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Aminopeptidase activity
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Advances in the knowledge of renal neoplasms have demonstrated the implication of several proteases in their genesis, growth and dissemination. Glutamyl-aminopeptidase (GAP) (EC. 3.4.11.7) is a zinc metallopeptidase with angiotensinase activity highly expressed in kidney tissues and its expression and activity have been associated wtih tumour development.
9p
virose2711
24-09-2020
9
1
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Melphalan has been used in the treatment of various hematologic malignancies for almost 60 years. Today it is part of standard therapy for multiple myeloma and also as part of myeloablative regimens in association with autologous allogenic stem cell transplantation. Melflufen (melphalan flufenamide ethyl ester, previously called J1) is an optimized derivative of melphalan providing targeted delivery of active metabolites to cells expressing aminopeptidases.
9p
vinaypyidaw2711
26-08-2020
25
2
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Antigen-processing machinery molecules play crucial roles in infectious diseases and cancers. Studies have shown that polymorphisms in endoplasmic reticulum aminopeptidase (ERAP) genes can influence the enzymatic activity of ERAP proteins and are associated with the risk of diseases.
11p
viorochimaru2711
01-06-2020
6
1
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In this study, the intracellular aminopeptidase activities and volatile’s profiles of seventeen Tetragenococcus halophilus strains, which were isolated previously from fish mash, were investigated.
7p
vidonut2711
08-11-2019
14
0
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Enzym từ ruột ấu trùng cá giò gồm alkaline phosphatase (AP), leucine aminopeptidase (LAP) và leucine-alanine peptidase (leu-ala) xuất hiện ngay từ khi ấu trùng ăn thức ăn ngoài (2 ngày tuổi) và hoạt tính của chúng tăng mạnh cùng với sự tăng trưởng của cá. Hoạt tính chuyên biệt (specifi c activity) của enzym màng thành ruột (bbm) AP tăng từ ngày 23 đến 26 ngày tuổi ở cá sử dụng hoàn toàn thức ăn sống (LF) (P < 0,05) và tăng từ 26 đến 30 ngày tuổi (P < 0,05) ở cá sử dụng thức ăn công nghiệp (L-MD) từ 17 ngày tuổi.
7p
advanger1
06-05-2018
56
0
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The importance of two putative Zn2+-binding (Asp347, Glu429) and two catalytic (Arg431, Lys354) residues in the tomato leucine aminopeptidase (LAP-A) function was tested. The impact of substitutions at these positions, corresponding to the bovine LAP residues Asp255, Glu334, Arg336, and Lys262, was evaluated in His6–LAP-A fusion proteins expressed in Escherichia coli. Sixty-five percent of the mutant His6–LAP-A proteins were unstable or had complete or partial defects in hexamer assembly or stability. The activity of hexameric His6–LAP-As on Xaa-Leu and Leu-Xaa dipeptides was tested.
11p
system191
01-06-2013
33
3
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Transglutaminase (TGase) fromStreptomyces mobaraensis is secreted as a precursor protein which is completely acti-vated by the endoprotease TAMEP, a member of the M4 protease family [Zotzel, J., Keller, P. & Fuchsbauer, H.-L. (2003) Eur. J. Biochem. 270, 3214–3222]. In contrast with the mature enzyme, TAMEP-activated TGase exhibits an additional N-terminal tetrapeptide (Phe-Arg-Ala-Pro) sug-gesting truncation, at least, by a second protease.
7p
tumor12
20-04-2013
49
1
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X-prolyl dipeptidyl aminopeptidases (X-PDAP) are enzymes catalysing the release of dipeptides from the amino termini of polypeptides containing a proline or an alanine at the penultimate position. Involved in various mam-malian regulation processes, as well as in chronic human diseases, they have been proposed to play a role in pathogenicity forStreptococci.
10p
awards
06-04-2013
30
2
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Human glutamate carboxypeptidase II (GCPII) is a co-catalytic metallopeptidase and its putative catalytic domain is homologous to the aminopeptidases fromVibrio proteolyticus and Streptomyces griseus.In humans, the enzyme is expressed predominantly in the nervous system and theprostate.Theprostate form, termedprostate-specific membraneantigen, is overexpressed inprostate cancer and is used as a diagnostic marker of the disease.II
9p
dell39
03-04-2013
34
2
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Aspartyl aminopeptidase (EC 3.4.11.21) cleaves only unblocked N-terminal acidic amino-acid residues. To date, it has been found only in mammals. We report here that aspartyl aminopeptidase activity is present in yeast. Yeast aminopeptidase is encoded by an uncharacterized gene in chromo-some VIII ( 1 YHR113W, Saccharomyces Genome Database).
7p
dell39
27-03-2013
44
3
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Human colon adenocarcinoma cells (HT29-ATCC) and the clone HT29-5F7 were cultured under conditions that differentiate cells to a polarized intestinal phenotype. Differentiated cells showed the presence of junctional complexes and intercellular lumina bordered by microvilli. Intestinal brush border hydrolase activities (sucrase, aminopeptidase N, lactase and mal-tase) were detected mainly in differentiated HT29-ATCC cells compared with the differentiated clone, HT29-5F7.
10p
inspiron33
25-03-2013
36
2
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The catalytic mechanism underlying the aminopeptidase fromStreptomyces griseus (SGAP) was investigated. pH-dependent activity profiles revealed the enthalpy of ionization for the hydrolysis of leucine-para-nitroanilide by SGAP. The value obtained (30 ± 5 kJÆmol )1 ) is typical of a zinc-bound water molecule, suggesting that the zinc-bound water⁄hydroxide molecule acts as the reaction nucleophile.
13p
galaxyss3
21-03-2013
62
2
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A new leucyl aminopeptidase activity has been identified in the fission yeast Schizosaccharomyces pombe. The enzyme, which has been purified and named leucyl aminopeptidase yspII (LAP yspII), had a molecular mass of 320 and 54 kDa by gel filtration and SDS⁄PAGE, respectively, suggesting a homohexameric structure.
13p
media19
05-03-2013
41
2
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An active site aspartate residue, Asp97, in the methionine aminopeptidase (MetAPs) from Escherichia coli(EcMetAP-I) was mutated to alanine, glu-tamate, and asparagine. Asp97 is the lone carboxylate residue bound to the crystallographically determined second metal-binding site in EcMetAP-I.
12p
vinaphone15
28-02-2013
21
1
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DPP IV has been attributed a large array of functions, some of which are mediated by its exopeptidase activity. Although it only removes two amino acid residues at the N-terminus of the peptide, this cleavage can inactivate or modify the activity of regulatory peptides, peptide hormones, chemokines and neuropeptides. Several excellent DPP IV substrates with high specificity constants were identified by the in vitro kinetic study of the truncation of bioactive peptides by DPP IV. In vivo studies e.g.
228p
hyperion75
18-01-2013
56
6
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