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Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Proteases enzymes, commonly known as biological catalysts, are responsible for a wide range of biochemical processes. They’ve been used in a variety of fields, especially therapeutics. The properties of molecules produced from the marine differ from those of their terrestrial counterparts. Marine microbes (epibionts and endosymbionts), which are abundant in unique environments, produce a plethora of medically and industrially essential molecules. These microbes secrete enzymes with specific characteristics like pH, metal, heat and cryo-tolerance and so on. Proteases are enzymes that break down lengthy chains of proteins into smaller fragments. Endopeptidases and exopeptidases are the two large families of proteases depending on their method of action. Exopeptidases degrade terminal amino acid positions attached to polypeptide chains, while endopeptidases catalyze the breakdown of peptide bonds in the middle portion of polypeptide chains. A further way of classifying proteases is by their optimum pH, which might be neutral, acidic, or alkaline. In terms of the active centers involved, enzymes can be classed as cysteine proteases, metalloproteases, serine proteases and aspartyl proteases.
Biodiscovery of Marine Microbial Enzymes in Indonesia
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Ekowati Chasanah, Pujo Yuwono, Dewi Seswita Zilda, Siswa Setyahadi
Proteases are categorized as hydrolases, enzymes of class 3, subclass 3.4, peptide hydrolases or peptidase according to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (Mamo & Assefa, 2018). They can be grouped as exopeptidases and endopeptidases; exopeptidase hydrolyzes the peptide bond proximal to the amino or carboxy terminal of the substrate, whereas endopeptidases cut the peptide bonds from the termini of the substrate. Based on the catalysis mechanism, that is, the hydrolysis of amide bonds in peptide substrates, proteases are classified as serine proteinases (EC 3.4.21), cysteine proteinases (EC 3.4.22), aspartyl proteinases (EC3.4.23), metalloproteinases (EC 3.4.24) and threonine peptidases (EC 3.4.25) (Kieliszek, Pobiega, Piwowarek, & Kot, 2021).
Soybean-Based Functional Foods Through Microbial Fermentation: Processing and Biological Activities
Published in Megh R. Goyal, Arijit Nath, Rasul Hafiz Ansar Suleria, Plant-Based Functional Foods and Phytochemicals, 2021
Arijit Nath, Titas Ghosh, Abinit Saha, Klára Pásztorné Huszár, Szilvia Bánvölgyi, Renáta Gerencsérné Berta, Ildikó Galambos, Edit Márki, Gyula Vatai, Andras Koris, Arpita Das
In Figure 1.2, metabolic pathway in microbes for soybean protein fermentation is presented. Arrays of intracellular and extracellular biochemical reactions promote microbial fermentation process and synthesis of bioactive peptides. Both exopeptidase and endopeptidase are responsible for soybean protein hydrolysis. When exopeptidase breaks the soybean proteins or polypeptides in a random basis, then there is a production of more free amino acids. And endopeptidase cleaves the particular or specific amino acid in peptide chain and produces small peptides [13, 20, 28, 44, 118]. Smaller peptides can be uptaken by microbes and free amino acids are produced by intracellular hydrolysis. Amino acids are capable to enter from abiotic phase to biotic phase through membrane protein transporters [10, 74, 98].
Saliva proteomic profile of early childhood caries and caries-free children
Published in Acta Odontologica Scandinavica, 2023
Bethania Paludo Oliveira, Marília Afonso Rabelo Buzalaf, Natália Caldeira Silva, Talita Mendes Oliveira Ventura, Júlia Toniolo, Jonas Almeida Rodrigues
Cystatin-S, Cystatin-SN, Cystatin-SA and Cystatin-B (2-fold increase) were up-regulated in the CF group. Cystatin-S and Cystatin-SN were also correlated with the absence of caries in previous studies of saliva [4], as well as Lipocalin-1, which was also up-regulated in the CF group. Cystatin-S, Cystatin-SN and Lipocalin-1 may indirectly provide tooth protection by inhibiting proteolytic events on other salivary proteins. Additionally, Cystatin-B is an intracellular thiol proteinase inhibitor and has cysteine-type endopeptidase inhibitor activity [22]. Interestingly, the results of a functional analysis of the most affected processes in the molecular function, when comparing the CF vs ECC groups, showed that 21.9% was involved in cysteine-type endopeptidase inhibitor activity (Figure 4).
Subcutaneous catabolism of peptide therapeutics: bioanalytical approaches and ADME considerations
Published in Xenobiotica, 2022
Simone Esposito, Laura Orsatti, Vincenzo Pucci
The most relevant biotransformation occurring at the SC injection site is the cleavage of peptide bonds by means of proteases or peptidases, which generates smaller peptides or amino acids. This type of biotransformation is referred to as catabolism, in contrast to the term metabolism used for biotransformation mainly observed in small molecules. Proteolytic enzymes are broadly divided into two categories: exopeptidases, which catalyse the cleavage at the N-terminal or C-terminal removing a single amino acid, and endopeptidases, which cleave peptide bonds within the sequence (López-Otín and Bond 2008). Exopeptidases are intuitively divided into aminopeptidases and carboxypeptidases, while endopeptidases are traditionally classified on the basis of their catalytic site as cysteine peptidases (e.g. dipeptidyl peptidase IV), aspartic peptidases (e.g. pepsin), serine peptidases (e.g. cathepsin B), and metallopeptidases (e.g. matrix metalloprotease 2 and 9) (de Veer et al. 2014a).
Bacteriophage endolysins as a potential weapon to combat Clostridioides difficile infection
Published in Gut Microbes, 2020
Shakhinur Islam Mondal, Lorraine A. Draper, R Paul Ross, Colin Hill
PG structure is highly conserved and consists of a polysaccharide of alternating N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues, linked by a β1-4 glycosidic bond (Figure 2). The D-lactoyl group of each MurNAc is linked with a short peptide stem, which is different between bacterial species.69 The tetrapeptide stem found in C. difficile is L-Ala-D-Glu-A2pm-D-Ala (A2pm: 2,6-diaminopimelic acid).70 Endolysins can recognize and digest a specific chemical bond within PG and are classified accordingly: (i) N-acetylmuramoyl-L-alanine amidases cleave the amide bond between N-acetylmuramoyl residues and L-alanine (the first amino acid of the peptide stem), (ii) L-alanoyl-D-glutamate endopeptidases target the bond between L-alanine and D-glutamate, (iii) interpeptide bridge endopeptidases digest the cross-link between peptide stems, (iv) D-glutamyl-m-DAP endopeptidase target bonds between D-glutamate and m-diaminopimelic acid, (v) N-acetyl-D-glucosaminidases hydrolyze the N-acetylglucosaminyl-β-1,4-N-acetylmuramine bond, (vi) N-acetyl-D-muramidases and lytic transglycosylases cleave the N-acetylmuramoyl−1,4-N-acetylglucosamine bond.