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Journal articles on the topic 'Leucina aminopeptidasa'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Tsujimoto, Masafumi, Kazuma Aoki, Yoshikuni Goto, and Atsushi Ohnishi. "Molecular and functional diversity of the oxytocinase subfamily of M1 aminopeptidases." Journal of Biochemistry 169, no. 4 (2021): 409–20. http://dx.doi.org/10.1093/jb/mvab009.

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Abstract The placental leucine aminopeptidase/insulin-regulated aminopeptidase, endoplasmic reticulum aminopeptidase 1 and endoplasmic reticulum aminopeptidase 2 are part of a distinct subfamily of M1 aminopeptidases termed the ‘oxytocinase subfamily’. The subfamily members show molecular diversity due to differential usage of translation initiation sites, alternative splicing and multiple single nucleotide polymorphisms. It is becoming evident that, depending on their intracellular or extracellular location, members of the oxytocinase subfamily play important roles in the maintenance of homeo

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2

Jóźwik, Artur, Ewa Polawska, Nina Strzałkowska, et al. "Effect of linseed, rapeseed, and vitamin E long term supplementation on the activity of the lysosomal enzymes in ostrich liver." Bulletin of the Veterinary Institute in Pulawy 57, no. 4 (2013): 573–78. http://dx.doi.org/10.2478/bvip-2013-0098.

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Abstract The aim of the study was to assess the activity of lysosomal enzymes: aminopeptidases, including alanine aminopeptidase (AlaAP), leucine aminopeptidase (LeuAP), arginine aminopeptidase (ArgAP), and glycosidases, such as β-galactosidase (BGAL), β-glucuronidase (BGRD), β-glucosidase (BGLU), N-acetyl-β-hexosaminidase (HEX), α-glucosidase (AGLU) and α-mannosidase (MAN) in the liver of ostriches (n = 80) fed diet supplemented with linseed (4% and 8%) and rapeseed (5% and 10%), with low and high level of vitamin E. (40 and 100 mg). The results indicate that higher level of vitamin E or 4% l

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3

JIA, H., M. A. TERKAWI, G. O. ABOGE, et al. "Characterization of a leucine aminopeptidase of Babesia gibsoni." Parasitology 136, no. 9 (2009): 945–52. http://dx.doi.org/10.1017/s0031182009006398.

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SUMMARYPeptidases of parasitic protozoa are currently under intense investigation in order to identify novel virulence factors, drug targets, and vaccine candidates, except in Babesia. Leucine aminopeptidases in protozoa, such as Plasmodium and Leishmania, have been identified to be involved in free amino acid regulation. We report here the molecular and enzymatic characterization, as well as the localization of a leucine aminopeptidase, a member of the M17 cytosolic aminopeptidase family, from B. gibsoni (BgLAP). A functional recombinant BgLAP (rBgLAP) expressed in Escherichia coli efficientl

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4

Requena, Teresa, Carmen Peláez, and Michel J. Desmazeaud. "Characterization of lactococci and lactobacilli isolated from semihard goats' cheese." Journal of Dairy Research 58, no. 1 (1991): 137–45. http://dx.doi.org/10.1017/s0022029900033586.

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SummarySeveral strains ofLactococcus lactissubsp.lactis, Lactobacillus caseiandLactobacillus plantarumisolated from traditional goats' cheese have been studied for titratable acidity, proteolysis in milk and enzymic activities. Aminopeptidasc activities were measured with whole cells and cells permeabilized with Triton X-100. Caseinolytic activity was investigated using electrophoresis in polyacrylamide gel with sodium dodecyl sulphate.Lc. lactissubsp.lactishad a level of proteolytic activity in skim milk greater than that ofLb. casei, while this activity inLb. plantarumwas very low. Alanine a

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5

Zhang, Xian, Chiyu Guan, Yi Hang, et al. "An M29 Aminopeptidase from Listeria Monocytogenes Contributes to In Vitro Bacterial Growth but not to Intracellular Infection." Microorganisms 8, no. 1 (2020): 110. http://dx.doi.org/10.3390/microorganisms8010110.

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Aminopeptidases that catalyze the removal of N-terminal residues from polypeptides or proteins are crucial for physiological processes. Here, we explore the biological functions of an M29 family aminopeptidase II from Listeria monocytogenes (LmAmpII). We show that LmAmpII contains a conserved catalytic motif (EEHYHD) that is essential for its enzymatic activity and LmAmpII has a substrate preference for arginine and leucine. Studies on biological roles indicate that LmAmpII is required for in vitro growth in a chemically defined medium for optimal growth of L. monocytogenes but is not required

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6

Wanat, Weronika, Michał Talma, Małgorzata Pawełczak, and Paweł Kafarski. "Phosphonic Acid Analogues of Phenylglycine as Inhibitors of Aminopeptidases: Comparison of Porcine Aminopeptidase N, Bovine Leucine Aminopeptidase, Tomato Acidic Leucine Aminopeptidase and Aminopeptidase from Barley Seeds." Pharmaceuticals 12, no. 3 (2019): 139. http://dx.doi.org/10.3390/ph12030139.

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The inhibitory activity of 14 racemic phosphonic acid analogs of phenylglycine, substituted in aromatic rings, towards porcine aminopeptidase N (pAPN) and barley seed aminopeptidase was determined experimentally. The obtained patterns of the inhibitory activity against the two enzymes were similar. The obtained data served as a basis for studying the binding modes of these inhibitors by pAPN using molecular modeling. It was found that their aminophosphonate fragments were bound in a highly uniform manner and that the difference in their affinities most likely resulted from the mode of substitu

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7

Mizutani, Shigehiko, John W. Wright, and Hiroshi Kobayashi. "Placental Leucine Aminopeptidase- and Aminopeptidase A- Deficient Mice Offer Insight concerning the Mechanisms Underlying Preterm Labor and Preeclampsia." Journal of Biomedicine and Biotechnology 2011 (2011): 1–12. http://dx.doi.org/10.1155/2011/286947.

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Preeclampsia and preterm delivery are important potential complications in pregnancy and represent the leading causes for maternal and perinatal morbidity and mortality. The mechanisms underlying both diseases remain unknown, thus available treatments (beta2-stimulants and magnesium sulfate) are essentially symptomatic. Both molecules have molecular weights less than 5–8 kDa, cross the placental barrier, and thus exert their effects on the fetus. The fetus produces peptides that are highly vasoactive and uterotonic and increase in response to maternal stress and with continued development. Fet

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8

Maruyama, Masato, Akira Hattori, Yoshikuni Goto, et al. "Laeverin/Aminopeptidase Q, a Novel Bestatin-sensitive Leucine Aminopeptidase Belonging to the M1 Family of Aminopeptidases." Journal of Biological Chemistry 282, no. 28 (2007): 20088–96. http://dx.doi.org/10.1074/jbc.m702650200.

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9

Jarocki, Veronica M., Jerran Santos, Jessica L. Tacchi, et al. "MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae." Open Biology 5, no. 1 (2015): 140175. http://dx.doi.org/10.1098/rsob.140175.

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Aminopeptidases are part of the arsenal of virulence factors produced by bacterial pathogens that inactivate host immune peptides. Mycoplasma hyopneumoniae is a genome-reduced pathogen of swine that lacks the genetic repertoire to synthesize amino acids and relies on the host for availability of amino acids for growth. M. hyopneumoniae recruits plasmin(ogen) onto its cell surface via the P97 and P102 adhesins and the glutamyl aminopeptidase MHJ_0125. Plasmin plays an important role in regulating the inflammatory response in the lungs of pigs infected with M. hyopneumoniae . We show that recomb

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10

Monod, Michel, Barbara Léchenne, Olivier Jousson, et al. "Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum." Microbiology 151, no. 1 (2005): 145–55. http://dx.doi.org/10.1099/mic.0.27484-0.

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The nature of secreted aminopeptidases in Trichophyton rubrum was investigated by using a reverse genetic approach. T. rubrum genomic and cDNA libraries were screened with Aspergillus spp. and Saccharomyces cerevisiae aminopeptidase genes as the probes. Two leucine aminopeptidases, ruLap1 and ruLap2, and two dipeptidyl-peptidases, ruDppIV and ruDppV, were characterized and compared to orthologues secreted by Aspergillus fumigatus using a recombinant protein from Pichia pastoris. RuLap1 is a 33 kDa nonglycosylated protein, while ruLap2 is a 58–65 kDa glycoprotein. The hydrolytic activity of ruL

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11

Chung, Dong-Min, Gang-Deog Lee, Sung-Sick Chun, Young-Chul Chung, and Hyo-Kon Chun. "Effect of NaCl on Hydrolytic Activity of Leucine Aminopeptidase from Bacillus sp. N2." Journal of Life Science 21, no. 5 (2011): 761–65. http://dx.doi.org/10.5352/jls.2011.21.5.761.

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12

Rossier, Ombeline, Jenny Dao, and Nicholas P. Cianciotto. "The Type II Secretion System of Legionella pneumophila Elaborates Two Aminopeptidases, as Well as a Metalloprotease That Contributes to Differential Infection among Protozoan Hosts." Applied and Environmental Microbiology 74, no. 3 (2007): 753–61. http://dx.doi.org/10.1128/aem.01944-07.

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ABSTRACT Legionella pneumophila, the agent of Legionnaires' disease, is an intracellular parasite of aquatic amoebae and human macrophages. A key factor for L. pneumophila in intracellular infection is its type II protein secretion system (Lsp). In order to more completely define Lsp output, we recently performed a proteomic analysis of culture supernatants. Based upon the predictions of that analysis, we found that L. pneumophila secretes two distinct aminopeptidase activities encoded by the genes lapA and lapB. Whereas lapA conferred activity against leucine, phenylalanine, and tyrosine amin

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13

Premarathne, A. A. A., and David W. M. Leung. "Characterization of Activity of a Potential Food-Grade Leucine Aminopeptidase from Kiwifruit." Enzyme Research 2010 (November 4, 2010): 1–5. http://dx.doi.org/10.4061/2010/517283.

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Aminopeptidase (AP) activity in ripe but firm fruit of Actinidia deliciosa was characterized using L-leucine-p-nitroanilide as a substrate. The enzyme activity was the highest under alkaline conditions and was thermolabile. EDTA, 1,10-phenanthroline, iodoacetamide, and had inhibitory effect while a low concentration of dithiothreitol (DTT) had stimulatory effect on kiwifruit AP activity. However, DTT was not essential for the enzyme activity. The results obtained indicated that the kiwifruit AP was a thiol-dependent metalloprotease. Its activity was the highest in the seeds, followed by the co

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14

Shevchenko, K. V., L. A. Andreeva, I. Yu Nagaev, V. P. Shevchenko, and N. F. Myasoedov. "Study of stability of proline-containing derivatives of dopamine and serotonin in the biological media in vitro experiments." Biomeditsinskaya Khimiya 65, no. 6 (2019): 498–506. http://dx.doi.org/10.18097/pbmc20196506498.

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Boc-Gly-Pro-DP, Z-Gly-Pro-DP, LA-Gly-Pro-DP, Boc-Gly-Pro-Srt, Z-Gly-Pro-Srt were synthesized for the first time. The stability of these compounds in the presence of leucine aminopeptidase, carboxypeptidase Y, carboxypeptidase B and proline endopeptidase (PEP) was determined. It turned out that the compounds are stable in the presence of aminopeptidases and carboxypeptidases. In the presence of PEP, dopamine (DP) and serotonin (Srt) are cleaved from the synthesized preparations. Thus, new proline-containing Srt and DP derivatives were obtained, Srt and DP could be gradually released from them.

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15

Beattie, R. E., D. J. S. Guthrie, D. T. Elmore, C. H. Williams, and B. Walker. "An improved spectrophotometric assay for leucine aminopeptidase." Biochemical Journal 242, no. 1 (1987): 281–83. http://dx.doi.org/10.1042/bj2420281.

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A sensitive assay to determine the activity of leucine aminopeptidase (EC 3.4.11.1), using L-leucine thiobenzyl ester as substrate, was developed. Hydrolysis of the ester by leucine aminopeptidase can be monitored in the presence of 5,5-dithiobis-(2-nitrobenzoic acid) by continuous spectrophotometric measurement at 412 nm. Comparison with some amide substrates showed that the thiol ester provides a much more sensitive assay, its specificity constant (Vmax./Km) being some 3000-fold higher than that of leucine p-nitroanilide.

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16

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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17

Ishizaki, Takashi, Aki Tosaka, Takayuki Nara, et al. "Leucine aminopeptidase during meiotic development." European Journal of Biochemistry 269, no. 3 (2002): 826–32. http://dx.doi.org/10.1046/j.0014-2956.2001.02713.x.

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18

Rogi, Tomohiro, Masafumi Tsujimoto, Hiroshi Nakazato, Shigehiko Mizutani, and Yutaka Tomoda. "Human Placental Leucine Aminopeptidase/Oxytocinase." Journal of Biological Chemistry 271, no. 1 (1996): 56–61. http://dx.doi.org/10.1074/jbc.271.1.56.

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19

Hattori, A., H. Matsumoto, S. Mizutani, and M. Tsujimoto. "Molecular Cloning of Adipocyte-Derived Leucine Aminopeptidase Highly Related to Placental Leucine Aminopeptidase/Oxytocinase." Journal of Biochemistry 125, no. 5 (1999): 931–38. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a022371.

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20

KANG, J. M., H. L. JU, W. M. SOHN, and B. K. NA. "Molecular cloning and characterization of a M17 leucine aminopeptidase of Cryptosporidium parvum." Parasitology 138, no. 6 (2011): 682–90. http://dx.doi.org/10.1017/s0031182011000199.

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SUMMARYLeucine aminopeptidases (LAPs) are a group of metalloexopeptidases that catalyse the sequential removal of amino acids from the N-termini of polypeptides or proteins. They play an important role in regulating the balance between catabolism and anabolism in living cells. LAPs of apicomplexa parasitic protozoa have been intensively investigated due to their crucial roles in parasite biology as well as their potentials as drug targets. In this study, we identified an M17 leucine aminopeptidase of Cryptosporidium parvum (CpLAP) and characterized the biochemical properties of the recombinant

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21

Dong, Lei, Ni Cheng, Ming-Wei Wang, Junfeng Zhang, Chang Shu, and De-Xu Zhu. "The leucyl aminopeptidase from Helicobacter pylori is an allosteric enzyme." Microbiology 151, no. 6 (2005): 2017–23. http://dx.doi.org/10.1099/mic.0.27767-0.

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This study describes the cloning, genetic analysis and biochemical characterization of a leucyl aminopeptidase (LAP) from Helicobacter pylori. A gene encoding LAP was cloned from H. pylori and the expressed 55 kDa protein displayed homology to aminopeptidases from Gram-negative bacteria, plants and mammals. This LAP demonstrated amidolytic activity against l-leucine-p-nitroanilide. Optimal activity was observed at pH 8·0 and 45 °C, with V max of 232 μmol min−1 (mg protein)−1 and S 0·5 of 0·65 mM. The data suggest that LAP could be allosteric (n H=2·27), with regulatory homohexamers, and its ac

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22

Bertin, Patrícia B., Silene P. Lozzi, Jerrilyn K. Howell, et al. "The Thermophilic, Homohexameric Aminopeptidase of Borrelia burgdorferi Is a Member of the M29 Family of Metallopeptidases." Infection and Immunity 73, no. 4 (2005): 2253–61. http://dx.doi.org/10.1128/iai.73.4.2253-2261.2005.

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ABSTRACT Proteases are implicated in several aspects of the physiology of microorganisms, as well as in host-pathogen interactions. Aminopeptidases are also emerging as novel drug targets in infectious agents. In this study, we have characterized an aminopeptidase from the spirochete Borrelia burgdorferi, the causative agent of Lyme disease. The aminopeptidolytic activity was identified in cell extracts from B. burgdorferi by using the substrate leucine-7-amido-4-methylcoumarin. A protein displaying this activity was purified from B. burgdorferi by a two-step chromatographic procedure, yieldin

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23

Hall, N. A. "Peptidases in Drosophila melanogaster—III. The regulation of leucine aminopeptidase P and leucine aminopeptidase G." Insect Biochemistry 18, no. 2 (1988): 157–61. http://dx.doi.org/10.1016/0020-1790(88)90019-4.

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24

Journal, Baghdad Science. "Estimation Activity And Partial Purification Of Leucine Amino Peptidase (Lap) In Patients Wiith Diabetic Nephropathy." Baghdad Science Journal 9, no. 4 (2012): 689–94. http://dx.doi.org/10.21123/bsj.9.4.689-694.

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Leucine aminopepotidase (LAP)[EC:3.4.11.1] activity has been assayed in (50) serum samples of patients with diabeties naphrophathy D.N (non-insulin dependent diabetic (NIDD) , and (50)serum sample of healthy individuals without any clinically detectable diseases have been as control group. The aim of this study is to measure leucine aminopeptidase activity and partially purifying the enzyme from sera of patients with diabetes nephropathy The results of this study revealed that Leucine aminopeptidase (LAP) activity of nephropathy patient’s serum shows a high signifiacant increase (p < 0.001)

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25

BEATTIE, RUTH E., CARVELL H. WILLIAMS, and DONALD T. ELMORE. "l-Leucine thioamide as an inhibitor of leucine aminopeptidase." Biochemical Society Transactions 16, no. 2 (1988): 185–86. http://dx.doi.org/10.1042/bst0160185.

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26

Sharma, K. Krishna, Nancy J. Elser, and Kathryn Kester. "Comparison of leucine aminopeptidase and aminopeptidase III activities in lens." Current Eye Research 15, no. 7 (1996): 774–81. http://dx.doi.org/10.3109/02713689609003462.

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27

Mizutani, Shigehiko, and Yutaka Tomoda. "Oxytocinase: Placental Cystine Aminopeptidase or Placental Leucine Aminopeptidase (P-LAP)." Seminars in Reproductive Medicine 10, no. 02 (1992): 146–53. http://dx.doi.org/10.1055/s-2007-1018870.

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28

Katoh, Masaya, and David W. Foltz. "Biochemical evidence for the existence of a null allele at the leucine aminopeptidase-2 (Lap-2) locus in the oyster Crassostrea virginica (Gmelin)." Genome 32, no. 4 (1989): 687–90. http://dx.doi.org/10.1139/g89-499.

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The existence of a null activity allele at the leucine aminopeptidase-2 (Lap-2) locus in the oyster Crassostrea virginica (Gmelin) was previously inferred from anomalous segregation patterns observed in offspring from pair crosses, and from the occurrence of individuals lacking Lap-2 bands on gels (presumed null homozygotes). The present research was done to determine whether leucine aminopeptidase specific activity was significantly reduced in oysters presumed from breeding experiments to be heterozygous for a Lap-2 null allele. Approximately thirty 4-month-old oysters from each of two crosse

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29

Candiotto, F. B., A. C. V. Freitas-Júnior, R. C. A. Neri, et al. "Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus." Brazilian Journal of Biology 78, no. 2 (2017): 281–88. http://dx.doi.org/10.1590/1519-6984.06616.

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Abstract Knowledge of specific enzyme activity, along with animal habits and digestive capacity is essential in formulating an appropriate diet for any species. In this study, we evaluated and characterized the activity of digestive enzymes present in the liver, intestine, and stomach of Paralichthys orbignyanus. The effects of pH and temperature on enzyme activity were also evaluated via the use of specific substrates. The use of specific substrates and inhibitors showed strong evidence of the presence of trypsin (BApNA= 0.51 ± 0.2 mU mg-1), chimotrypsin (SApNA= 2.62 ± 1.8 mU mg-1), and amino

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30

Francoeur, SN, and RG Wetzel. "Regulation of periphytic leucine-aminopeptidase activity." Aquatic Microbial Ecology 31 (2003): 249–58. http://dx.doi.org/10.3354/ame031249.

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31

Nakonieczna, Łucja, Juliusz J. Pastuszak, and Andrzej Chimiak. "Catechoyl-Dipeptides as Leucine Aminopeptidase Inhibitors." Zeitschrift für Naturforschung B 44, no. 7 (1989): 811–16. http://dx.doi.org/10.1515/znb-1989-0715.

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Several 2,3- (and 3,4)-dihydroxybenzoyl-dipeptides (5) have been obtained as new ligands able to interact with therapeutically important metalloproteases. Some of them appeared to be strong inhibitors of leucine aminopeptidase [EC 3.4.11.1].

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32

Manganaris, A. G., and F. H. Alston. "Genetics of leucine aminopeptidase in apple." Theoretical and Applied Genetics 83, no. 3 (1992): 345–52. http://dx.doi.org/10.1007/bf00224281.

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33

Ziemska, Joanna, Jolanta Solecka, and Małgorzata Jarończyk. "In Silico Screening for Novel Leucine Aminopeptidase Inhibitors with 3,4-Dihydroisoquinoline Scaffold." Molecules 25, no. 7 (2020): 1753. http://dx.doi.org/10.3390/molecules25071753.

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Cancers are the leading cause of deaths worldwide. In 2018, an estimated 18.1 million new cancer cases and 9.6 million cancer-related deaths occurred globally. Several previous studies have shown that the enzyme, leucine aminopeptidase is involved in pathological conditions such as cancer. On the basis of the knowledge that isoquinoline alkaloids have antiproliferative activity and inhibitory activity towards leucine aminopeptidase, the present study was conducted a study which involved database search, virtual screening, and design of new potential leucine aminopeptidase inhibitors with a sca

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34

Blattler, R., and U. Feller. "Identification and Stability of Aminopeptidases in Extracts From Bean Seeds." Functional Plant Biology 15, no. 5 (1988): 613. http://dx.doi.org/10.1071/pp9880613.

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Extract from ungerminated bean seeds (Phaseolus vulgaris L. cv. Saxa) was fractionated by gel chromatography on Sephacryl S-200 and by anion exchange chromatography on diethylaminoethyl- Sephacel. Aminopeptidase activities were measured with the following amino acid-p-nitroanilides: phenylalanine, leucine, methionine, proline, alanine, lysine, arginine and glycine. Four forms differing in their substrate specificities were identified: form 1 (liberating alanine, lysine and arginine), form 2 (liberating leucine, methionine, phenylalanine and perhaps also proline), form 3 (liberating glycine) an

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35

Janiszewska, Kamila, Michał Talma, Bartosz Oszywa, Małgorzata Pawełczak, Paweł Kafarski, and Artur Mucha. "N-Benzyl Residues as the P1′ Substituents in Phosphorus-Containing Extended Transition State Analog Inhibitors of Metalloaminopeptidases." Molecules 25, no. 18 (2020): 4334. http://dx.doi.org/10.3390/molecules25184334.

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Peptidyl enzyme inhibitors containing an internal aminomethylphosphinic bond system (P(O)(OH)-CH2-NH) can be termed extended transition state analogs by similarity to the corresponding phosphonamidates (P(O)(OH)-NH). Phosphonamidate pseudopeptides are broadly recognized as competitive mechanism-based inhibitors of metalloenzymes, mainly hydrolases. Their practical use is, however, limited by hydrolytic instability, which is particularly restricting for dipeptide analogs. Extension of phosphonamidates by addition of the methylene group produces a P-C-N system fully resistant in water conditions

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36

BEATTIE, R. E., B. WALKER, D. T. ELMORE, and C. H. WILLIAMS. "Thiol ester derivatives of leucine as substrates for leucine aminopeptidase." Biochemical Society Transactions 15, no. 2 (1987): 232–33. http://dx.doi.org/10.1042/bst0150232.

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37

MAIA, Juracy de Freitas, and Joselita Maria Mendes dos SANTOS. "Padrões ontogenéticos das Esterases, Leucina Aminopeptidase e X-Glicerofosfato Desidrogenase em Anopheles (Nyssorhynchus) Albitarsis lynch-arribálzaga, 1878 (Diptera: Culicidae)." Acta Amazonica 29, no. 1 (1999): 135. http://dx.doi.org/10.1590/1809-43921999291144.

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Modificações na expressão gênica foram observadas nos sistemas esterase, leucina aminopeptidase e x-glicerofosfato desidrogenase, durante o desenvolvimento ontogenético de Anopheles albitarsis. A esterase revelou quatro regiões de atividade, sendo a esterase 1 detectada apenas em larvas de 4º estádio velhas e em pupas, as esterases 2 e 4 foram presentes durante todo o desenvolvimento, e a esterase 3 revelou-se praticamente apenas em larvas e raríssimas vezes em pupas. Também foram observadas quatro regiões de atividade na leucina aminopeptidase, durante a ontogenia. As LAP1 c LAP2 foram caract

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38

Woolwine, Samuel C., April B. Sprinkle, and Daniel J. Wozniak. "Loss of Pseudomonas aeruginosa PhpA Aminopeptidase Activity Results in Increased algDTranscription." Journal of Bacteriology 183, no. 15 (2001): 4674–79. http://dx.doi.org/10.1128/jb.183.15.4674-4679.2001.

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ABSTRACT Inactivation of Pseudomonas aeruginosa phpA, encoding a putative leucine aminopeptidase, results in increased transcription ofalgD. The homologous protein in Escherichia coli, PepA, is multifunctional, possessing independent aminopeptidase and DNA-binding activities. Here we provide in vitro evidence that PhpA is an aminopeptidase and show that this activity is the relevant property with regard to algD expression. This regulation occurred at the previously mapped algDtranscription initiation site and was not due to activation of an alternative promoter.

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Bataglia, Luana, Isabel Cristina Godoy, Marco Antonio Del Lama, and Francis Morais Franco Nunes. "Leucine-aminopeptidase A (LAP-A) Encoding Gene in Apoidea: from Genomic Identification to Functional Insights Based on Gene Expression." Sociobiology 65, no. 4 (2018): 654. http://dx.doi.org/10.13102/sociobiology.v65i4.3475.

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Aminopeptidases are enzymes that cleave the N-terminal region of proteins and show structural conservation in prokaryotes and eukaryotes. We aimed to identify leucine-aminopeptidase A (LAP-A) orthologs in the genome of bee species with diff erent levels of social organization, and to explore the putative roles of this enzyme based on gene expression data. We identified a single gene for LAP-A on chromosome 15 of Apis mellifera L. and predicted orthologs in genomes of 11 bee species. We found evidence of LAP-A expression in more than 50 bee species. In honeybee and other bees, LAP-A transcripts

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Zhao, Guozhong, Yunping Yao, Chunling Wang, et al. "Transcriptome and Proteome Expression Analysis of the Metabolism of Amino Acids by the FungusAspergillus oryzaein Fermented Soy Sauce." BioMed Research International 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/456802.

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Amino acids comprise the majority of the flavor compounds in soy sauce. A portion of these amino acids are formed from the biosynthesis and metabolism of the fungusAspergillus oryzae; however, the metabolic pathways leading to the formation of these amino acids inA. oryzaeremain largely unknown. We sequenced the transcriptomes ofA. oryzae100-8 andA. oryzae3.042 under similar soy sauce fermentation conditions. 2D gel electrophoresis was also used to find some differences in protein expression. We found that many amino acid hydrolases (endopeptidases, aminopeptidases, and X-pro-dipeptidyl aminop

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Skinner-Adams, Tina S., Christopher L. Peatey, Karen Anderson, et al. "The Aminopeptidase Inhibitor CHR-2863 Is an Orally Bioavailable Inhibitor of Murine Malaria." Antimicrobial Agents and Chemotherapy 56, no. 6 (2012): 3244–49. http://dx.doi.org/10.1128/aac.06245-11.

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ABSTRACTMalaria remains a significant risk in many areas of the world, with resistance to the current antimalarial pharmacopeia an ever-increasing problem. The M1 alanine aminopeptidase (PfM1AAP) and M17 leucine aminopeptidase (PfM17LAP) are believed to play a role in the terminal stages of digestion of host hemoglobin and thereby generate a pool of free amino acids that are essential for parasite growth and development. Here, we show that an orally bioavailable aminopeptidase inhibitor, CHR-2863, is efficacious against murine malaria.

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Tlak Gajger, I., S. Nejedli, and Z. Kozaric. "The effect of Nozevit on leucine aminopeptidase and esterase activity in the midgut of honey bees (Apis mellifera)." Veterinární Medicína 58, No. 8 (2013): 422–29. http://dx.doi.org/10.17221/6982-vetmed.

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The histochemical activity of aminopeptidase and non-specific esterase, both important enzymes of intermediate metabolism in the mid gut of honeybees (Apis mellifera), was investigated. Nosema disease control poses a major challenge, and thus, the treatment of this serious parasitic disease using natural phyto-pharmacological preparations could be of great besnefit. Additionally, the effects of residues and their by-products in honey and wax represent an environmental concern and are another reason for reducing the use of conventional chemical control methods in beekeeping. Nozevit is a natura

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Waditee-Sirisattha, Rungaroon, Akira Hattori, Junko Shibato, et al. "Role of the Arabidopsis leucine aminopeptidase 2." Plant Signaling & Behavior 6, no. 10 (2011): 1581–83. http://dx.doi.org/10.4161/psb.6.10.17105.

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Sadoon, Taghreed. "Placental Leucine Aminopeptidase/Oxytocinase Expression in Miscarriage." British Journal of Medicine and Medical Research 4, no. 17 (2014): 3283–92. http://dx.doi.org/10.9734/bjmmr/2014/6185.

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Ludewig, M., B. Fricke, and H. Aurich. "Leucine aminopeptidase in intracytoplasmic membranes ofAcinetobacter calcoaceticus." Journal of Basic Microbiology 27, no. 10 (1987): 557–63. http://dx.doi.org/10.1002/jobm.3620271004.

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BUITRAGO, J. M. GONZALEZ, J. A. NAVAJO, L. C. GARCIA DIEZ, and A. HERRUZO. "Seminal Plasma Leucine Aminopeptidase in Male Fertility." Andrologia 17, no. 2 (2009): 139–42. http://dx.doi.org/10.1111/j.1439-0272.1985.tb00973.x.

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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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Fukuda, Mitsuhiro, Hiroshi Shima, and Shigeru Kunugi. "Pressure Dependence of L-Leucine-p-nitroanilide Hydrolysis by Leucine Aminopeptidase." Bulletin of the Chemical Society of Japan 58, no. 4 (1985): 1349–50. http://dx.doi.org/10.1246/bcsj.58.1349.

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Gong, Qiuyu, Wen Shi, Lihong Li, and Huimin Ma. "Leucine aminopeptidase may contribute to the intrinsic resistance of cancer cells toward cisplatin as revealed by an ultrasensitive fluorescent probe." Chemical Science 7, no. 1 (2016): 788–92. http://dx.doi.org/10.1039/c5sc03600c.

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Guo, Dan, Zhen-Fei Gan, Lei Jiang, et al. "Detection of leucine aminopeptidase activity in serum using surface-enhanced Raman spectroscopy." Analyst 144, no. 4 (2019): 1394–400. http://dx.doi.org/10.1039/c8an02182a.

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