types. Over the past two decades, accumulating evidences indicates that NCLs are caused by mutations in eight different genes, including genes encoding several soluble proteins (cathepsin D, PPT1, and TPP1).[7] Mutations of gene TPP1 result in late-infantile neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome.[8] Mutations in the TPP1 gene lead to late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood.[6] It has been demonstrated that a single injection of intravitreal implantation of autologous bone marrow derived stem cells transduced with a TPP1 expression construct at an early stage in the disease progression could substantially inhibit the development of ...
Treatment of manifestations: Treatment is currently symptomatic and palliative only. Seizures, malnutrition, gastroesophageal reflux, pneumonia, sialorrhea, depression and anxiety, spasticity, Parkinsonian symptoms, and dystonia can be effectively managed. Antiepileptic drugs (AEDs) should be selected with caution. Benzodiazepines may help control seizures, anxiety, and spasticity. Trihexyphenydate may improve dystonia and sialorrhea. Individuals with swallowing problems may benefit from placement of a gastric (G) tube.. Surveillance: Routine medical management of children and young adults with complex neurodisability will be relevant to all those affected by CLN, and may include surveillance for swallowing difficulties and recurrent aspiration and radiograph surveillance of hip joints and spine.. Agents/circumstances to avoid: Carbamazepine and phenytoin may increase seizure activity and myoclonus and result in clinical deterioration; lamotrigine may exacerbate seizures and myoclonus.. Genetic ...
ObjectiveTo describe subdural fluid collections on magnetic resonance imaging as part of the natural history of infantile neuronal ceroid lipofuscinosis.DesignC
A biochemical and histochemical investigation with specific substrates and inhibitors was used to visualize protease, esterase and aminopeptidase activities produced in situ during penetration of Calliphora vomitoria and Manduca sexta cuticles by hyphae of the entomopathogenic fungus Metarhizium anisopliae. Two endoproteases, and aminopeptidase and esterase activities, were mainly localized in simple and complex appressoria and germinating conidia. The effect of inhibitors on two characterized proteases (Pr1 and Pr2) and aminopeptidase activity in appressorial plates was quantified by microdensitometric measurement of reaction products. Pr1 and Pr2 activities were differentially inhibited by various protease inhibitors. Pr1, Pr2, esterase, aminopeptidase and N-acetylglucosaminidase (exochitinase) activities were present during penetration as detected directly following desorption from fungal and cuticle components. The proteases produced in situ were fractionated, and were shown by immunological ...
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Read "Physical mapping and partial genetic characterization of the Lactobacillus delbrueckii subsp. bulgaricus bacteriophage lb539, Archives of Virology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Adult-onset neuronal ceroid lipofuscinosis, also known as Kufs disease, is a neurodegenerative disorder without retinal involvement. There are 2 overlapping phenotypes: type A, characterized by progressive myoclonic epilepsy, and type B, characterized by dementia and a variety of motor-system signs (summary by {1:Arsov et al., 2011}). In general, the neuronal ceroid lipofuscinoses (NCL; CLN) are a clinically and genetically heterogeneous group of neurodegenerative disorders characterized by the intracellular accumulation of autofluorescent lipopigment storage material in different patterns ultrastructurally. The clinical course includes progressive dementia, seizures, and progressive visual failure ({8:Mole et al., 2005}). The ultrastructural pattern of lipopigment in CLN4 comprises a mixed pattern of granular, curvilinear, and fingerprint profiles. ({8:Mole et al., 2005}). For a general phenotypic description and a discussion of genetic heterogeneity of CLN, see CLN1 ({256730 ...

Leucyl/cystinyl aminopeptidase - WikipediaLeucyl/cystinyl aminopeptidase - Wikipedia

Leucyl/cystinyl aminopeptidase, also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human ... end and chromosomal assignment of human placental leucine aminopeptidase/insulin-regulated membrane aminopeptidase gene". ... Leucine aminopeptidase". Acta genetica et statistica medica. 16 (2): 122-31. doi:10.1159/000151957. PMID 5953194. Itoh C, ... Mutations in this gene have been associated to psoriasis risk.(doi:10.1038/jid.2013.317) Cystinyl aminopeptidase has been shown ...
more infohttps://en.wikipedia.org/wiki/Leucyl/cystinyl_aminopeptidase

ANPEP alanyl aminopeptidase, membrane [Homo sapiens (human)] - Gene - NCBIANPEP alanyl aminopeptidase, membrane [Homo sapiens (human)] - Gene - NCBI

aminopeptidase N. Names. AP-M. AP-N. alanyl (membrane) aminopeptidase. aminopeptidase M. hAPN. membrane alanyl aminopeptidase. ... ANPEP alanyl aminopeptidase, membrane [Homo sapiens] ANPEP alanyl aminopeptidase, membrane [Homo sapiens]. Gene ID:290 ... M1_APN_2; Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 ( ... M1_APN_2; Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 ( ...
more infohttps://www.ncbi.nlm.nih.gov/gene/?term=290

Leucine aminopeptidase legal definition of leucine aminopeptidaseLeucine aminopeptidase legal definition of leucine aminopeptidase

What is leucine aminopeptidase? Meaning of leucine aminopeptidase as a legal term. What does leucine aminopeptidase mean in law ... Definition of leucine aminopeptidase in the Legal Dictionary - by Free online English dictionary and encyclopedia. ... A leucine aminopeptidase gene of the Pacific oyster Crassostrea gigas exhibits an unusually high level of sequence variation, ... redirected from leucine aminopeptidase). Also found in: Dictionary, Thesaurus, Medical, Encyclopedia.. Related to leucine ...
more infohttps://legal-dictionary.thefreedictionary.com/leucine+aminopeptidase

Malarial aminopeptidase molecule - Stock Image C035/8499 - Science Photo LibraryMalarial aminopeptidase molecule - Stock Image C035/8499 - Science Photo Library

Computer model showing the structure of the M18 aspartyl aminopeptidase with a dodecameric assembly arranged via dimer and ... Caption: Malarial aminopeptidase molecule. Computer model showing the structure of the M18 aspartyl aminopeptidase with a ... Keywords: aminopeptidase, antimalarial, art, artwork, aspartyl, biochemical, biochemistry, biological, biology, compound, cut ...
more infohttp://www.sciencephoto.com/media/850907/view

arginyl aminopeptidase (aminopeptidase B)-like 1 ELISA Kits | Biocompare.comarginyl aminopeptidase (aminopeptidase B)-like 1 ELISA Kits | Biocompare.com

... aminopeptidase B)-like 1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and ... Your search returned 12 arginyl aminopeptidase (aminopeptidase B)-like 1 ELISA ELISA Kit across 1 supplier. ...
more infohttp://www.biocompare.com/pfu/110627/soids/2-318256/Assay_Kit/ELISA_arginyl_aminopeptidase_aminopeptidase_B-like_1

Discovery of Inhibitors of Insulin-Regulated Aminopeptidase as Cognitive EnhancersDiscovery of Inhibitors of Insulin-Regulated Aminopeptidase as Cognitive Enhancers

It has been proposed that the insulin-regulated aminopeptidase (IRAP) is the main target of Ang IV. This paper discusses ... Proteolytic cleavage by glutamyl aminopeptidase A (AP-A) and membrane alanyl aminopeptidase N (AP-N), for example, results in ... IRAP has been identified as cystinyl aminopeptidase (CAP, EC 3.4.11.3), placental leucine aminopeptidase (P-LAP, soluble human ... K. Ito, Y. Nakajima, Y. Onohara et al., "Crystal structure of aminopeptidase N (Proteobacteria alanyl aminopeptidase) from ...
more infohttps://www.hindawi.com/journals/ijhy/2012/789671/

Produktübersicht 7 Aspartyl Aminopeptidase ProteineProduktübersicht 7 Aspartyl Aminopeptidase Proteine

... vergleichen Sie unsere Aspartyl Aminopeptidase Proteine von vielen Spezies. Finden Sie das richtige Produkt auf antikoerper- ... Aspartyl Aminopeptidase (DNPEP) Protein Überblick Protein Überblick The protein encoded by this gene is an aminopeptidase which ... Aspartyl Aminopeptidase Proteine (DNPEP). The protein encoded by DNPEP is an aminopeptidase which prefers acidic amino acids, ... Human Aspartyl Aminopeptidase (DNPEP) Interaktionspartner * aspartyl aminopeptidase was upregulated in colorectal cancer ...
more infohttp://www.antikoerper-online.de/abstract/Aspartyl+Aminopeptidase+

Diagnostic usefulness of dipeptidyl aminopeptidase IV monoclonal antibody in paraffin-embedded thyroid follicular tumours -...Diagnostic usefulness of dipeptidyl aminopeptidase IV monoclonal antibody in paraffin-embedded thyroid follicular tumours -...

Marcus A. Lima, Valéria A. Gontijo, Fernando C. L. Schmitt, CD26 (dipeptidyl aminopeptidase IV) expression in normal and ... Monoclonal antibodies to dipeptidyl aminopeptidase IV (DAP IV, EC 3.4.14.5) were raised and selectively applied to paraffin- ... Diagnostic usefulness of dipeptidyl aminopeptidase IV monoclonal antibody in paraffin-embedded thyroid follicular tumours. ... Dipeptidyl aminopeptidase IV in the cytologic diagnosis of thyroid carcinoma, Diagnostic Cytopathology, 1998, 19, 1, 4. Wiley ...
more infohttp://onlinelibrary.wiley.com/doi/10.1002/path.1711680108/abstract?globalMessage=0

Promoter methylation of aminopeptidase N/CD13 in malignant melanoma  - Zurich Open Repository and ArchivePromoter methylation of aminopeptidase N/CD13 in malignant melanoma - Zurich Open Repository and Archive

Aminopeptidase N (APN)/CD13 as ubiquitously expressed membrane peptidase exerts important functions in diverse cellular ... Aminopeptidase N (APN)/CD13 as ubiquitously expressed membrane peptidase exerts important functions in diverse cellular ... Download PDF Promoter methylation of aminopeptidase N/CD13 in malignant melanoma. Item availability may be restricted. ... Download PDF Promoter methylation of aminopeptidase N/CD13 in malignant melanoma. Item availability may be restricted. ...
more infohttp://www.zora.uzh.ch/id/eprint/64933/

Circulating Aminopeptidase N/CD13 Is an Independent Prognostic Factor in Patients with Non-Small Cell Lung Cancer | Clinical...Circulating Aminopeptidase N/CD13 Is an Independent Prognostic Factor in Patients with Non-Small Cell Lung Cancer | Clinical...

Association of serum aminopeptidase N/CD13 level with clinicopathologic variables. A high serum aminopeptidase N/CD13 level was ... The origin of circulating aminopeptidase N/CD13 is unclear at present. In our series, serum aminopeptidase N/CD13 levels were ... High levels of circulating aminopeptidase N/CD13 may, at least in part, reflect high levels of aminopeptidase N/CD13 expression ... In this study, we determined serum aminopeptidase N/CD13 concentrations in patients with NSCLC using an aminopeptidase N/CD13- ...
more infohttp://clincancerres.aacrjournals.org/content/11/24/8674.long

Crystal Structure of Insulin-Regulated Aminopeptidase with Bound Substrate Analogue Provides Insight on Antigenic Epitope...Crystal Structure of Insulin-Regulated Aminopeptidase with Bound Substrate Analogue Provides Insight on Antigenic Epitope...

endoplasmic reticulum aminopeptidase. hPhe. homophenylalanine. IRAP. insulin-regulated aminopeptidase. PDB. Protein Data Bank. ... The three aminopeptidases have been recently classified under the oxytocinase subfamily of M1 aminopeptidases and characterized ... As a result, aminopeptidases that are tasked with further processing these peptides have to be able to recognize a very large ... The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism. Proc. Natl ...
more infohttp://www.jimmunol.org/content/195/6/2842

Aminopeptidase N (Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or Microsomal...Aminopeptidase N (Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or Microsomal...

Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or Microsomal Aminopeptidase or gp150 or ... Aminopeptidase N (Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or Microsomal ... The report reviews Aminopeptidase N (Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or ... The report assesses Aminopeptidase N (Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or ...
more infohttps://www.marketresearch.com/Global-Markets-Direct-v3480/Aminopeptidase-Myeloid-Plasma-Membrane-Glycoprotein-11296626/

Investigations towards the mechanisms of action of insulin-regulated aminopeptidase ligands in spatial memory and limbic...Investigations towards the mechanisms of action of insulin-regulated aminopeptidase ligands in spatial memory and limbic...

Investigations towards the mechanisms of action of insulin-regulated aminopeptidase ligands in spatial memory and limbic ... Investigations towards the mechanisms of action of insulin-regulated aminopeptidase ligands in spatial memory and limbic ...
more infohttps://www.vub.be/en/events/2009/investigations-towards-mechanisms-action-insulin-regulated-aminopeptidase-ligands

Bovine brain pyroglutamyl aminopeptidase (type-1): Purification and characterisation of a neuropeptide-inactivating peptidase -...Bovine brain pyroglutamyl aminopeptidase (type-1): Purification and characterisation of a neuropeptide-inactivating peptidase -...

Bovine brain pyroglutamyl aminopeptidase (type-1): Purification and characterisation of a neuropeptide-inactivating peptidase ... Pyroglutamyl aminopeptidase type-1 (PAP-I) is reported to be a soluble, broad specificity aminopeptidase, capable of removing ... Bovine brain pyroglutamyl aminopeptidase (type-1): Purification and characterisation of a neuropeptide-inactivating peptidase. ... Cummins, P., M.; O'connor, B., 1996: Bovine brain pyroglutamyl aminopeptidase (type-1): Purification and characterisation ...
more infohttps://geoscience.net/research/008/241/008241925.php

ENPEP Gene - GeneCards | AMPE Protein | AMPE AntibodyENPEP Gene - GeneCards | AMPE Protein | AMPE Antibody

Glutamyl Aminopeptidase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human ... R&D Systems Antibodies for ENPEP (Aminopeptidase A/ENPEP). *R&D Systems Proteins and Enzymes for ENPEP (Aminopeptidase A/ENPEP) ... cDNA cloning and expression of human glutamyl aminopeptidase (aminopeptidase A). (PMID: 8244382) Li L … Cooper MD (Genomics ... High-resolution genetic map of the human glutamyl aminopeptidase gene (ENPEP). (PMID: 9268642) Li L … Cooper MD (Genomics 1997) ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=ENPEP

Ruth Landau - NeL.eduRuth Landau - NeL.edu

Journal Article 2010; 31(1): 63-66 PubMed PMID: 20150869 Keywords: Case-Control Studies, Cystinyl Aminopeptidase:blood, Down- ... Alteration of circulating Placental Leucine Aminopeptidase (P-LAP) activity in preeclampsia.. Landau R, Laverrière A, Bischof P ... Landau R, Laverrière A, Bischof P, Irion O, Morales M, Cohen M. Alteration of circulating Placental Leucine Aminopeptidase (P- ...
more infohttp://www.nel.edu/landau-6113/

Aminopeptidase - WikipediaAminopeptidase - Wikipedia

One important aminopeptidase is a zinc-dependent enzyme produced and secreted by glands of the small intestine. It helps the ... Aminopeptidases are enzymes that catalyze the cleavage of amino acids from the amino terminus (N-terminus) of proteins or ... Aminopeptidases are used in essential cellular functions. Many, but not all, of these peptidases are zinc metalloenzymes. Some ... Alanine aminopeptidase Carboxypeptidase PDB: 3QNF​: Vollmar, M.; Kochan, G.; Krojer, T.; Harvey, D.; Chaikuad, A.; Allerston, C ...
more infohttps://en.wikipedia.org/wiki/Aminopeptidase

Aminopeptidase Y - WikipediaAminopeptidase Y - Wikipedia

Aminopeptidase Y (EC 3.4.11.15, aminopeptidase Co, aminopeptidase (cobalt-activated), lysyl aminopeptidase) is an enzyme. This ... Sequence analysis and gene disruption of a new aminopeptidase". J. Biol. Chem. 269: 13651-13655. PMID 8175800. Aminopeptidase Y ... Yasuhara, T.; Nakai, T.; Ohashi, A. (1994). "Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. Purification ... Nishizawa, M.; Yasuhara, T.; Nakai, T.; Fujiki, Y.; Ohashi, A. (1994). "Molecular cloning of the aminopeptidase Y gene of ...
more infohttps://en.wikipedia.org/wiki/Aminopeptidase_Y

Aminopeptidase | Define Aminopeptidase at Dictionary.comAminopeptidase | Define Aminopeptidase at Dictionary.com

Aminopeptidase definition, any of several intestinal hydrolytic enzymes that remove an amino acid from the end of a peptide ... aminopeptidase in Medicine Expand. aminopeptidase a·mi·no·pep·ti·dase (ə-mēnō-pěptĭ-dās, -dāz, āmə-nō-). n. Any of various ...
more infohttp://www.dictionary.com/browse/aminopeptidase

Leucine aminopeptidase - urine: MedlinePlus Medical EncyclopediaLeucine aminopeptidase - urine: MedlinePlus Medical Encyclopedia

Leucine aminopeptidase is a type of protein called an enzyme. It is normally found in liver cells and cells of the small ... Leucine aminopeptidase is a type of protein called an enzyme. It is normally found in liver cells and cells of the small ...
more infohttps://medlineplus.gov/ency/article/003617.htm

Aspartyl aminopeptidase (Q9ULA0) | InterPro | EMBL-EBIAspartyl aminopeptidase (Q9ULA0) | InterPro | EMBL-EBI

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
more infohttp://www.ebi.ac.uk/interpro/protein/Q9ULA0

AminopeptidaseAminopeptidase

... on WN Network delivers the latest Videos and Editable pages for News & Events, including Entertainment, Music, ... Aminopeptidase Y. Aminopeptidase Y (EC 3.4.11.15, aminopeptidase Co, aminopeptidase (cobalt-activated), lysyl aminopeptidase) ... Aminopeptidase S. Aminopeptidase S (EC 3.4.11.24, Mername-AA022 peptidase, SGAP, aminopeptidase (Streptomyces griseus), ... Aminopeptidase N (Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or Microsomal .... *. ...
more infohttps://wn.com/Aminopeptidase

Probable cytosol aminopeptidase (C1DPG2) | InterPro | EMBL-EBIProbable cytosol aminopeptidase (C1DPG2) | InterPro | EMBL-EBI

Peptidase M17, leucine aminopeptidase/peptidase B (IPR011356)*Peptidase M17, leucine aminopeptidase (IPR023042) ... GO:0004177 aminopeptidase activity GO:0008235 metalloexopeptidase activity GO:0030145 manganese ion binding ...
more infohttps://www.ebi.ac.uk/interpro/protein/C1DPG2

Specific Inhibitors of Aminopeptidase P | SpringerLinkSpecific Inhibitors of Aminopeptidase P | SpringerLink

Aminopeptidase P (APP, EC 3.4.11.9) is a metal-dependent proline-specific peptidase. The enzyme splits N-terminal Xaa-Pro ... aminopeptidase B and aminopeptidase M.4 X-ray crystallografic results demonstrated the bestatin chelation of one of the active ... Simmons, W. H. and Orawski, A. T.: Membrane-bound Aminopeptidase P from Bovine Lung. J. Biol. Chem. 267: 4897-4903, 1992.PubMed ... Aminopeptidase P (APP, EC 3.4.11.9) is a metal-dependent proline-specific peptidase. The enzyme splits N-terminal Xaa-Pro ...
more infohttps://link.springer.com/chapter/10.1007/978-1-4757-9613-1_5

Leucine aminopeptidase urine test: MedlinePlus Medical Encyclopedia ImageLeucine aminopeptidase urine test: MedlinePlus Medical Encyclopedia Image

Leucine aminopeptidase (LAP) is a proteolytic enzyme that breaks chemical bonds in proteins at specific sites next to leucine ... Leucine aminopeptidase (LAP) is a proteolytic enzyme that breaks chemical bonds in proteins at specific sites next to leucine ...
more infohttps://medlineplus.gov/ency/imagepages/9501.htm
  • Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. (nih.gov)
  • Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. (nih.gov)
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