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Journal articles on the topic 'Exopeptidasas'

Author: Grafiati

Published: 5 June 2025

Last updated: 24 June 2025

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1

Efraín, A. García, Tovar Belkis, Peralta Darlene, and Hernández Dioselauren. "Proteasas sintetizadas por microorganismos utilizadas en la producción de quesos." Observador del Conocimiento Edición Especial 2021, no. 2343-6212 (2022): 96–113. https://doi.org/10.5281/zenodo.6916218.

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Las proteasas son elementos fundamentales en las actividades fisiológicas de los seres vivos, vegetales, animales, bacterias, hongos y virus, es allí donde su presencia es significativa, tanto en la vida como en la muerte, tanto en la reproducción como en la descomposición. Las proteasa actúan de manera específica sobre enlaces peptídicos que conforman a las proteínas y polipéptidos, están clasificadas dentro del grupo de las hidrolasas, por su forma de acción pueden ser exopeptidasas o endopeptidasas, por su pH pueden ser acida, neutra o alcalinas, depende del aminoácido o elemento presente en su sitio activo. Son muy versátiles en su aplicación, el farmacéutico, alimentario, el químico, siendo el primero de ellos el de mayor importancia a nivel de investigación, por lo que implica para la salud del ser humano. Las proteasas de interés en el mundo actual está siendo investigada y producidas bajo condiciones controladas a partir de microorganismos, siendo las bacterias las mayor aprovechamiento por su forma de cultivo en fermentación sumergida, es más fácil de controlar, escalar y recuperar. El interés de la investigación está enfocada en la disminución de los costos utilizando sustratos económicos, mejorar los rendimientos de producción y en el uso de la bioinformática a través de las herramientas omica, proteómica y ADN recombinante para encontrar la especie más productiva, más específica, más resistente. En esta revisión se evidencian trabajos desarrollados en la producción de proteasas y la aplicación de las mismas especialmente en el campo de la producción de quesos.

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2

Hara, Kenji, and Tadashi Ishihara. "Exopeptidase." NIPPON SUISAN GAKKAISHI 62, no. 1 (1996): 147–48. http://dx.doi.org/10.2331/suisan.62.147.

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3

Porodko, Andreas, Ana Cirnski, Drazen Petrov, et al. "The two cathepsin B-like proteases of Arabidopsis thaliana are closely related enzymes with discrete endopeptidase and carboxydipeptidase activities." Biological Chemistry 399, no. 10 (2018): 1223–35. http://dx.doi.org/10.1515/hsz-2018-0186.

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Abstract The genome of the model plant Arabidopsis thaliana encodes three paralogues of the papain-like cysteine proteinase cathepsin B (AtCathB1, AtCathB2 and AtCathB3), whose individual functions are still largely unknown. Here we show that a mutated splice site causes severe truncations of the AtCathB1 polypeptide, rendering it catalytically incompetent. By contrast, AtCathB2 and AtCathB3 are effective proteases which display comparable hydrolytic properties and share most of their substrate specificities. Site-directed mutagenesis experiments demonstrated that a single amino acid substitution (Gly336→Glu) is sufficient to confer AtCathB2 with the capacity to tolerate arginine in its specificity-determining S2 subsite, which is otherwise a hallmark of AtCathB3-mediated cleavages. A degradomics approach utilizing proteome-derived peptide libraries revealed that both enzymes are capable of acting as endopeptidases and exopeptidases, releasing dipeptides from the C-termini of substrates. Mutation of the carboxydipeptidase determinant His207 also affected the activity of AtCathB2 towards non-exopeptidase substrates, highlighting mechanistic differences between plant and human cathepsin B. This was also noted in molecular modeling studies which indicate that the occluding loop defining the dual enzymatic character of cathepsin B does not obstruct the active-site cleft of AtCathB2 to the same extent as in its mammalian orthologues.

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4

Stoka, Veronika, Olga Vasiljeva, Hiroshi Nakanishi, and Vito Turk. "The Role of Cysteine Protease Cathepsins B, H, C, and X/Z in Neurodegenerative Diseases and Cancer." International Journal of Molecular Sciences 24, no. 21 (2023): 15613. http://dx.doi.org/10.3390/ijms242115613.

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Papain-like cysteine proteases are composed of 11 human cysteine cathepsins, originally located in the lysosomes. They exhibit broad specificity and act as endopeptidases and/or exopeptidases. Among them, only cathepsins B, H, C, and X/Z exhibit exopeptidase activity. Recently, cysteine cathepsins have been found to be present outside the lysosomes and often participate in various pathological processes. Hence, they have been considered key signalling molecules. Their potentially hazardous proteolytic activities are tightly regulated. This review aims to discuss recent advances in understanding the structural aspects of these four cathepsins, mechanisms of their zymogen activation, regulation of their activities, and functional aspects of these enzymes in neurodegeneration and cancer. Neurodegenerative effects have been evaluated, particularly in Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, amyotrophic lateral sclerosis, multiple sclerosis, and neuropsychiatric disorders. Cysteine cathepsins also participate in tumour progression and metastasis through the overexpression and secretion of proteases, which trigger extracellular matrix degradation. To our knowledge, this is the first review to provide an in-depth analysis regarding the roles of cysteine cathepsins B, H, C, and X in neurodegenerative diseases and cancer. Further advances in understanding the functions of cysteine cathepsins in these conditions will result in the development of novel, targeted therapeutic strategies.

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5

YOSHIMOTO, Tadashi. "Exopeptidases produced by genus Bacillus." Journal of the agricultural chemical society of Japan 65, no. 1 (1991): 60–62. http://dx.doi.org/10.1271/nogeikagaku1924.65.60.

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6

Caira, Simonetta, Pasquale Ferranti, Monica Gatti, et al. "Synthetic peptides as substrate for assaying the proteolytic activity of Lactobacillus helveticus." Journal of Dairy Research 70, no. 3 (2003): 315–25. http://dx.doi.org/10.1017/s0022029903006368.

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Four Lactobacillus helveticus strains were studied for proteolytic capacity and general aminopeptidase (AP) and X-Pro dipeptidyl aminopeptidase (DAP) activity. The rate of hydrolysis and the activity against synthetic substrates with N-terminal residues of Arg, Lys, Leu, Glu or Pro, varied markedly among the strains. The X-Pro DAP activity was consistently high. The crude cell-wall and cytoplasm extracts from strain Lb. helveticus ISLC59 were analysed thoroughly for their proteolysis ability by using four synthetic peptide substrates, including αs1-CN(f1-23). Peptides formed during in vitro hydrolysis of the synthetic substrates by cell wall and cytoplasm preparations were identified by LC-ESI/MS. In doing so, it was possible to infer a prevalent endopeptidase activity splitting Lys7-His8 and Gln13-Glu14 bonds in the cytoplasm, and to deduce a secondary activity, which hydrolysed Glu14-Val15, Leu16-Asn17, Glu18-Asn19 and Lys3-His4 bonds lacking in the cell-wall. The presence of exopeptidases, as mainly AP, DAP, and carboxypeptidase (CPase) was deduced from the formation of several N- and C-terminally truncated peptides sets. The AP activity was higher in the cell-wall layer, where CPase activity was absent. The in vitro assays with cell extracts of the Lb. helveticus ISLC59 strain revealed extensive exopeptidase and endopeptidase activities. In several cases, the hydrolytic system of Lb. helveticus that splits in vitro αs1-CN(f1-23) peptide bonds was similar to that of Lactococcus lactis. The effects were also compared with those occurring in vivo in hard cheese such as Grana Padano.

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7

MINAGAWA, Etsuo, Shuichi KAMINOGAWA, Fuji TSUKASAKI, Hidemasa MOTOSHIMA, and Kunio YAMAUCHI. "Exopeptidase profiles of bifidobacteria." Journal of Nutritional Science and Vitaminology 31, no. 6 (1985): 599–606. http://dx.doi.org/10.3177/jnsv.31.599.

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8

Kim, Hye-Suk, Jin-Soo Kim, and Min-Soo Heu. "Fractionation of Exopeptidase from Viscera of Argentina Shortfin Squid, Illex argentinus." Journal of the Korean Society of Food Science and Nutrition 37, no. 8 (2008): 1009–17. http://dx.doi.org/10.3746/jkfn.2008.37.8.1009.

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9

Hooper, Nigel M. "Proteases: a primer." Essays in Biochemistry 38 (October 1, 2002): 1–8. http://dx.doi.org/10.1042/bse0380001.

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A protease can be defined as an enzyme that hydrolyses peptide bonds. Proteases can be divided into endopeptidases, which cleave internal peptide bonds in substrates, and exopeptidases, which cleave the terminal peptide bonds. Exopeptidases can be further subdivided into aminopeptidases and carboxypeptidases. The Schechter and Berger nomenclature provides a model for describing the interactions between the peptide substrate and the active site of a protease. Proteases can also be classified as aspartic proteases, cysteine proteases, metalloproteases, serine proteases and threonine proteases, depending on the nature of the active site. Different inhibitors can be used experimentally to distinguish between these classes of protease. The MEROPs database groups proteases into families on the basis of similarities in sequence and structure. Protease activity can be regulated in vivo by endogenous inhibitors, by the activation of zymogens and by altering the rate of their synthesis and degradation.

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10

Chandu, Dilip, and Dipankar Nandi. "PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress." Microbiology 149, no. 12 (2003): 3437–47. http://dx.doi.org/10.1099/mic.0.26518-0.

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PepN and its homologues are involved in the ATP-independent steps (downstream processing) during cytosolic protein degradation. To obtain insights into the contribution of PepN to the peptidase activity in Escherichia coli, the hydrolysis of a selection of endopeptidase and exopeptidase substrates was studied in extracts of wild-type strains and two pepN mutants, 9218 and DH5αΔpepN. Hydrolysis of three of the seven endopeptidase substrates tested was reduced in both pepN mutants. Similar studies revealed that hydrolysis of 10 of 14 exopeptidase substrates studied was greatly reduced in both pepN mutants. This decreased ability to cleave these substrates is pepN-specific as there is no reduction in the ability to hydrolyse exopeptidase substrates in E. coli mutants lacking other peptidases, pepA, pepB or pepE. PepN overexpression complemented the hydrolysis of the affected exopeptidase substrates. These results suggest that PepN is responsible for the majority of aminopeptidase activity in E. coli. Further in vitro studies with purified PepN revealed a preference to cleave basic and small amino acids as aminopeptidase substrates. Kinetic characterization revealed the aminopeptidase cleavage preference of E. coli PepN to be Arg>Ala>Lys>Gly. Finally, it was shown that PepN is a negative regulator of the sodium-salicylate-induced stress in E. coli, demonstrating a physiological role for this aminoendopeptidase under some stress conditions.

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11

Mercado-Flores, Yuridia, César Hernández-Rodríguez, José Ruiz-Herrera, and Lourdes Villa-Tanaca. "Proteinases and exopeptidases from the phytopathogenic fungusUstilago maydis." Mycologia 95, no. 2 (2003): 327–39. http://dx.doi.org/10.1080/15572536.2004.11833118.

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12

Sampath, G. "Amino acid discrimination in a nanopore and the feasibility of sequencing peptides with a tandem cell and exopeptidase." RSC Advances 5, no. 39 (2015): 30694–700. http://dx.doi.org/10.1039/c5ra02118a.

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13

Aoyagi, T., T. Wada, F. Kojima, M. Nagai, S. Harada, and H. Umezawa. "A Multivariate Study on Enzymatic Changes in Limb Muscles and Heart Muscle of Dystrophic Mice." Biotechnology and Applied Biochemistry 9, no. 5 (1987): 355–61. http://dx.doi.org/10.1111/j.1470-8744.1987.tb00483.x.

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The present study was undertaken to elucidate further the enzymatic changes in dystrophic muscle using multivariate analysis. The activities of 14 kinds of enzymes, including 6 exopeptidases, 4 endopeptidases, beta‐N‐acetyl‐D‐glucosaminidase, phosphatase, esterase, and ribonuclease, were examined in forelimb and hindlimb muscles as well as in cardiac muscle of dystrophic mice and their controls. Two principal components identified from the enzymatic spectrum proved to be related especially to aminopeptidases and to serine proteinases, respectively. The enzymatic changes in forelimb muscle were very similar to those in hindlimb muscle when both were compared to those in cardiac muscle. The changes in aminopeptidases were unique to the limb muscles, whereas those of serine proteinases were unique to cardiac muscle of dystrophic mice. In the future, more attention should be focused on the role of exopeptidases in pathogenetic mechanisms of muscular dystrophy, because of the possibility that they play a major role in the initial stage of muscular dystrophy.

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14

Mercado-Flores, Yuridia, Cesar Hernandez-Rodriguez, Jose Ruiz-Herrera, and Lourdes Villa-Tanaca. "Proteinases and Exopeptidases from the Phytopathogenic Fungus Ustilago maydis." Mycologia 95, no. 2 (2003): 327. http://dx.doi.org/10.2307/3762044.

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15

Nchienzia, H. A., R. O. Morawicki, and V. P. Gadang. "Enzymatic hydrolysis of poultry meal with endo- and exopeptidases." Poultry Science 89, no. 10 (2010): 2273–80. http://dx.doi.org/10.3382/ps.2008-00558.

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16

Kenny, John. "Mammalian proteinases: A glossary and bibliography volume 2 exopeptidases." FEBS Letters 224, no. 1 (1987): 235–36. http://dx.doi.org/10.1016/0014-5793(87)80457-x.

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17

TURNER, A. J. "Mammalian Proteases: A Glossary and Bibliography; Volume 2: Exopeptidases." Biochemical Society Transactions 15, no. 6 (1987): 1198–99. http://dx.doi.org/10.1042/bst0151198a.

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18

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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19

KRUPA, Joanne C., Sadiq HASNAIN, Dorit K. NÄGLER, Robert MÉNARD, and John S. MORT. "S′2 substrate specificity and the role of His110 and His111 in the exopeptidase activity of human cathepsin B." Biochemical Journal 361, no. 3 (2002): 613–19. http://dx.doi.org/10.1042/bj3610613.

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The ability of the lysosomal cysteine protease cathepsin B to function as a peptidyldipeptidase (removing C-terminal dipeptides) has been attributed to the presence of two histidine residues (His110 and His111) present in the occluding loop, an extra peptide segment located in the primed side of the active-site cleft. Whereas His111 is unpaired, His110 is present as an ion pair with Asp22 on the main body of the protease. This ion pair appears to act as a latch to hold the loop in a closed position. The exopeptidase activity of cathepsin B, examined using quenched fluorescence substrates, was shown to have a 20-fold preference for aromatic side chains in the P′3 position relative to glutamic acid as the least favourable residue. Site-directed mutagenesis demonstrated that His111 makes a positive 10-fold contribution to the exopeptidase activity, whereas His110 is critical for this action with the Asp22—His110 ion pair stabilizing the electrostatic interaction by a maximum of 13.9kJ/mol (3.3kcal/mol). These studies showed that cathepsin B is optimized to act as an exopeptidase, cleaving dipeptides from protein substrates in a successive manner, because of its relaxed specificity in P′3 and its other subsites.

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20

Tomić, A., B. Kovačević, and S. Tomić. "Concerted nitrogen inversion and hydrogen bonding to Glu451 are responsible for protein-controlled suppression of the reverse reaction in human DPP III." Physical Chemistry Chemical Physics 18, no. 39 (2016): 27245–56. http://dx.doi.org/10.1039/c6cp04580d.

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21

Ewert, Jacob, Felix Schlierenkamp, Lena Nesensohn, Lutz Fischer, and Timo Stressler. "Improving the colloidal and sensory properties of a caseinate hydrolysate using particular exopeptidases." Food & Function 9, no. 11 (2018): 5989–98. http://dx.doi.org/10.1039/c8fo01749b.

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22

Kim, Jin-Soo, Min Ji Kim, Ki Hyun Kim, et al. "Debittering of Enzymatic Hydrolysate Using Exopeptidase Active Fractions from the Argentina Shortfin Squid Illex argentinus Hepatopancreas." Korean Journal of Fisheries and Aquatic Sciences 47, no. 2 (2014): 135–43. http://dx.doi.org/10.5657/kfas.2014.0135.

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23

Kluge, Bogusaw, Anna Gambin, and Wojciech Niemiro. "Modeling Exopeptidase Activity from LC-MS Data." Journal of Computational Biology 16, no. 2 (2009): 395–406. http://dx.doi.org/10.1089/cmb.2008.22tt.

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24

Woods, Glenn M., Michael L. Lathem, Edward J. Parish, Anna Markiw, and Leon W. Bone. "Exopeptidase activity in eggs ofTrichostrongylus colubriformis(Nematoda)." International Journal of Invertebrate Reproduction and Development 9, no. 3 (1986): 279–87. http://dx.doi.org/10.1080/01688170.1986.10510204.

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25

Takahashi, T., A. H. Dehdarani, S. Yonezawa, and J. Tang. "Porcine spleen cathepsin B is an exopeptidase." Journal of Biological Chemistry 261, no. 20 (1986): 9375–81. http://dx.doi.org/10.1016/s0021-9258(18)67665-3.

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26

NAGASAWA, Takashi, Toshihiro UCHIDA, and Ryoji ONODERA. "Exopeptidase Activity of Mixed Rumen Ciliate Protozoa." Nihon Chikusan Gakkaiho 63, no. 5 (1992): 481–87. http://dx.doi.org/10.2508/chikusan.63.481.

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27

Miazek, A., and B. Zagdanska. "Involvement of exopeptidases in dehydration tolerance of spring wheat seedlings." Biologia plantarum 52, no. 4 (2008): 687–94. http://dx.doi.org/10.1007/s10535-008-0133-1.

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28

Sapatinha, Maria, Carolina Camacho, Antónia Juliana Pais-Costa, Ana Luísa Fernando, António Marques, and Carla Pires. "Enzymatic Hydrolysis Systems Enhance the Efficiency and Biological Properties of Hydrolysates from Frozen Fish Processing Co-Products." Marine Drugs 23, no. 1 (2024): 14. https://doi.org/10.3390/md23010014.

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Co-products from the frozen fish processing industry often lead to financial losses. Therefore, it is essential to transform these co-products into profitable goods. This study explores the production of fish protein hydrolysates (FPH) from three co-products: the heads and bones of black scabbardfish (Aphanopus carbo), the carcasses of gilthead seabream (Sparus aurata), and the trimmings of Nile perch (Lates niloticus). Four enzymatic hydrolysis systems were tested: an endopeptidase (Alcalase, A), an exopeptidase (Protana, P), two-stage hydrolysis with an endopeptidase followed by an exopeptidase (A + P), and a single stage with endo- and exopeptidase (AP). The results show that combined enzymatic treatments, especially single-stage Alcalase and Protana (AP), achieved high protein yields (80%) and enhanced degrees of hydrolysis (34 to 49%), producing peptides with lower molecular weights. FPH exhibited significant antioxidant activity, in 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) assays, with EC50 values below 5 mg/mL. Additionally, AP hydrolysates demonstrated over 60% angiotensin-converting enzyme (ACE) inhibition at 5 mg/mL, indicating potential antihypertensive applications. Antidiabetic and anti-Alzheimer activities were present, but at relatively low levels. AP hydrolysates, especially from gilthead seabream, proved to be the most promising. This study highlights the value of fish co-products as sources of functional peptides, contributing to waste reduction, and their potential applications in food, agriculture, and nutraceuticals.

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29

Andersen, Knut-Jan, and J. Ken McDonald. "Presence and possible role of a renal brush-border Gly-Pro-X-releasing exopeptidase." American Journal of Physiology-Renal Physiology 253, no. 4 (1987): F649—F655. http://dx.doi.org/10.1152/ajprenal.1987.253.4.f649.

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Differential pelleting of a rat renal cortical homogenate clearly demonstrated the microsomal localization of an N-terminal exopeptidase of the tripeptidyl peptidase (TPP) class that typically requires a free N-terminus to catalyze the release of collagen-related (Gly-Pro-X) “triplets” at pH 7.0 (TPP 7). Once fractionated by differential pelleting, microsomal populations of different size were subfractionated by equilibrium banding in sucrose gradients for the purpose of comparing the distribution profiles and the isopycnic banding densities of TPP 7 to those for known marker enzymes. This analytical approach permitted the localization of these enzymes to specific membrane domains in the renal cortex and provided evidence for the brush-border location of TPP 7. Notably, dipeptidyl peptidase IV (DPP IV), an established plasma membrane exopeptidase with a prolyl-bond specificity, gave banding densities and distributions that were consistent with the presence of both TPP 7 and DPP IV in the same membrane compartment. Because triplets of the Gly-Pro-X type released by TPP 7 would be ideal substrates for DPP IV, a coupled TPP 7-DPP IV exopeptidase mechanism at the luminal surface (brush border) of proximal tubule cells could therefore make a major contribution to the renal degradation and reabsorption of filtered collagen fragments. tripeptidyl peptidase; aminopeptidase; collagen; rat kidney cortex Submitted on February 11, 1987 Accepted on May 13, 1987

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30

Turk, Dŭsan, Boris Turk, and Vito Turk. "Papain-like lysosomal cysteine proteases and their inhibitors: drug discovery targets?" Biochemical Society Symposia 70 (September 1, 2003): 15–30. http://dx.doi.org/10.1042/bss0700015.

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Papain-like lysosomal cysteine proteases are processive and digestive enzymes that are expressed in organisms from bacteria to humans. Increasing knowledge about the physiological and pathological roles of cysteine proteases is bringing them into the focus of drug discovery research. These proteases have rather short active-site clefts, comprising three well defined substrate-binding subsites (S2, S1 and S1') and additional broad binding areas (S4, S3, S2' and S3'). The geometry of the active site distinguishes cysteine proteases from other protease classes, such as serine and aspartic proteases, which have six and eight substrate-binding sites respectively. Exopeptidases (cathepsins B, C, H and X), in contrast with endopeptidases (such as cathepsins L, S, V and F), possess structural features that facilitate the binding of N- and C-terminal groups of substrates into the active-site cleft. Other than a clear preference for free chain termini in the case of exopeptidases, the substrate-binding sites exhibit no strict specificities. Instead, their subsite preferences arise more from the specific exclusion of substrate types. This presents a challenge for the design of inhibitors to target a specific cathepsin: only the cumulative effect of an assembly of inhibitor fragments will bring the desired result.

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31

Helbig, Andreas O., and Andreas Tholey. "Exopeptidase Assisted N- and C-Terminal Proteome Sequencing." Analytical Chemistry 92, no. 7 (2020): 5023–32. http://dx.doi.org/10.1021/acs.analchem.9b05288.

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32

Rowsell, S., R. A. Pauptit, A. D. Tucker, et al. "Crystal structure of carboxypeptidase G2and comparison with other zinc-containing exopeptidases." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (1996): C138. http://dx.doi.org/10.1107/s0108767396093725.

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33

Kugler, P., and A. Huber. "Histochemical demonstration of exopeptidases in the rat visceral yolk-sac epithelium." Histochemistry 82, no. 4 (1985): 397–400. http://dx.doi.org/10.1007/bf00494070.

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34

Raksakulthai, Rocharake, and Norman F. Haard. "Exopeptidases and Their Application to Reduce Bitterness in Food: A Review." Critical Reviews in Food Science and Nutrition 43, no. 4 (2003): 401–45. http://dx.doi.org/10.1080/10408690390826572.

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35

Sohár, István, Hans-Jürgen Hütter, Ferenc Guba, and Reinhard J. Haschen. "Changes in exopeptidase activities in skeletal muscles during disuse." International Journal of Biochemistry 18, no. 12 (1986): 1129–34. http://dx.doi.org/10.1016/0020-711x(86)90087-x.

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36

Lee, Michael J., and John H. Anstee. "Characterization of midgut exopeptidase activity from larval Spodoptera littoralis." Insect Biochemistry and Molecular Biology 25, no. 1 (1995): 63–71. http://dx.doi.org/10.1016/0965-1748(94)00041-f.

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37

Tao, L., H. Zhou, X. S. Guo, R. J. Long, Y. Zhu, and W. Cheng. "Contribution of exopeptidases to formation of nonprotein nitrogen during ensiling of alfalfa." Journal of Dairy Science 94, no. 8 (2011): 3928–35. http://dx.doi.org/10.3168/jds.2010-3752.

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38

Botbol, V., and O. A. Scornik. "Role of bestatin-Sensitive Exopeptidases in the Intracellular Degradation of Hepatic Proteins." Journal of Biological Chemistry 264, no. 23 (1989): 13504–9. http://dx.doi.org/10.1016/s0021-9258(18)80025-4.

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39

Osnes, Knut Kr, and Viggo Mohr. "On the purification and characterization of exopeptidases from antarctic krill, Euphausia superba." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 83, no. 2 (1986): 445–58. http://dx.doi.org/10.1016/0305-0491(86)90394-9.

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40

Ge, Shi-Jun, and Long-Xiang Zhang. "The immobilized porcine pancreatic exopeptidases and its application in casein hydrolysates debittering." Applied Biochemistry and Biotechnology 59, no. 2 (1996): 159–65. http://dx.doi.org/10.1007/bf02787817.

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41

Obayashi, Yumiko, and Satoru Suzuki. "Proteolytic enzymes in coastal surface seawater: Significant activity of endopeptidases and exopeptidases." Limnology and Oceanography 50, no. 2 (2005): 722–26. http://dx.doi.org/10.4319/lo.2005.50.2.0722.

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Andersen, K. J., and J. K. McDonald. "Subcellular distribution of renal tripeptide-releasing exopeptidases active on collagen-like sequences." American Journal of Physiology-Renal Physiology 252, no. 5 (1987): F890—F898. http://dx.doi.org/10.1152/ajprenal.1987.252.5.f890.

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The rat kidney cortex was found to contain two N-terminal exopeptidases of the tripeptidyl peptidase (TPP) class. Each required a free N-terminus to catalyze the release of collagen-related (Gly-Pro-X) "triplets." In accordance with their apparent pH optima, activities were routinely determined fluorimetrically at pH 4.0 (TPP 4) and at pH 7.0 (TPP 7) on Gly-Pro-Met-2-naphthylamide. The specific activity in both the homogenate and the classical subfractions was much greater at pH 7 than at pH 4. Subfractionation of the microsomal fraction by equilibrium banding in sucrose did not separate the TPP 4 and TPP 7 activities. The banding density (1.18 g/ml) and the distribution patterns for TPP 7 in the microsomal subfractions, and also in the subfractions of the small lysosomes in the mitochondrial-lysosomal (ML) fraction, demonstrate that TPP 7 is associated with smooth membranes. The TPP 4 and TPP 7 activities were clearly separated during subfractionation of the ML fraction. Rate sedimentation demonstrated that TPP 4 was present in the large, fast-sedimenting lysosomes (protein droplets) and in a heterogeneous broad band of smaller lysosomes. Equilibrium banding of the small lysosomes gave two distinct TPP 4-containing populations at densities 1.20 and 1.235 g/ml. Notably, dipeptidyl peptidase II (DPP II) gave identical banding densities and showed distributions very similar to TPP 4.(ABSTRACT TRUNCATED AT 250 WORDS)

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Jiráček, Jiří, Tomislav Barth, Jiří Velek, Ivo Bláha, Jan Pospíšek, and Ivan Svoboda. "Purification of Penicillin Amidohydrolase, an Enzyme for Semisynthetic Procedures." Collection of Czechoslovak Chemical Communications 57, no. 10 (1992): 2187–91. http://dx.doi.org/10.1135/cccc19922187.

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Penicillin amidohydrolase (EC 3.5.1.11.) is one of the few enzymes used successfully for deprotection of primary amino groups of semisynthetic peptides. The available material is usually contamined by endo- and exopeptidases. We managed to prepare the enzyme devoid of trypsin- and chymotrypsin-like activities using affinity chromatography with specific ligands: Gly-D-Phe-Phe-Tyr-Thr-Pro-Lys-Thr (the fF peptide) and Leu-Gly-Val-D-Arg-Arg-Gly-Phe (the rR peptide). For further purification of the enzyme affinity chromatography with N-phenylacetyl-D-tert-Leu as a ligand was used.

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St. Leger, Raymond J. "The role of cuticle-degrading proteases in fungal pathogenesis of insects." Canadian Journal of Botany 73, S1 (1995): 1119–25. http://dx.doi.org/10.1139/b95-367.

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The proteinaceous outer integument of insects forms an effective barrier against most microbes. Only the 700 known species of entomopathogenic fungi effect entry into their hosts by breaching the cuticle. There is accumulating evidence that the ability of fungi to degrade protein may aid their invasion of and growth in this orderly complex structure. Evidence for the particular importance of proteinases derives largely from studies of their production in infected cuticles associated with cuticle degradation, the effects of proteinase inhibitors on pathogen behavior, and by the analysis of protease-deficient mutants. More recently, studies have included the cloning, identification, and manipulation of specific protease genes of Metarhizium anisopliae, particularly those of the subtilisin (chymoelastase) type (designated Pr1) also produced by many other entomopathogenic fungi. Following solubilization of cuticle proteins by Pr1-type endoproteases, complete degradation of the cuticle involves a number of interacting enzyme species including a family of trypsin-like proteinases, metalloproteinases, several aminopeptidases, and a carboxypeptidase. Testing genetically engineered M. anisopliae null mutants of Pr1 indicated that the other endopeptidases can partially substitute for Pr1. The exopeptidases further degrade peptides released by the endopeptidases producing free amino acids for uptake and metabolism. Utilization of these enzymes has assisted investigators in understanding cuticle structure and how the cuticle is degraded naturally, and could lead to improved strain selection of entomopathogenic fungi or the introduction of their genes into other microbes and plants for the purpose of insect control. Key words: proteinaceous insect cuticle, pathogen endopeptidases, exopeptidases, multiple isozymes, enzyme regulation.

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MORT, John S., Marie-Claude MAGNY, and Eunice R. LEE. "Cathepsin B: an alternative protease for the generation of an aggrecan ‘metalloproteinase’ cleavage neoepitope." Biochemical Journal 335, no. 3 (1998): 491–94. http://dx.doi.org/10.1042/bj3350491.

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Previously, only matrix metalloproteinases were believed capable of cleaving the cartilage proteoglycan, aggrecan, between Asn341 and Phe342, to yield a small G1 fragment terminating in the residues VDIPEN. We show that the combined endo- and exopeptidase activities of the cysteine protease, cathepsin B, also generate this epitope, suggesting that it should no longer be considered as an exclusive marker of metalloproteinase activity.

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Diaz-Jimenez, David, Maria Grazia Petrillo, Jonathan T. Busada, Marcela A. Hermoso, and John A. Cidlowski. "Glucocorticoids mobilize macrophages by transcriptionally up-regulating the exopeptidase DPP4." Journal of Biological Chemistry 295, no. 10 (2020): 3213–27. http://dx.doi.org/10.1074/jbc.ra119.010894.

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Glucocorticoids are potent endogenous anti-inflammatory molecules, and their cognate receptor, glucocorticoid receptor (GR), is expressed in nearly all immune cells. Macrophages are heterogeneous immune cells having a central role in both tissue homeostasis and inflammation and also play a role in the pathogenesis of some inflammatory diseases. Paradoxically, glucocorticoids have only a limited efficacy in controlling the resolution of these macrophage-related diseases. Here, we report that the transcriptomes of monocyte-like THP-1 cells and macrophage-like THP-1 cells (THP1-MΦ) have largely conserved gene expression patterns. In contrast, the differentiation to THP1-MΦ significantly altered the sensitivity of gene transcription to glucocorticoids. Among glucocorticoid-regulated genes, we identified the exopeptidase dipeptidyl peptidase-4 (DPP4) as a critical glucocorticoid-responsive gene in THP1-MΦ. We found that GR directly induces DPP4 gene expression by binding to two glucocorticoid-responsive elements (GREs) within the DPP4 promoter. Additionally, we show that glucocorticoid-induced DPP4 expression is blocked by the GR antagonist RU-486 and by GR siRNA transfection and that DPP4 enzyme activity is reduced by DPP4 inhibitors. Of note, glucocorticoids highly stimulated macrophage mobility; unexpectedly, DPP4 mediated the glucocorticoid-induced macrophage migration, and siRNA-mediated knockdowns of GR and DPP4 blocked dexamethasone-induced THP1-MΦ migration. Moreover, glucocorticoid-induced DPP4 activation was also observed in proinflammatory M1-polarized murine macrophages, as well as peritoneal macrophages, and was associated with increased macrophage migration. Our results indicate that glucocorticoids directly up-regulate DPP4 expression and thereby induce migration in macrophages, potentially explaining why glucocorticoid therapy is less effective in controlling macrophage-dominated inflammatory disorders.

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Wagner, R. M. "Exopeptidase-high-performance liquid chromatography peptide mapping of small peptides." Journal of Chromatography A 326 (June 1985): 399–405. http://dx.doi.org/10.1016/s0021-9673(01)87465-3.

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Peters, Jürgen, Anne-Marie Schönegge, Beate Rockel, and Wolfgang Baumeister. "Molecular ruler of tripeptidylpeptidase II: Mechanistic principle of exopeptidase selectivity." Biochemical and Biophysical Research Communications 414, no. 1 (2011): 209–14. http://dx.doi.org/10.1016/j.bbrc.2011.09.058.

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Scharpé, Simon L., Greta C. Vanhoof, Ingrid A. De Meester, et al. "Exopeptidases in human platelets: an indication for proteolytic modulation of biologically active peptides." Clinica Chimica Acta 195, no. 3 (1991): 125–31. http://dx.doi.org/10.1016/0009-8981(91)90132-v.

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Mihelič, Marko, Cory Teuscher, Vito Turk, and Dušan Turk. "Mouse stefins A1 and A2 (Stfa1andStfa2) differentiate between papain-like endo- and exopeptidases." FEBS Letters 580, no. 17 (2006): 4195–99. http://dx.doi.org/10.1016/j.febslet.2006.06.076.

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