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Journal articles on the topic 'Aminopeptidase inhibition'

Author: Grafiati

Published: 4 June 2025

Last updated: 1 August 2025

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1

Baranczyk-Kuzma, Anna, and Kenneth L. Audus. "Characteristics of Aminopeptidase Activity from Bovine Brain Microvessel Endothelium." Journal of Cerebral Blood Flow & Metabolism 7, no. 6 (1987): 801–5. http://dx.doi.org/10.1038/jcbfm.1987.137.

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Blood–brain barrier (BBB) aminopeptidase activity was investigated using an in vitro model consisting of primary cultures of brain microvessel endothelium. Using two different substrates, both membrane-bound and soluble aminopeptidases were found to be associated with brain endothelium. That the enzyme activity was aminopeptidase activity was confirmed with the competitive inhibition of substrate degradation by typical aminopeptidase inhibitors puromycin and bestatin. The aminopeptidase activity was also competitively inhibited by enkephalin, met-enkephalin, and leu-enkephalin. Results from pa

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2

Sanz, Yolanda, and Fidel Toldrá. "Myoglobin as an Inhibitor of Exopeptidases from Lactobacillus sake." Applied and Environmental Microbiology 64, no. 6 (1998): 2313–14. http://dx.doi.org/10.1128/aem.64.6.2313-2314.1998.

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ABSTRACT The effects of myoglobin on exopeptidases of Lactobacillus sake were determined. Inhibition of the aminopeptidases increased as the myoglobin concentration increased; aminopeptidase 3 was the most affected (90% inhibition). Aminopeptidases 1, 2, and 4 showed similar inhibition levels (around 60%). Myoglobin did not affect tripeptidase activity. Thus, myoglobin could limit amino acid generation in meat systems.

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3

Cunningham, Eithne, Marcin Drag, Pawel Kafarski та Angus Bell. "Chemical Target Validation Studies of Aminopeptidase in Malaria Parasites Using α-Aminoalkylphosphonate and Phosphonopeptide Inhibitors". Antimicrobial Agents and Chemotherapy 52, № 9 (2008): 3221–28. http://dx.doi.org/10.1128/aac.01327-07.

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ABSTRACT During its intraerythrocytic phase, the most lethal human malarial parasite, Plasmodium falciparum, digests host cell hemoglobin as a source of some of the amino acids required for its own protein synthesis. A number of parasite endopeptidases (including plasmepsins and falcipains) process the globin into small peptides. These peptides appear to be further digested to free amino acids by aminopeptidases, enzymes that catalyze the sequential cleavage of N-terminal amino acids from peptides. Aminopeptidases are classified into different evolutionary families according to their sequence

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4

Dalal, Seema, and Michael Klemba. "Roles for Two Aminopeptidases in Vacuolar Hemoglobin Catabolism in Plasmodium falciparum." Journal of Biological Chemistry 282, no. 49 (2007): 35978–87. http://dx.doi.org/10.1074/jbc.m703643200.

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During the erythrocytic stage of its life cycle, the human malaria parasite Plasmodium falciparum catabolizes large quantities of host-cell hemoglobin in an acidic organelle, the food vacuole. A current model for the catabolism of globin-derived oligopeptides invokes peptide transport out of the food vacuole followed by hydrolysis to amino acids by cytosolic aminopeptidases. To test this model, we have examined the roles of four parasite aminopeptidases during the erythrocytic cycle. Localization of tagged aminopeptidases, coupled with biochemical analysis of enriched food vacuoles, revealed t

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5

Salomon, Emmanuel, Marjorie Schmitt, Anil Marapaka, et al. "Aminobenzosuberone Scaffold as a Modular Chemical Tool for the Inhibition of Therapeutically Relevant M1 Aminopeptidases." Molecules 23, no. 10 (2018): 2607. http://dx.doi.org/10.3390/molecules23102607.

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The synthesis of racemic substituted 7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one hydrochlorides was optimized to enhance reproducibility and increase the overall yield. In order to investigate their specificity, series of enzyme inhibition assays were carried out against a diversity of proteases, covering representative members of aspartic, cysteine, metallo and serine endopeptidases and including eight members of the monometallic M1 family of aminopeptidases as well as two members of the bimetallic M17 and M28 aminopeptidase families. This aminobenzosuberone scaffold indeed demonstrated

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6

Jackson, M. C., Y. Choudry, A. Bourne, J. F. Woodley, and A. J. Kenny. "A fluorimetric assay for aminopeptidase W." Biochemical Journal 253, no. 1 (1988): 299–302. http://dx.doi.org/10.1042/bj2530299.

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A novel two-step enzyme-linked assay for aminopeptidase W is described and validated by comparison with other assays. L-alpha-Glutamyl-L-tryptophan (Glu-Trp) is a favoured substrate for this enzyme. With the use of glutamate dehydrogenase (EC 1.4.1.2) in a second step, the assay measured the release of free glutamate from L-alpha-glutamyl-L-tryptophan by the increase in NADH fluorescence. In the presence of 5 mM-1,10-phenanthroline and 50 microM-cilastatin the contribution of other membrane peptidases, in particular aminopeptidases N and A and microsomal dipeptidase in kidney, was very small.

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7

Farsa, Oldřich, Veronika Ballayová, Radka Žáčková, Peter Kollar, Tereza Kauerová, and Peter Zubáč. "Aminopeptidase N Inhibitors as Pointers for Overcoming Antitumor Treatment Resistance." International Journal of Molecular Sciences 23, no. 17 (2022): 9813. http://dx.doi.org/10.3390/ijms23179813.

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Aminopeptidase N (APN), also known as CD13 antigen or membrane alanyl aminopeptidase, belongs to the M1 family of the MA clan of zinc metallopeptidases. In cancer cells, the inhibition of aminopeptidases including APN causes the phenomenon termed the amino acid deprivation response (AADR), a stress response characterized by the upregulation of amino acid transporters and synthetic enzymes and activation of stress-related pathways such as nuclear factor kB (NFkB) and other pro-apoptotic regulators, which leads to cancer cell death by apoptosis. Recently, APN inhibition has been shown to augment

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8

Hooper, N. M., R. J. Hesp, and S. Tieku. "Metabolism of aspartame by human and pig intestinal microvillar peptidases." Biochemical Journal 298, no. 3 (1994): 635–39. http://dx.doi.org/10.1042/bj2980635.

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The artificial sweetener aspartame (N-L-alpha-aspartyl-L-phenyl-alanine-1-methyl ester; Nutrasweet), its decomposition product alpha Asp-Phe and the related peptide alpha Asp-PheNH2 were rapidly hydrolysed by microvillar membranes prepared from human duodenum, jejunum and ileum, and from pig duodenum and kidney. The metabolism of aspartame by the human and pig intestinal microvillar membrane preparations was inhibited significantly (> 78%) by amastatin or 1,10-phenanthroline, and partially (> 38%) by actinonin or bestatin, and was activated 2.9-4.5-fold by CaCl2. The inhibition by amasta

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9

Herranz, Rosario, Julia Castro-Pichel, M. Teresa García-López, Isabel Gómez-Monterrey, Concepción Pérez, and Soledad Vinuesa. "Ketomethylenebestatin: Synthesis and Aminopeptidase Inhibition." Archiv der Pharmazie 326, no. 7 (1993): 395–98. http://dx.doi.org/10.1002/ardp.19933260705.

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10

Albiston, Anthony L., Mauricio Cacador, Puspha Sinnayah, Peta Burns, and Siew Yeen Chai. "Insulin-regulated aminopeptidase inhibitors do not alter glucose handling in normal and diabetic rats." Journal of Molecular Endocrinology 58, no. 4 (2017): 193–98. http://dx.doi.org/10.1530/jme-17-0033.

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Insulin-regulated aminopeptidase (IRAP) co-localizes with the glucose transporter 4 (GLUT4) in GLUT4 storage vesicles (GSV) in insulin-responsive cells. In response to insulin, IRAP is the only transmembrane enzyme known to translocate together with GLUT4 to the plasma membrane in adipocytes and muscle cells. Although the intracellular region of IRAP is associated with GLUT4 vesicle trafficking, the role of the aminopeptidase activity in insulin-responsive cells has not been elucidated. The aim of this study was to investigate whether the inhibition of the aminopeptidase activity of IRAP facil

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11

Davies, Faith E., Hannah E. Moore, Emma L. Davenport, et al. "Aminopeptidase Inhibition as a Targeted Treatment Strategy in Myeloma." Blood 110, no. 11 (2007): 2505. http://dx.doi.org/10.1182/blood.v110.11.2505.2505.

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Abstract Myeloma cells are highly dependent on the unfolded protein response to assemble folded immunoglobulins correctly. Therefore targeting protein handling within a myeloma cell by inhibiting the aminopeptidase enzyme system that catalyses the hydrolysis of amino acids from the N terminus of proteins may be a novel therapeutic approach. The effect of the aminopeptidase inhibitor CHR-2797 on myeloma cell proliferation and survival, gene expression, protein turnover, cell migration and myeloma-bone marrow stromal cell interactions was determined on a panel of myeloma cell lines and patient c

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12

Menozzi, D., Z. F. Gu, P. N. Maton, and N. W. Bunnett. "Inhibition of peptidases potentiates enkephalin-stimulated contraction of gastric muscle cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 261, no. 3 (1991): G476—G484. http://dx.doi.org/10.1152/ajpgi.1991.261.3.g476.

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Cell surface peptidases degrade enkephalins and thereby restrict the number of molecules available to activate receptors. The effects of peptidase inhibitors on degradation of enkephalins and on enkephalin-stimulated contraction of gastric smooth muscle cells were examined. Muscle cells dispersed from the guinea pig stomach degraded [Tyr1-3H] [Leu5]enkephalin (41.6 +/- 9.0% degradation at 60 min incubation, mean +/- SD, n = 4 animals). Amastatin (10 microM, an aminopeptidase inhibitor) inhibited degradation by 72.1 +/- 1.5% The residual peptidase activity was inhibited by phosphoramidon (1 mic

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13

R. Helgren, Travis, Phumvadee Wangtrakuldee, Bart L. Staker, and Timothy J. Hagen. "Advances in Bacterial Methionine Aminopeptidase Inhibition." Current Topics in Medicinal Chemistry 16, no. 4 (2015): 397–414. http://dx.doi.org/10.2174/1568026615666150813145410.

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14

Lu, Jing-Ping, Sergio C. Chai, and Qi-Zhuang Ye. "Catalysis and Inhibition ofMycobacterium tuberculosisMethionine Aminopeptidase." Journal of Medicinal Chemistry 53, no. 3 (2010): 1329–37. http://dx.doi.org/10.1021/jm901624n.

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15

Simmons, William H. "Inhibition of Membrane-Bound Aminopeptidase P." Emerging Therapeutic Targets 1, no. 1 (1997): 125–28. http://dx.doi.org/10.1517/14728222.1.1.125.

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16

Marinova, Margarita D., and Bozhidar P. Tchorbanov. "Preparation of Antioxidant Enzymatic Hydrolysates from Honeybee-Collected Pollen Using Plant Enzymes." Enzyme Research 2010 (January 9, 2010): 1–5. http://dx.doi.org/10.4061/2010/415949.

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Enzymatic hydrolysates of honeybee-collected pollen were prepared using food-grade proteinase and aminopeptidases entirely of plant origin. Bromelain from pineapple stem was applied (8 mAU/g substrate) in the first hydrolysis stage. Aminopeptidase (0.05 U/g substrate) and proline iminopeptidase (0.03 U/g substrate) from cabbage leaves (Brassica oleracea var. capitata), and aminopeptidase (0.2 U/g substrate) from chick-pea cotyledons (Cicer arietinum L.) were involved in the additional hydrolysis of the peptide mixtures. The degree of hydrolysis (DH), total phenolic contents, and protein conten

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17

Poloz, Yekaterina, Andrew Catalano, and Danton H. O'Day. "Bestatin Inhibits Cell Growth, Cell Division, and Spore Cell Differentiation in Dictyostelium discoideum." Eukaryotic Cell 11, no. 4 (2012): 545–57. http://dx.doi.org/10.1128/ec.05311-11.

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ABSTRACTBestatin methyl ester (BME) is an inhibitor of Zn2+-binding aminopeptidases that inhibits cell proliferation and induces apoptosis in normal and cancer cells. We have usedDictyosteliumas a model organism to study the effects of BME. Only two Zn2+-binding aminopeptidases have been identified inDictyosteliumto date, puromycin-sensitive aminopeptidase A and B (PsaA and PsaB). PSA from other organisms is known to regulate cell division and differentiation. Here we show that PsaA is differentially expressed throughout growth and development ofDictyostelium, and its expression is regulated b

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18

Jenkins, Christopher, Ken Mills, Chris Pepper, and Burnett Alan. "Cellular Aminopeptidase Inhibition as a Target for the Therapy of AML by the Novel Agent CHR 2797." Blood 110, no. 11 (2007): 1608. http://dx.doi.org/10.1182/blood.v110.11.1608.1608.

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Abstract CHR 2797 is one of a new class of enzyme inhibitors with pleiotropic effects against cancer cells which is currently in Phase II clinical trials. It inhibits a number of the M1 family of metalloenzymes that include the Zn++-dependent aminopeptidases. Aminopeptidases catalyze the hydrolysis of the terminal amino acids from short chain polypeptides, and are involved in the continuous cycle of protein formation and degradation in cells. As malignant cells may be more dependent on protein cycling than normal cells, interrupting this pathway is, therefore, a potential therapeutic target fo

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19

Egli, Christine M., Regiane S. Natumi, Martin R. Jones, and Elisabeth M. L. Janssen. "Inhibition of Extracellular Enzymes Exposed to Cyanopeptides." CHIMIA International Journal for Chemistry 74, no. 3 (2020): 122–28. http://dx.doi.org/10.2533/chimia.2020.122.

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Harmful cyanobacterial blooms in freshwater ecosystems produce bioactive secondary metabolites including cyanopeptides that pose ecological and human health risks. Only adverse effects of one class of cyanopeptides, microcystins, have been studied extensively and have consequently been included in water quality assessments. Inhibition is a commonly observed effect for enzymes exposed to cyanopeptides and has mostly been investigated for human biologically relevant model enzymes. Here, we investigated the inhibition of ubiquitous aquatic enzymes by cyanobacterial metabolites. Hydrolytic enzymes

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20

Chauvel, Eric N., Catherine Llorens-Cortes, Pascale Coric, Sherwin Wilk, Bernard P. Roques, and Marie-Claude Fournie-Zaluski. "Differential Inhibition of Aminopeptidase A and Aminopeptidase N by New .beta.-Amino Thiols." Journal of Medicinal Chemistry 37, no. 18 (1994): 2950–57. http://dx.doi.org/10.1021/jm00044a016.

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21

Ramírez-Expósito, María Jesús, and José Manuel Martínez-Martos. "Differential Effects of Doxazosin on Renin-Angiotensin-System- Regulating Aminopeptidase Activities in Neuroblastoma and Glioma Tumoral Cells." CNS & Neurological Disorders - Drug Targets 18, no. 1 (2019): 29–36. http://dx.doi.org/10.2174/1871527317666181029111739.

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Background: It has been described that doxazosin, an antihypertensive drug, also promotes glioblastoma cells death by inhibiting cell proliferation, arresting cell cycle and inducing apoptosis. Doxazosin has also demonstrated several modulator effects on renin-angiotensin system (RAS)- regulating aminopeptidase activities, which are highly involved in tumor growth in experimental glioma. Therefore, it remains to elucidate if the anti-tumoral effects of doxazosin could also be mediated by the proteolytic regulatory components of the RAS. Objective: To analyze the effects of doxazosin on cell gr

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22

Bykov, V. V., A. A. Vologzhannikova, M. V. Trunilina, T. A. Kudryashov, A. S. Sokolov, and Yu S. Lapteva. "Cloning of the Thermus thermophilus methionine aminopeptidase gene and confirmation of the enzyme functional activity." Acta Biomedica Scientifica 9, no. 5 (2024): 75–83. http://dx.doi.org/10.29413/abs.2024-9.5.8.

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Background. Methionine aminopeptidases (MAPs) are a class of enzymes that catalyze the removal of the N-terminal initiator methionine from a polypeptide chain. Bacterial MAPs are considered as targets for the development of broad-spectrum antibacterial drugs, and using MAPs in biotechnology necessitates the search for new MAPs and the study of their functioning and inhibition mechanisms.The aim of the study. To identify methionine aminopeptidase in the Thermus thermophilus genome (Tt-MAP) and to confirm its functional activity.Materials and methods. To identify Tt-MAP, we analyzed the Thermus

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23

Jenkins, Christopher, Chris Pepper, Ken Mills, and Alan Burnett. "Inhibition of Cellular Aminopeptidases as Novel Therapy for AML." Blood 108, no. 11 (2006): 2588. http://dx.doi.org/10.1182/blood.v108.11.2588.2588.

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Abstract CHR 2797 is one of a new class of enzyme inhibitors with a pleiotropic effect against a number of human cancer cells. It is thought to inhibit the M1 family of metalloenzymes that include aminopeptidases, and is under investigation for the treatment of acute myeloid leukemia. Aminopeptidases catalyse the hydrolysis of the terminal amino acids from short chain polypeptides and they are involved in the continuous cycle of protein formation and degradation in cells. As malignant cells are thought to be more highly dependant on this protein cycling, interrupting this pathway is therefore

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24

MILLERSHIP, J. J., C. L. CHAPPELL, P. C. OKHUYSEN, and K. F. SNOWDEN. "Characterization of a cytosolic aminopeptidase from Encephalitozoon intestinalis." Parasitology 124, no. 1 (2002): 1–7. http://dx.doi.org/10.1017/s0031182001008940.

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Aminopeptidase activity was detected in Encephalitozoon intestinalis using a fluorometric assay. The aminopeptidase was capable of hydrolysing different amino acids bound to 7-amino-4-trifluoromethyl coumarin, with maximal activity against the amino acid, leucine. Aminopeptidase activity was localized in E. intestinalis spores and in intracellular stages. Enzymatic activity was inhibited by the traditional aminopeptidase inhibitors, bestatin and its analogue, nitrobestatin. Inhibition with the chelating agents, EDTA and 1,10-phenanthroline, suggested that the enzyme activity belongs to the met

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Bergin, Joseph D., and Charles H. Clapp. "Inhibition of Aminopeptidase M by Alkyl D-Cysteinates." Journal of Enzyme Inhibition 3, no. 2 (1989): 127–31. http://dx.doi.org/10.3109/14756368909030371.

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26

Orning, L., G. Krivi, G. Bild, J. Gierse, S. Aykent, and F. A. Fitzpatrick. "Inhibition of leukotriene A4 hydrolase/aminopeptidase by captopril." Journal of Biological Chemistry 266, no. 25 (1991): 16507–11. http://dx.doi.org/10.1016/s0021-9258(18)55329-1.

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27

Bradshaw, Ralph A. "Methionine aminopeptidase 2 inhibition: antiangiogenesis and tumour therapy." Expert Opinion on Therapeutic Patents 14, no. 1 (2004): 1–6. http://dx.doi.org/10.1517/13543776.14.1.1.

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28

ITO, Osamu, Shinichi KAMATA, Norihide KAKIICHI, Hidemichi TAKAHASHI, Masatoshi HAYASHI та Hiroharu OTUKA. "Inhibition of Aminopeptidase by Cow's Milk κ-Casein". Nihon Chikusan Gakkaiho 62, № 9 (1991): 854–60. http://dx.doi.org/10.2508/chikusan.62.854.

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29

Borhade, Sanjay R., Ulrika Rosenström, Jonas Sävmarker, et al. "Inhibition of Insulin-Regulated Aminopeptidase (IRAP) by Arylsulfonamides." ChemistryOpen 3, no. 6 (2014): 256–63. http://dx.doi.org/10.1002/open.201402027.

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30

Chai, Sergio C., and Qi-Zhuang Ye. "Metal-mediated inhibition is a viable approach for inhibiting cellular methionine aminopeptidase." Bioorganic & Medicinal Chemistry Letters 19, no. 24 (2009): 6862–64. http://dx.doi.org/10.1016/j.bmcl.2009.10.082.

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31

Cloos, Jacqueline, Godefridus J. Peters, Marjon Al, et al. "Statins Potentiate Aminopeptidase Inhibitor (pro)Drug Activity in Acute Myeloid Leukemia Cells." Blood 132, Supplement 1 (2018): 3945. http://dx.doi.org/10.1182/blood-2018-99-114447.

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Abstract Tosedostat represents a next generation oral aminopeptidase inhibitor prodrug that has recently demonstrated promising activity in elderly patients with relapsed and refractory acute myeloid leukemia (AML). This prodrug is bio-activated to its hydrophilic active metabolite by intracellular esterases including carboxylesterase 1 (CES1) hence enhancing its cellular retention and promoting targeting of multiple aminopeptidases. Aminopeptidase inhibition provokes an amino acid deprivation response, inhibition of mTOR activity and blockade of protein synthesis. The fact that CES1 also has

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32

Ferreira, Glaucio Monteiro, Thales Kronenberger, Éryka Costa de Almeida, et al. "Inhibition of Porcine Aminopeptidase M (pAMP) by the Pentapeptide Microginins." Molecules 24, no. 23 (2019): 4369. http://dx.doi.org/10.3390/molecules24234369.

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Aminopeptidase M (AMP) inhibition is of interest for several diseases, such as highly vascularized cancer types. AMP can be inhibited by linear pentapeptides isolated from Microcystis aeruginosa LTPNA08 (MG7XX). Porcine AMP inhibition—a model for human AMP—activity was spectrophotometrically measured by the formation of p-nitroanilide from L-leucine-p-nitroanilide substrate by AMP. AMP inhibition by MG770 exhibited comparable inhibition levels to amastatin (IC50 values: 1.20 ± 0.1 μM and 0.98 ± 0.1 μM, respectively), while MG756 was slightly less potent (with IC50 values of 3.26 ± 0.5 μM). Mol

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Hensbergen, Yvette, Erna Peters, Sareena Rana, et al. "Aminopeptidase inhibitor bestatin stimulates microvascular endothelial cell invasion in a fibrin matrix." Thrombosis and Haemostasis 90, no. 11 (2003): 921–29. http://dx.doi.org/10.1160/th03-03-0144.

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SummaryThe aminopeptidase inhibitor bestatin has been shown to have anti-angiogenic effects in a number of model systems. These effects are thought to result from inhibition of CD13 activity. Because tumor angiogenesis can evolve in a fibrin-rich stroma matrix we have studied for the first time the effects of bestatin on microvascular endothelial capillary-like tube formation in a fibrin matrix. Bestatin enhanced the formation of capillary-like tubes dose-dependently. Its effects were apparent at 8 µM; the increase was 3.7-fold at 125 µM; while high concentrations (>250 µM), that were shown

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Amoscato, A. A., J. W. Alexander, and G. F. Babcock. "Surface aminopeptidase activity of human lymphocytes. I. Biochemical and biologic properties of intact cells." Journal of Immunology 142, no. 4 (1989): 1245–52. http://dx.doi.org/10.4049/jimmunol.142.4.1245.

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Abstract Surface aminopeptidase activity in intact lymphocytes was studied and was shown to have the following properties when alanine-p-nitroanilide was used as substrate: 1) The activity was surface associated and not secreted as determined by extracellular location of product and the effect of proteases and diazotized sulfanilic acid on enzyme activity. 2) The enzyme activity was shown to have a pH optimum of 7.4 to 8.0. 3) Enzyme activity was shown to be inhibited by amastatin, bestatin, and 1,10 phenanthroline. Inhibition by amastatin consisted of a high-affinity component (Ki = 3.5 x 10(

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Luan, Yepeng, Chunhua Ma, Zhongguo Sui, et al. "LYP3, a New Bestatin Derivative for Aminopeptidase N Inhibition." Medicinal Chemistry 7, no. 1 (2011): 32–36. http://dx.doi.org/10.2174/157340611794072706.

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36

Osana, Shion, Kazutaka Murayama, Naoki Suzuki, Hiroaki Takada, Takahiro Kubota, and Ryoichi Nagatomi. "Inhibition of leucine aminopeptidase affects myocyte proliferation and differentiation." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.02075.

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Herranz, Rosario, Soledad Vinuesa, Julia Castro-Pichel, Concepción Pérez, and M. Teresa García-López. "Aminodeoxybestatin and epi-aminodeoxybestatin: stereospecific synthesis and aminopeptidase inhibition." J. Chem. Soc., Perkin Trans. 1, no. 14 (1992): 1825–30. http://dx.doi.org/10.1039/p19920001825.

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38

Moore, Hannah E., Emma L. Davenport, Emma M. Smith, et al. "Aminopeptidase inhibition as a targeted treatment strategy in myeloma." Molecular Cancer Therapeutics 8, no. 4 (2009): 762–70. http://dx.doi.org/10.1158/1535-7163.mct-08-0735.

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39

Xie, Sheng-Xue, Wei-Jun Huang, Ze-Qiang Ma, Min Huang, Robert P. Hanzlik, and Qi-Zhuang Ye. "Structural analysis of metalloform-selective inhibition of methionine aminopeptidase." Acta Crystallographica Section D Biological Crystallography 62, no. 4 (2006): 425–32. http://dx.doi.org/10.1107/s0907444906003878.

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40

Huang, Min, Sheng-Xue Xie, Ze-Qiang Ma, Robert P. Hanzlik, and Qi-Zhuang Ye. "Metal mediated inhibition of methionine aminopeptidase by quinolinyl sulfonamides." Biochemical and Biophysical Research Communications 339, no. 2 (2006): 506–13. http://dx.doi.org/10.1016/j.bbrc.2005.11.042.

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Marijanovic, Emilia M., Karolina Weronika Swiderska, James Andersen, et al. "X-ray crystal structure and specificity of the Toxoplasma gondii ME49 TgAPN2." Biochemical Journal 477, no. 19 (2020): 3819–32. http://dx.doi.org/10.1042/bcj20200569.

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Toxoplasmosis is a parasitic disease caused by infection with Toxoplasma gondii that currently has few therapeutic options. The M1 aminopeptidase enzymes have been shown to be attractive targets for anti-parasitic agents and/or vaccine candidates, suggesting potential to re-purpose inhibitors between parasite M1 aminopeptidase targets. The M1 aminopeptidase TgAPN2 has been suggested to be a potential new drug target for toxoplasmosis. Here we investigate the structure and function of TgAPN2, a homologue of the antimalarial drug target PfA-M1, and evaluate the capacity to use inhibitors that ta

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42

Danielsen, E. M. "Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N." Biochemical Journal 254, no. 1 (1988): 219–22. http://dx.doi.org/10.1042/bj2540219.

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The effect of 2,6-dichloro-4-nitrophenol (DCNP), an inhibitor of phenol sulphotransferases (EC 2.8.2.-), on the biosynthesis of aminopeptidase N (EC 3.4.11.2) was studied in organ-cultured pig intestinal mucosal explants. At 50 microM DCNP did not affect protein synthesis but it decreased incorporation of [35S]sulphate into aminopeptidase N and other major microvillar hydrolases by 70-85% compared with controls, indicating an inhibition of their post-translational tyrosine sulphation. In labelling experiments with [35S]methionine from 0.5 to 5 h, DCNP was tested for its possible influence on s

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Ashmun, RA, and AT Look. "Metalloprotease activity of CD13/aminopeptidase N on the surface of human myeloid cells." Blood 75, no. 2 (1990): 462–69. http://dx.doi.org/10.1182/blood.v75.2.462.462.

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Abstract We previously found that the myeloid cell surface glycoprotein CD13 (gp150) is identical to aminopeptidase N (EC 3.4.11.2), a widely distributed membrane-bound, zinc-dependent metalloprotease with an extracellular enzymatic domain that cleaves N-terminal amino acid residues from oligopeptides (J Clin Invest 83:1299, 1989). As a first step toward defining the function of this molecule on myeloid cells, we assessed cell surface-associated N-terminal peptidase activity by sensitive spectrophotometric measurements of the cleavage of p- nitroanilide amino acid derivatives. Aminopeptidase a

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Ashmun, RA, and AT Look. "Metalloprotease activity of CD13/aminopeptidase N on the surface of human myeloid cells." Blood 75, no. 2 (1990): 462–69. http://dx.doi.org/10.1182/blood.v75.2.462.bloodjournal752462.

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Abstract:

We previously found that the myeloid cell surface glycoprotein CD13 (gp150) is identical to aminopeptidase N (EC 3.4.11.2), a widely distributed membrane-bound, zinc-dependent metalloprotease with an extracellular enzymatic domain that cleaves N-terminal amino acid residues from oligopeptides (J Clin Invest 83:1299, 1989). As a first step toward defining the function of this molecule on myeloid cells, we assessed cell surface-associated N-terminal peptidase activity by sensitive spectrophotometric measurements of the cleavage of p- nitroanilide amino acid derivatives. Aminopeptidase activity d

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Barlow, Nicholas, Sudarsana Reddy Vanga, Jonas Sävmarker, et al. "Macrocyclic peptidomimetics as inhibitors of insulin-regulated aminopeptidase (IRAP)." RSC Medicinal Chemistry 11, no. 2 (2020): 234–44. http://dx.doi.org/10.1039/c9md00485h.

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Sri Krishna, G., and A. S. Kanagasabapathy. "A peptidase activity from primate liver that inactivates oxytocin in vitro: purification and partial characterization." Journal of Endocrinology 121, no. 3 (1989): 537–44. http://dx.doi.org/10.1677/joe.0.1210537.

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ABSTRACT An aminopeptidase from monkey (Macaca radiata) liver, inactivating oxytocin in vitro and located predominantly in the lysosomal and microsomal fractions, was purified by chromatography on Bio-Gel HTP, DEAE-Sephacel and nickel ion chelate gel and gel filtration on Sephacryl S300. Absence of binding to nickel ion chelate gel indicated the absence of exposed histidine and thiol residues on the enzyme. The enzyme appeared to be a high molecular weight (Mr 106 000) monomeric protein. It was sensitive to inhibition by metal chelators and was found to be a zinc metalloprotein by atomic absor

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LIJNEN, P., V. PETROV, and R. FAGARD. "Aminopeptidase B-inhibition attenuates collagen production in cardiac fibroblasts through inhibition of lysyl oxidase." American Journal of Hypertension 18, no. 5 (2005): A163. http://dx.doi.org/10.1016/j.amjhyper.2005.03.452.

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Beattie, R. E., D. T. Elmore, C. H. Williams, and D. J. S. Guthrie. "The behaviour of leucine aminopeptidase towards thionopeptides." Biochemical Journal 245, no. 1 (1987): 285–88. http://dx.doi.org/10.1042/bj2450285.

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Thionoleucine S-anilide (Leut-anilide), Leut-Gly-OEt and Leut-Phe-OMe were synthesized and shown to be competitive inhibitors of leucine aminopeptidase from pig kidney. The kinetics of inhibition were determined in the presence of leucine 4-methylcoumarin-7-amide as substrate. Although the compounds showed only moderate inhibitory potency, it was found that all were resistant to hydrolysis by the enzyme, in contrast with the reported behaviour of some thionopeptide analogues of substrates for other Zn2+-peptidases such as carboxypeptidase A and angiotensin-converting enzyme.

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Lijnen, Paul J., Victor V. Petrov, Marisa Turner, and Robert H. Fagard. "Collagen Production in Cardiac Fibroblasts During Inhibition of Aminopeptidase B." Journal of the Renin-Angiotensin-Aldosterone System 6, no. 2 (2005): 69–77. http://dx.doi.org/10.3317/jraas.2005.012.

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Dijkman, Henry B. P. M., Karel J. M. Assmann, Eric J. Steenbergen, and Jack F. M. Wetzels. "Expression and Effect of Inhibition of Aminopeptidase-A during Nephrogenesis." Journal of Histochemistry & Cytochemistry 54, no. 2 (2006): 253–62. http://dx.doi.org/10.1369/jhc.5a6815.2005.

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