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Journal articles on the topic 'Proteases; Peptidases; enzymes'

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Published: 4 June 2021
Last updated: 15 February 2022

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1

Mamo, Jermen, and Fassil Assefa. "The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries." Journal of Food Quality 2018 (July 3, 2018): 1–15. http://dx.doi.org/10.1155/2018/7957269.

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Proteases represent one of the three largest groups of industrial enzymes and account for about 60% of the total global enzymes sale. According to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, proteases are classified in enzymes of class 3, the hydrolases, and the subclass 3.4, the peptide hydrolases or peptidase. Proteases are generally grouped into two main classes based on their site of action, that is, exopeptidases and endopeptidases. Protease has also been grouped into four classes based on their catalytic action: aspartic, cysteine, metallo
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2

Salvesen, Guy S., Gillian Murphy та Hideaki Nagase. "The trap hypothesis: α2 and protease inhibition". Biochemist 28, № 3 (2006): 46–48. http://dx.doi.org/10.1042/bio02803046.

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In the 1970s, the Strangeways Laboratory in Cambridge consisted of a small number of groups collectively focused on the mechanisms of pathological connective-tissue damage. One of these groups, headed by Alan Barrett, was breaking ground on the destruction of the protein components of the matrix and was therefore heavily involved in identifying and categorizing newly emerging types of tissue-degrading enzymes. These enzymes, which Alan Barrett urges scientists to call peptidases, are also commonly called proteases or proteinases*. In the early 1970s, there were about 100 described human peptid
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3

Wolke, Carmen, Alexander Teumer, Karlhans Endlich, et al. "Serum protease activity in chronic kidney disease patients: The GANI_MED renal cohort." Experimental Biology and Medicine 242, no. 5 (2016): 554–63. http://dx.doi.org/10.1177/1535370216684040.

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Serum or plasma proteases have been associated with various diseases including cancer, inflammation, or reno-cardiovascular diseases. We aimed to investigate whether the enzymatic activities of serum proteases are associated with the estimated glomerular filtration rate (eGFR) in patients with different stages of chronic kidney disease (CKD). Our study population comprised 268 participants of the “Greifswald Approach to Individualized Medicine” (GANI_MED) cohort. Enzymatic activity of aminopeptidase A, aminopeptidase B, alanyl (membrane) aminopeptidase, insulin-regulated aminopeptidase, puromy
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4

SHAN, Lu, Thomas MARTI, Ludvig M. SOLLID, Gary M. GRAY, and Chaitan KHOSLA. "Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue." Biochemical Journal 383, no. 2 (2004): 311–18. http://dx.doi.org/10.1042/bj20040907.

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Prolyl endopeptidases have potential for treating coeliac sprue, a disease of the intestine caused by proteolytically resistant peptides from proline-rich prolamins of wheat, barley and rye. We compared the properties of three similar bacterial prolyl endopeptidases, including the known enzymes from Flavobacterium meningosepticum (FM) and Sphingomonas capsulate (SC) and a novel enzyme from Myxococcus xanthus (MX). These enzymes were interrogated with reference chromogenic substrates, as well as two related gluten peptides (PQPQLPYPQPQLP and LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF), believed to play
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5

Marokházi, Judit, Katalin Lengyel, Szilvia Pekár, et al. "Comparison of Proteolytic Activities Produced by Entomopathogenic Photorhabdus Bacteria: Strain- and Phase-Dependent Heterogeneity in Composition and Activity of Four Enzymes." Applied and Environmental Microbiology 70, no. 12 (2004): 7311–20. http://dx.doi.org/10.1128/aem.70.12.7311-7320.2004.

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ABSTRACT Twenty strains (including eight phase variant pairs) of nematode-symbiotic and insect-pathogenic Photorhabdus bacteria were examined for the production of proteolytic enzymes by using a combination of several methods, including gelatin liquefaction, zymography coupled to native and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and activity measurement with two chromogen substrate types. Four protease activities (∼74, ∼55, ∼54, and ∼37 kDa) could be separated. The N-terminal sequences of three of the proteases were determined, and a comparison with sequences in databases a
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6

Kryukov, V. S., S. V. Zinoviev, and R. V. Nekrasov. "Proteases in the diet of monogastric animals." Agrarian science 344, no. 1 (2021): 30–38. http://dx.doi.org/10.32634/0869-8155-2021-344-1-30-38.

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There are many proteases, and about 2% of the human genome is involved in the regulation of their formation. The share of proteases involved in digestion accounts for only a small part. Despite this, the mechanisms of action of digestive proteases are less studied than carbohydrases and lipases. The incorporation of exogenous proteases into young animal feeds is often accompanied by improved utilization of protein and other nutrients. Exogenous proteases degrade inhibitors of the endogenous protease and lectins in feed. Alkaline proteases are of interest due to their broader substrate specific
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7

Massaoud, Mustafa K., Judit Marokh�zi, Andr�s Fodor, and Istv�n Venekei. "Proteolytic Enzyme Production by Strains of the Insect Pathogen Xenorhabdus and Characterization of an Early-Log-Phase-Secreted Protease as a Potential Virulence Factor." Applied and Environmental Microbiology 76, no. 20 (2010): 6901–9. http://dx.doi.org/10.1128/aem.01567-10.

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ABSTRACT As a comparison to a similar study on Photorhabdus strains, 15 Xenorhabdus bacterial strains and secondary phenotypic variants of two strains were screened for proteolytic activity by five detection methods. Although the number and intensity of proteolytic activities were different, every strain was positive for proteolytic activity by several tests. Zymography following native PAGE detected two groups of activities with different substrate affinities and a higher and lower electrophoretic mobility that were distinguished as activity 1 and 2, respectively. Zymography following SDS-PAG
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8

Suido, H., T. Eguchi, T. Tanaka, and M. Nakamura. "Identification of Periodontopathic Bacteria Based Upon their Peptidase Activities." Advances in Dental Research 2, no. 2 (1988): 304–9. http://dx.doi.org/10.1177/08959374880020021701.

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Black-pigmented Bacteroides (BPB) and spirochetes are associated with some forms of periodontal diseases. The enzymes produced by these bacteria may participate in the destruction of gingival and periodontal tissues. Certain proteases and peptidases are unique to Bacteroides gingivalis and Treponema denticola. Our purpose was to study the peptidases of periodontopathogens and to evaluate the use of unique peptidases for detection and identification of these bacteria. Bacteria used were BPB, Treponema, Fusobacterium, Capnocytophaga, Actinobacillus (Haemophilus), and Eikenella species. Twenty-fi
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9

Sriranganadane, Dev, Utz Reichard, Karine Salamin, et al. "Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium." Microbiology 157, no. 5 (2011): 1541–50. http://dx.doi.org/10.1099/mic.0.048603-0.

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In an acidic protein medium Aspergillus fumigatus secretes an aspartic endoprotease (Pep) as well as tripeptidyl-peptidases, a prolyl-peptidase and carboxypeptidases. In addition, LC-MS/MS revealed a novel glutamic protease, AfuGprA, homologous to Aspergillus niger aspergillopepsin II. The importance of AfuGprA in protein digestion was evaluated by deletion of its encoding gene in A. fumigatus wild-type D141 and in a pepΔ mutant. Either A. fumigatus Pep or AfuGprA was shown to be necessary for fungal growth in protein medium at low pH. Exoproteolytic activity is therefore not sufficient for co
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10

Heywood, Astra, and Iain L. Lamont. "Cell envelope proteases and peptidases of Pseudomonas aeruginosa: multiple roles, multiple mechanisms." FEMS Microbiology Reviews 44, no. 6 (2020): 857–73. http://dx.doi.org/10.1093/femsre/fuaa036.

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ABSTRACT Pseudomonas aeruginosa is a Gram-negative bacterium that is commonly isolated from damp environments. It is also a major opportunistic pathogen, causing a wide range of problematic infections. The cell envelope of P. aeruginosa, comprising the cytoplasmic membrane, periplasmic space, peptidoglycan layer and outer membrane, is critical to the bacteria's ability to adapt and thrive in a wide range of environments. Over 40 proteases and peptidases are located in the P. aeruginosa cell envelope. These enzymes play many crucial roles. They are required for protein secretion out of the cyto
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11

Valencia, Ricardo, Valentina González, Agustina Undabarrena, Leonardo Zamora-Leiva, Juan A. Ugalde, and Beatriz Cámara. "An Integrative Bioinformatic Analysis for Keratinase Detection in Marine-Derived Streptomyces." Marine Drugs 19, no. 6 (2021): 286. http://dx.doi.org/10.3390/md19060286.

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Keratinases present promising biotechnological applications, due to their ability to degrade keratin. Streptomyces appears as one of the main sources of these enzymes, but complete genome sequences of keratinolytic bacteria are still limited. This article reports the complete genomes of three marine-derived streptomycetes that show different levels of feather keratin degradation, with high (strain G11C), low (strain CHD11), and no (strain Vc74B-19) keratinolytic activity. A multi-step bioinformatics approach is described to explore genes encoding putative keratinases in these genomes. Despite
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MAROKHÁZI, Judit, György KÓCZÁN, Ferenc HUDECZ, László GRÁF, András FODOR, and István VENEKEI. "Enzymic characterization with progress curve analysis of a collagen peptidase from an enthomopathogenic bacterium, Photorhabdus luminescens." Biochemical Journal 379, no. 3 (2004): 633–40. http://dx.doi.org/10.1042/bj20031116.

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A proteolytic enzyme, Php-B (Photorhabdus protease B), was purified from the entomopathogenic bacterium, Photorhabdus luminescens. The enzyme is intracellular, and its molecular mass is 74 kDa. Tested on various peptide and oligopeptide substrates, Php-B hydrolysed only oligopeptides, with significant activity against bradykinin and a 2-furylacryloyl-blocked peptide, Fua-LGPA (2-furylacryloyl-Leu-Gly-Pro-Ala; kcat=3.6×102 s−1, Km=5.8×10−5 M−1, pH optimum approx. 7.0). The pKa1 and the pKa2 values of the enzyme activity (6.1 and 7.9 respectively), as well as experiments with enzyme inhibitors a
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Zilda, Dewi Seswita, Yusro Nuri Fawzya, and Agustinus Robert Uria. "Identification of Protease-Producing Bacteria Isolated from Banyuwedang, Bali, and Characterization of its Protease." Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 13, no. 3 (2018): 101. http://dx.doi.org/10.15578/squalen.v13i3.367.

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Proteases or peptidases is known as a largest group of hydrolytic enzymes and have been applied in various industries such as food, pharmacy, leather, detergent and waste treatment. Although they are also produced by plants and animals, microbes remain the main source of proteases in the world market which mostly derived from Bacillus sp. Aims of this research were to identify isolate BII-1 and study its protease. Analysis of 16Sr RNA sequencing showed the identity of BII-1 as Bacillus subtilis (99% similarity with the same species in GenBank). It was found that protease from BII-1 exhibited o
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14

De Oliveira Martinez, Juan Pinheiro, Guiqin Cai, Matthias Nachtschatt, et al. "Challenges and Opportunities in Identifying and Characterising Keratinases for Value-Added Peptide Production." Catalysts 10, no. 2 (2020): 184. http://dx.doi.org/10.3390/catal10020184.

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Keratins are important structural proteins produced by mammals, birds and reptiles. Keratins usually act as a protective barrier or a mechanical support. Millions of tonnes of keratin wastes and low value co-products are generated every year in the poultry, meat processing, leather and wool industries. Keratinases are proteases able to breakdown keratin providing a unique opportunity of hydrolysing keratin materials like mammalian hair, wool and feathers under mild conditions. These mild conditions ameliorate the problem of unwanted amino acid modification that usually occurs with thermochemic
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15

LEITING, Barbara, KellyAnn D. PRYOR, Joseph K. WU, et al. "Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII." Biochemical Journal 371, no. 2 (2003): 525–32. http://dx.doi.org/10.1042/bj20021643.

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There is currently intense interest in the emerging group of proline-specific dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific dipeptidases, DPP-VII (also known as quiescent cell proline dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII
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16

Icimoto, Marcelo Yudi, Adrianne Marlise Mendes Brito, Marcos Paulo Cyrillo Ramos, Vitor Oliveira, and Iseli Lourenço Nantes-Cardoso. "Increased Stability of Oligopeptidases Immobilized on Gold Nanoparticles." Catalysts 10, no. 1 (2020): 78. http://dx.doi.org/10.3390/catal10010078.

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The metallopeptidases thimet oligopeptidase (THOP, EC 3.4.24.25) and neurolysin (NEL, EC 3.4.24.26) are enzymes that belong to the zinc endopeptidase M13 family. Numerous studies suggest that these peptidases participate in the processing of bioactive peptides such as angiotensins and bradykinin. Efforts have been conducted to develop biotechnological tools to make possible the use of both proteases to regulate blood pressure in mice, mainly limited by the low plasmatic stability of the enzymes. In the present study, it was investigated the use of nanotechnology as an efficient strategy for to
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17

Jedeszko, Christopher, and Bonnie F. Sloane. "Cysteine cathepsins in human cancer." Biological Chemistry 385, no. 11 (2004): 1017–27. http://dx.doi.org/10.1515/bc.2004.132.

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Abstract Proteases play causal roles in the malignant progression of human tumors. This review centers on the roles in this process of cysteine cathepsins, i.e., peptidases belonging to the papain family (C1) of the CA clan of cysteine proteases. Cysteine cathepsins, most likely along with matrix metalloproteases (MMPs) and serine proteases, degrade the extracellular matrix, thereby facilitating growth and invasion into surrounding tissue and vasculature. Studies on tumor tissues and cell lines have shown changes in expression, activity and distribution of cysteine cathepsins in numerous human
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18

Reinheckel, T., J. Deussing, W. Roth, and C. Peters. "Towards Specific Functions of Lysosomal Cysteine Peptidases: Phenotypes of Mice Deficient for Cathepsin B or Cathepsin L." Biological Chemistry 382, no. 5 (2001): 735–41. http://dx.doi.org/10.1515/bc.2001.089.

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Abstract The lysosomal cysteine peptidases cathepsin B and cathepsin L are abundant and ubiquitously expressed members of the papain family, and both enzymes contribute to the terminal degradation of proteins in the lysosome. However, there is accumulating evidence for specific functions of lysosomal proteases in health and disease. The generation of knock out mouse strains that are deficient in lysosomal proteases provides a valuable tool for evaluation of existing hypotheses and gaining new insights into the in vivo functions of these proteases. In this minireview, we summarise and discuss t
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Sheikhs, Nabiha Naeem, Qurat-ul-ain, and Saba Altaf. "Production of Extracellular Protease from Bacterial Co-cultures using Solid State Fermentation." BioScientific Review 2, no. 4 (2020): 13–23. http://dx.doi.org/10.32350/bsr/2020/24/726.

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Proteases (also known as peptidases or proteinases) are hydrolytic enzymes that cleave proteins into amino acids. They comprise 60% of the total industrial usage of enzymes worldwide and can be obtained from many sources. The current study aims to isolate and screen protease-producing bacterial strains from the soil and to produce protease from the bacterial co-cultures using solid-state fermentation (SSF). Primary screening of the protease-producing bacterial strains was carried out on skim milk agar and they were sub-cultured and preserved on the nutrient agar for further testing. Thirty-two
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Sheikhs, Nabiha Naeem, Qurat-ul-ain, and Saba Altaf. "Production of Extracellular Protease from Bacterial Co-cultures using Solid State Fermentation." BioScientific Review 2, no. 4 (2020): 13–23. http://dx.doi.org/10.32350/bsr.0204.02.

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Proteases (also known as peptidases or proteinases) are hydrolytic enzymes that cleave proteins into amino acids. They comprise 60% of the total industrial usage of enzymes worldwide and can be obtained from many sources. The current study aims to isolate and screen protease-producing bacterial strains from the soil and to produce protease from the bacterial co-cultures using solid-state fermentation (SSF). Primary screening of the protease-producing bacterial strains was carried out on skim milk agar and they were sub-cultured and preserved on the nutrient agar for further testing. Thirty-two
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Ferraris, R. P., W. W. Kwan, and J. Diamond. "Regulatory signals for intestinal amino acid transporters and peptidases." American Journal of Physiology-Gastrointestinal and Liver Physiology 255, no. 2 (1988): G151—G157. http://dx.doi.org/10.1152/ajpgi.1988.255.2.g151.

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Dietary protein ultimately regulates many processes involved in protein digestion, but it is often unclear whether proteins themselves, peptides, or amino acids (AAs) are the proximate regulatory signal. Hence we compared several processes involved in protein digestion in mice adapted to one of three rations, identical except for containing 54% of either casein, a partial hydrolysate of casein, or a free AA mixture simulating a complete hydrolysate of casein. We measured brush-border uptakes of seven AAs that variously serve as substrates for four AA transporters, and brush-border and cytosoli
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22

Kumari, Saravana, and Reshma R. "Effect of alkaline protease produced from fish waste as substrate by Bacillus clausii on destaining of blood stained fabric." Journal of Tropical Life Science 11, no. 1 (2021): 59–66. http://dx.doi.org/10.11594/jtls.11.01.08.

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Alkaline protease or peptidases are the largest groups of enzymes in the biological industry with a variety of application in manufacturing units used in the process of substrate stabilization, dehairing, diagnosis, extraction, food production, destaining, etc., where the pH of the environmental conditions remain above neutral pH. Because of these wider applications of alkaline proteases in industries, their demand is increasing to compete with their chemical counterpart. An alkaline tolerant bacterial strain Bacillus clausii wasisolated from fish waste and used for mass production of alkaline
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González, Valentina, María José Vargas-Straube, Walter O. Beys-da-Silva, et al. "Enzyme Bioprospection of Marine-Derived Actinobacteria from the Chilean Coast and New Insight in the Mechanism of Keratin Degradation in Streptomyces sp. G11C." Marine Drugs 18, no. 11 (2020): 537. http://dx.doi.org/10.3390/md18110537.

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Marine actinobacteria are viewed as a promising source of enzymes with potential technological applications. They contribute to the turnover of complex biopolymers, such as pectin, lignocellulose, chitin, and keratin, being able to secrete a wide variety of extracellular enzymes. Among these, keratinases are a valuable alternative for recycling keratin-rich waste, which is generated in large quantities by the poultry industry. In this work, we explored the biocatalytic potential of 75 marine-derived actinobacterial strains, focusing mainly on the search for keratinases. A major part of the str
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Sharikov, A. Y., E. N. Sokolova, M. V. Amelyakina, T. V. Yuraskina, V. V. Ivanov, and E. M. Serba. "Development of a concept for the production of wheat snacks with the elimination of gluten by the biocatalysis." Proceedings of the Voronezh State University of Engineering Technologies 82, no. 4 (2021): 77–83. http://dx.doi.org/10.20914/2310-1202-2020-4-77-83.

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The increase in the number of cases of allergic reactions and celiac disease is an important problem. The solution to this problem is the search and development of relevant and effective ways to eliminate gluten. Specific amino acid sequences glutamine and proline determine the resistance to protease hydrolysis of the structural domains of gluten fractions. The analysis of the literature data showed that an alternative to the gluten-free diet is the use of biotechnological methods for modifying ingredients containing gluten. Such methods include the use of leavens on the base of lactic acid ba
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Michalska, Karolina, Andrew Steen, Gekleng Chhor, et al. "Structure and specificity of novel aminopeptidase from marine sediment Archaea." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C468. http://dx.doi.org/10.1107/s205327331409531x.

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The Earth's microbial diversity remained largely unexplored until recent developments in DNA sequencing. Novel methods enabled us to access genomic information of uncultured microbial organisms and create hypotheses about their metabolic capabilities. These predictions primarily rely on the sequence similarity between a novel protein and characterized proteins. Such an approach introduces a "culture" bias: the well-understood proteins come from a set of laboratory-grown bacteria, while novel microbial proteins are obtained from a variety of environments, including the most extreme. One such ni
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John-White, Marietta, Geoff J. Dumsday, Priscilla Johanesen, Dena Lyras, Nyssa Drinkwater та Sheena McGowan. "Crystal structure of a β-aminopeptidase from an AustralianBurkholderiasp." Acta Crystallographica Section F Structural Biology Communications 73, № 7 (2017): 386–92. http://dx.doi.org/10.1107/s2053230x17007737.

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β-Aminopeptidases are a unique group of enzymes that have the unusual capability to hydrolyze N-terminal β-amino acids from synthetic β-peptides. β-Peptides can form secondary structures mimicking α-peptide-like structures that are resistant to degradation by most known proteases and peptidases. These characteristics of β-peptides give them great potential as peptidomimetics. Here, the X-ray crystal structure of BcA5-BapA, a β-aminopeptidase from a Gram-negativeBurkholderiasp. that was isolated from activated sludge from a wastewater-treatment plant in Australia, is reported. The crystal struc
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Uddin, Md Jalal, Jirapat Dawan, Gibeom Jeon, Tao Yu, Xinlong He, and Juhee Ahn. "The Role of Bacterial Membrane Vesicles in the Dissemination of Antibiotic Resistance and as Promising Carriers for Therapeutic Agent Delivery." Microorganisms 8, no. 5 (2020): 670. http://dx.doi.org/10.3390/microorganisms8050670.

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The rapid emergence and spread of antibiotic-resistant bacteria continues to be an issue difficult to deal with, especially in the clinical, animal husbandry, and food fields. The occurrence of multidrug-resistant bacteria renders treatment with antibiotics ineffective. Therefore, the development of new therapeutic methods is a worthwhile research endeavor in treating infections caused by antibiotic-resistant bacteria. Recently, bacterial membrane vesicles (BMVs) have been investigated as a possible approach to drug delivery and vaccine development. The BMVs are released by both pathogenic and
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Delfini, Claudio, Chiara Cocito, and M. Bonino. "A review. Biochemical and molecular mechanisms in Saccharomyces cerevisiae that are involved in the formation of some volatile compounds in wines." OENO One 33, no. 4 (1999): 195. http://dx.doi.org/10.20870/oeno-one.1999.33.4.1018.

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<p style="text-align: justify;">There are evidences that a grape must of a non aromatic vine, not having perfume and revealing by gaschromatographie only some classes of compounds common to the musts of all the vine varieties, can originate a pool of characterizing fragrant substances after contact with the yeast during fermentation. Therefore, despite the scarce scientific knowledge available on biochemical mechanisms involved in <em>Saccharomyces cerevisiae</em> in the formation of a wine aromatic pattern, it can be likely hypothesized that the yeast could be the biological
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Llorente-Bousquets, Adriana, Sandra Pérez-Munguía, and Amelia Farrés. "Novel extracellular proteolytic activity inPediococcus acidilacticiATCC 8042." Canadian Journal of Microbiology 54, no. 8 (2008): 694–99. http://dx.doi.org/10.1139/w08-055.

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Proteolytic systems are common in lactic acid bacteria, but there are few reports about proteases or peptidases in the genus Pediococcus . To evaluate the presence of these types of enzymes, Pediococcus acidilactici ATCC 8042 was cultured in MRS broth. Supernatants collected during the log phase showed proteolytic activity towards an elastin dispersion when assayed using a spectrophotometer. Zn2+showed a stimulatory effect, and the proteolytic activity reached its maximum when 200 mmol/L NaCl was included in the reaction buffer. On the other hand, activity was reduced when 5 mmol/L EDTA, 10 mm
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Peng, Sheng-Bin, Li Wang, John Moomaw, et al. "Biochemical Characterization of Signal Peptidase I from Gram-Positive Streptococcus pneumoniae." Journal of Bacteriology 183, no. 2 (2001): 621–27. http://dx.doi.org/10.1128/jb.183.2.621-627.2001.

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ABSTRACT Bacterial signal peptidase I is responsible for proteolytic processing of the precursors of secreted proteins. The enzymes from gram-negative and -positive bacteria are different in structure and specificity. In this study, we have cloned, expressed, and purified the signal peptidase I of gram-positive Streptococcus pneumoniae. The precursor of streptokinase, an extracellular protein produced in pathogenic streptococci, was identified as a substrate of S. pneumoniae signal peptidase I. Phospholipids were found to stimulate the enzymatic activity. Mutagenetic analysis demonstrated that
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Koppen, Mirko, Florian Bonn, Sarah Ehses, and Thomas Langer. "Autocatalytic Processing of m-AAA Protease Subunits in Mitochondria." Molecular Biology of the Cell 20, no. 19 (2009): 4216–24. http://dx.doi.org/10.1091/mbc.e09-03-0218.

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m-AAA proteases are ATP-dependent proteolytic machines in the inner membrane of mitochondria which are crucial for the maintenance of mitochondrial activities. Conserved nuclear-encoded subunits, termed paraplegin, Afg3l1, and Afg3l2, form various isoenzymes differing in their subunit composition in mammalian mitochondria. Mutations in different m-AAA protease subunits are associated with distinct neuronal disorders in human. However, the biogenesis of m-AAA protease complexes or of individual subunits is only poorly understood. Here, we have examined the processing of nuclear-encoded m-AAA pr
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Sannes, P. L., B. H. Schofield, and D. F. McDonald. "Histochemical localization of cathepsin B, dipeptidyl peptidase I, and dipeptidyl peptidase II in rat bone." Journal of Histochemistry & Cytochemistry 34, no. 8 (1986): 983–88. http://dx.doi.org/10.1177/34.8.3016074.

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The histochemical distribution of the thiol proteases cathepsin B and dipeptidyl peptidase I and the serine protease dipeptidyl peptidase II was examined in rat bone and joint using amino acid derivatives of 4-methoxy-2-naphthylamine (MNA). The liberated MNA was then visualized by simultaneous coupling with fast blue B. Cathepsin B was examined with CBZ-Arg-Arg-MNA, dipeptidyl peptidase I (DPP I) with Gly-Arg- or Pro-Arg-MNA, and dipeptidyl peptidase II (DPP II) with Lys-ALA- or Lys-Pro-MNA. Bright red reaction product indicative of proteolytic activity was observed in most cell types associat
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Wilson, Claire H., Hui Emma Zhang, Mark D. Gorrell, and Catherine A. Abbott. "Dipeptidyl peptidase 9 substrates and their discovery: current progress and the application of mass spectrometry-based approaches." Biological Chemistry 397, no. 9 (2016): 837–56. http://dx.doi.org/10.1515/hsz-2016-0174.

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Abstract The enzyme members of the dipeptidyl peptidase 4 (DPP4) gene family have the very unusual capacity to cleave the post-proline bond to release dipeptides from the N-terminus of peptide/protein substrates. DPP4 and related enzymes are current and potential therapeutic targets in the treatment of type II diabetes, inflammatory conditions and cancer. Despite this, the precise biological function of individual dipeptidyl peptidases (DPPs), other than DPP4, and knowledge of their in vivo substrates remains largely unknown. For many years, identification of physiological DPP substrates has b
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34

Brüning, Mareke, Martina Lummer, Caterina Bentele, Marcel M. W. Smolenaars, Kees W. Rodenburg, and Hermann Ragg. "The Spn4 gene from Drosophila melanogaster is a multipurpose defence tool directed against proteases from three different peptidase families." Biochemical Journal 401, no. 1 (2006): 325–31. http://dx.doi.org/10.1042/bj20060648.

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By alternative use of four RSL (reactive site loop) coding exon cassettes, the serpin (serine protease inhibitor) gene Spn4 from Drosophila melanogaster was proposed to enable the synthesis of multiple protease inhibitor isoforms, one of which has been shown to be a potent inhibitor of human furin. Here, we have investigated the inhibitory spectrum of all Spn4 RSL variants. The analyses indicate that the Spn4 gene encodes inhibitors that may inhibit serine proteases of the subtilase family (S8), the chymotrypsin family (S1), and the papain-like cysteine protease family (C1), most of them at hi
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35

Oriano, Martina, Francesco Amati, Andrea Gramegna, et al. "Protease–Antiprotease Imbalance in Bronchiectasis." International Journal of Molecular Sciences 22, no. 11 (2021): 5996. http://dx.doi.org/10.3390/ijms22115996.

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Airway inflammation plays a central role in bronchiectasis. Protease–antiprotease balance is crucial in bronchiectasis pathophysiology and increased presence of unopposed proteases activity may contribute to bronchiectasis onset and progression. Proteases’ over-reactivity and antiprotease deficiency may have a role in increasing inflammation in bronchiectasis airways and may lead to extracellular matrix degradation and tissue damage. Imbalances in serine proteases and matrix-metallo proteinases (MMPs) have been associated to bronchiectasis. Active neutrophil elastase has been associated with d
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36

De Toni, C. H., M. F. Richter, J. R. Chagas, J. AP Henriques, and C. Termignoni. "Purification and characterization of an alkaline serine endopeptidase from a feather-degradingXanthomonas maltophiliastrain." Canadian Journal of Microbiology 48, no. 4 (2002): 342–48. http://dx.doi.org/10.1139/w02-027.

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A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis. This enzyme has a molecular mass of 36 kDa, an optimum pH of 9.0, and an optimum temperature of 60°C. The inhibitory profile using protease inhibitors shows that this enzyme is a serine endopeptidase. Besides keratin, the enzyme is active upon the substrates azokeratin,
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37

Hedger, Mark P., and Michael D. Culler. "Comparison of LHRH-peptidase and plasminogen activator activity in rat testis extracts." Reproduction, Fertility and Development 9, no. 7 (1997): 659. http://dx.doi.org/10.1071/r97062.

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Testicular LHRH-peptidase and testicular urokinase-type plasminogen activator are Sertoli cell-secreted proteases which display similar molecular properties. However, there is relatively little information regarding the substrate specificity and potential cross-reactivity of these enzymes. Testicular extracts were prepared from homogenates of whole rat testes and assessed by LHRH-peptidase assay, and by radial caseinolysis assays for plasminogen activator and plasmin-like activity. Following partial purification of the protease activities in testicular extracts by gel filtration and ion-exchan
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38

Kudzhaev, A. M., A. G. Andrianova, E. S. Dubovtseva, O. V. Serova та T. V. Rotanova. "Role of the Inserted α-Helical Domain in E. coli ATP-Dependent Lon Protease Function". Acta Naturae 9, № 2 (2017): 75–81. http://dx.doi.org/10.32607/20758251-2017-9-2-75-81.

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Multidomain ATP-dependent Lon protease of E. coli (Ec-Lon) is one of the key enzymes of the quality control system of the cellular proteome. A recombinant form of Ec-Lon with deletion of the inserted characteristic -helical HI(CC) domain (Lon-dHI(CC)) has been prepared and investigated to understand the role of this domain. A comparative study of the ATPase, proteolytic, and peptidase activities of the intact Lon protease and Lon-dHI(CC) has been carried out. The ability of the enzymes to undergo autolysis and their ability to bind DNA have been studied as well. It has been shown that the HI(C
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39

Swatek, Anita, and Magdalena Staszczak. "Effect of Ferulic Acid, a Phenolic Inducer of Fungal Laccase, on 26S Proteasome Activities In Vitro." International Journal of Molecular Sciences 21, no. 7 (2020): 2463. http://dx.doi.org/10.3390/ijms21072463.

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The 26S proteasome is an ATP-dependent protease complex (2.5 MDa) that degrades most cellular proteins in Eukaryotes, typically those modified by a polyubiquitin chain. The proteasome-mediated proteolysis regulates a variety of critical cellular processes such as transcriptional control, cell cycle, oncogenesis, apoptosis, protein quality control, and stress response. Previous studies conducted in our laboratory have shown that 26S proteasomes are involved in the regulation of ligninolytic enzymes (such as laccase) in white-rot fungi in response to nutrient starvation, cadmium exposure, and ER
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40

Magnen, Mélia, Brigitta Margit Elsässer, Olga Zbodakova, et al. "Kallikrein-related peptidase 5 and seasonal influenza viruses, limitations of the experimental models for activating proteases." Biological Chemistry 399, no. 9 (2018): 1053–64. http://dx.doi.org/10.1515/hsz-2017-0340.

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Abstract Every year, influenza A virus (IAV) affects and kills many people worldwide. The viral hemagglutinin (HA) is a critical actor in influenza virus infectivity which needs to be cleaved by host serine proteases to exert its activity. KLK5 has been identified as an activating protease in humans with a preference for the H3N2 IAV subtype. We investigated the origin of this preference using influenza A/Puerto Rico/8/34 (PR8, H1N1) and A/Scotland/20/74 (Scotland, H3N2) viruses. Pretreatment of noninfectious virions with human KLK5 increased infectivity of Scotland IAV in MDCK cells and trigg
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Levesque, Jean-Pierre, Fulu Liu, Paul J. Simmons, et al. "Characterization of hematopoietic progenitor mobilization in protease-deficient mice." Blood 104, no. 1 (2004): 65–72. http://dx.doi.org/10.1182/blood-2003-05-1589.

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Abstract Recent evidence suggests that protease release by neutrophils in the bone marrow may contribute to hematopoietic progenitor cell (HPC) mobilization. Matrix metalloproteinase-9 (MMP-9), neutrophil elastase (NE), and cathepsin G (CG) accumulate in the bone marrow during granulocyte colony-stimulating factor (G-CSF) treatment, where they are thought to degrade key substrates including vascular cell adhesion molecule-1 (VCAM-1) and CXCL12. To test this hypothesis, HPC mobilization was characterized in transgenic mice deficient in one or more hematopoietic proteases. Surprisingly, HPC mobi
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42

Gonçalves, Rayane Natshe, Suellen Duarte Gozzini Barbosa, and Raquel Elisa da Silva-López. "Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology." Biotechnology Research International 2016 (August 17, 2016): 1–11. http://dx.doi.org/10.1155/2016/3427098.

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Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts exhibited peaks of activity at various pH values, suggesting the presence of distinctive classes of proteases. N-α-Tosyl-L-arginine methyl ester hydrolysis was maximal at 30°C to 60°C and peptidase activity from all extracts presented very good thermal stability after 24 h incubation at 70°C. C. en
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43

Wiederanders, Bernd. "Structure-function relationships in class CA1 cysteine peptidase propeptides." Acta Biochimica Polonica 50, no. 3 (2003): 691–713. http://dx.doi.org/10.18388/abp.2003_3661.

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Regulation of proteolytic enzyme activity is an essential requirement for cells and tissues because proteolysis at a wrong time and location may be lethal. Proteases are synthesized as inactive or less active precursor molecules in order to prevent such inappropriate proteolysis. They are activated by limited intra- or intermolecular proteolysis cleaving off an inhibitory peptide. These regulatory proenzyme regions have attracted much attention during the last decade, since it became obvious that they harbour much more information than just triggering activation. In this review we summarize th
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44

Madhu, Swati N., Savitri Sharma, and Devarshi U. Gajjar. "Identification of Proteases: Carboxypeptidase and Aminopeptidase as Putative Virulence Factors of Fusarium solani Species Complex." Open Microbiology Journal 14, no. 1 (2020): 266–77. http://dx.doi.org/10.2174/1874434602014010266.

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Background: Fusarium keratitis accounts for around 50% of mycotic keratitis cases. Major virulence factors produced by keratopathogenic fungi are proteases. Objective: The aim of the current study was to identify proteases contributing to corneal pathogenicity of Fusarium species. Methods: Culture filtrates from fourteen Fusarium solani species complex (FSSC) isolates and three F. delphinoides isolates were evaluated for protease activity and gelatine zymography. Mass spectroscopy was carried out using a partially purified enzyme and total extracellular extract. Protease gene expression in an
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45

Banbula, Agnieszka, Marcin Bugno, Jason Goldstein, et al. "Emerging Family of Proline-Specific Peptidases ofPorphyromonas gingivalis: Purification and Characterization of Serine Dipeptidyl Peptidase, a Structural and Functional Homologue of Mammalian Prolyl Dipeptidyl Peptidase IV." Infection and Immunity 68, no. 3 (2000): 1176–82. http://dx.doi.org/10.1128/iai.68.3.1176-1182.2000.

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ABSTRACT Porphyromonas gingivalis is an asaccharolytic and anaerobic bacterium that possesses a complex proteolytic system which is essential for its growth and evasion of host defense mechanisms. In this report, we show the purification and characterization of prolyl dipeptidyl peptidase IV (DPPIV) produced by this organism. The enzyme was purified to homogeneity, and its enzymatic activity and biochemical properties were investigated. P. gingivalis DPPIV, like its human counterpart, is able to cleave the N terminus of synthetic oligopeptides with sequences analogous to those of interleukins
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46

Fukasawa, Kayoko M., Toshiyuki Hata, Yukio Ono, and Junzo Hirose. "Metal Preferences of Zinc-Binding Motif on Metalloproteases." Journal of Amino Acids 2011 (May 11, 2011): 1–7. http://dx.doi.org/10.4061/2011/574816.

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Almost all naturally occurring metalloproteases are monozinc enzymes. The zinc in any number of zinc metalloproteases has been substituted by some other divalent cation. Almost all Co(II)- or Mn(II)-substituted enzymes maintain the catalytic activity of their zinc counterparts. However, in the case of Cu(II) substitution of zinc proteases, a great number of enzymes are not active, for example, thermolysin, carboxypeptidase A, endopeptidase from Lactococcus lactis, or aminopeptidase B, while some do have catalytic activity, for example, astacin (37%) and DPP III (100%). Based on structural stud
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47

Su, Q., and A. Boschetti. "Substrate- and species-specific processing enzymes for chloroplast precursor proteins." Biochemical Journal 300, no. 3 (1994): 787–92. http://dx.doi.org/10.1042/bj3000787.

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Using different precursors of chloroplast proteins and stromal extracts from both Chlamydomonas reinhardii and pea chloroplasts, we analysed the specificity of stroma-localized processing peptidases. By gel filtration of a stromal extract from isolated Chlamydomonas chloroplasts, fractions could be separated containing enzymic activities for processing the precursors of the small subunit of ribulose-1,5-bisphosphate carboxylase (pSS) and of the protein OEE1 from the photosynthetic water-splitting complex (pOEE1). The enzymes differed not only in molecular size, but also in their sensitivity to
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48

Mølgaard, Anne, Jose Arnau, Conni Lauritzen, Sine Larsen, Gitte Petersen, and John Pedersen. "The crystal structure of human dipeptidyl peptidase I (cathepsin C) in complex with the inhibitor Gly-Phe-CHN2." Biochemical Journal 401, no. 3 (2007): 645–50. http://dx.doi.org/10.1042/bj20061389.

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hDDPI (human dipeptidyl peptidase I) is a lysosomal cysteine protease involved in zymogen activation of granule-associated proteases, including granzymes A and B from cytotoxic T-lymphocytes and natural killer cells, cathepsin G and neutrophil elastase, and mast cell tryptase and chymase. In the present paper, we provide the first crystal structure of an hDPPI–inhibitor complex. The inhibitor Gly-Phe-CHN2 (Gly-Phe-diazomethane) was co-crystallized with hDPPI and the structure was determined at 2.0 Å (1 Å=0.1 nm) resolution. The structure of the native enzyme was also determined to 2.05 Å resol
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49

Chukhontseva, Ksenia N., Vadim V. Salnikov, Oleg S. Morenkov, Sergey V. Kostrov, and Ilya V. Demidyuk. "Protealysin is not Secreted Constitutively." Protein & Peptide Letters 26, no. 3 (2019): 221–26. http://dx.doi.org/10.2174/0929866526666181212114907.

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Background:Protealysin, a zinc metalloprotease of Serratia proteamaculans, is the prototype of a new group within the peptidase family M4. Protealysin-like proteases (PLPs) are widely spread in bacteria but are also found in fungi and archaea. The biological functions of PLPs have not been well studied, but published data showed the involvement of enzymes of this group in the interaction of bacteria with higher organisms, and most likely in the pathogenesis. Such functionality requires the release of the proteases from bacterial cells; however, the data on the cellular localization of PLPs are
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50

Ting, Yi Tian, Paul W. R. Harris, Gaelle Batot, Margaret A. Brimble, Edward N. Baker, and Paul G. Young. "Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization." IUCrJ 3, no. 1 (2016): 10–19. http://dx.doi.org/10.1107/s2052252515019971.

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Bacterial type I signal peptidases (SPases) are membrane-anchored serine proteases that process the signal peptides of proteins exported via the Sec and Tat secretion systems. Despite their crucial importance for bacterial virulence and their attractiveness as drug targets, only one such enzyme, LepB from Escherichia coli, has been structurally characterized, and the transient nature of peptide binding has stymied attempts to directly visualize SPase–substrate complexes. Here, the crystal structure of SpsB, the type I signal peptidase from the Gram-positive pathogen Staphylococcus aureus, is r
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