Topic
Proteolytic enzymes
About: Proteolytic enzymes is a research topic. Over the lifetime, 23096 publications have been published within this topic receiving 835544 citations.
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01 Jan 1998
TL;DR: In this paper, Serine Peptidases with a Ser/Lys Catalytic Dyad (SC) are described, as well as their relation to the Nodavirus Coat Protein.
Abstract: (Abbreviated Contents Including Section Headings:) Serine Peptidases. Serine Peptidases and Their Clans. Family S1 of Trypsin (Clan SA). Tissue Kallikrein and Its Relatives. Other Families of Clan SA. Clan SB Containing the Subtilisin Family. Clan SC Containing Peptidases with the Alpha/Beta Hydrolase Fold. Clan SE Containing Serine-Type D-Ala-D-Ala Peptidases. Clan SF Containing Peptidases with a Ser/Lys Catalytic Dyad. Clan SH Containing Herpesvirus Assemblins. Clan TA Containing N-Terminal Nucleophile Peptidases. Other Families of Serine Peptidases. Unsequenced Serine Peptidases. Cysteine Peptidases. Cysteine Peptidases and Their Clans. Clan CA Containing Papain and Its Relatives. Clan CC Containing Viral 'Papain Like' Cysteine Endopeptidases. Clan CB Containing the Nodavirus Coat Protein. Other Families of Aspartic Endopeptidases. Metallopeptidases. Metallopeptidases and Their Clans. Clan MA Containing Thermolysin and Its Relatives. Family M1 of Membrane Alanyl Aminopeptidase. Other Families of Clan MA. Family M3 of Thimet Oligopeptidase. Clan MB Containing 'Metzincins' (Clan MB). Family M10 of Interstitial Collagenase (Clan MB). Family M12 of Astacin (Clan MB). Introduction to the Reprolysins (Family M12). Clan MC Containing the Metallocarboxypeptidases. Clan MD Containing Zinc D-Ala-D-Ala-Carboxypeptidase. Clan ME Containing Pitrilysin and Its Relatives. Clan MF Containing Co-Catalytic Leucyl Amino-Peptidases. Clan MG Containing the Methionyl Aminopeptidase Family. Clan MH Containing Varied Co-Catalytic Metallopeptidases. Other Families of Metallopeptidases. Metallopeptidases of Unknown Sequence. Unclassified Peptidases. Peptidases of Unknown Catalytic Type. Subject Index.
2,315 citations
TL;DR: Protein Analysis Through Evolutionary Relationships is a resource for the evolutionary and functional classification of genes from organisms across the tree of life, and an entirely new PANTHER GO-slim is developed, containing over four times as many Gene Ontology terms as the previous GO- slim.
Abstract: PANTHER (Protein Analysis Through Evolutionary Relationships, http://pantherdb.org) is a resource for the evolutionary and functional classification of genes from organisms across the tree of life. We report the improvements we have made to the resource during the past two years. For evolutionary classifications, we have added more prokaryotic and plant genomes to the phylogenetic gene trees, expanding the representation of gene evolution in these lineages. We have refined many protein family boundaries, and have aligned PANTHER with the MEROPS resource for protease and protease inhibitor families. For functional classifications, we have developed an entirely new PANTHER GO-slim, containing over four times as many Gene Ontology terms as our previous GO-slim, as well as curated associations of genes to these terms. Lastly, we have made substantial improvements to the enrichment analysis tools available on the PANTHER website: users can now analyze over 900 different genomes, using updated statistical tests with false discovery rate corrections for multiple testing. The overrepresentation test is also available as a web service, for easy addition to third-party sites.
2,162 citations
TL;DR: Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes and deciphering these secrets would enable to exploit proteases for their applications in biotechnology.
Abstract: Proteases represent the class of enzymes which occupy a pivotal position with respect to their physiological roles as well as their commercial applications. They perform both degradative and synthetic functions. Since they are physiologically necessary for living organisms, proteases occur ubiquitously in a wide diversity of sources such as plants, animals, and microorganisms. Microbes are an attractive source of proteases owing to the limited space required for their cultivation and their ready susceptibility to genetic manipulation. Proteases are divided into exo- and endopeptidases based on their action at or away from the termini, respectively. They are also classified as serine proteases, aspartic proteases, cysteine proteases, and metalloproteases depending on the nature of the functional group at the active site. Proteases play a critical role in many physiological and pathophysiological processes. Based on their classification, four different types of catalytic mechanisms are operative. Proteases find extensive applications in the food and dairy industries. Alkaline proteases hold a great potential for application in the detergent and leather industries due to the increasing trend to develop environmentally friendly technologies. There is a renaissance of interest in using proteolytic enzymes as targets for developing therapeutic agents. Protease genes from several bacteria, fungi, and viruses have been cloned and sequenced with the prime aims of (i) overproduction of the enzyme by gene amplification, (ii) delineation of the role of the enzyme in pathogenecity, and (iii) alteration in enzyme properties to suit its commercial application. Protein engineering techniques have been exploited to obtain proteases which show unique specificity and/or enhanced stability at high temperature or pH or in the presence of detergents and to understand the structure-function relationships of the enzyme. Protein sequences of acidic, alkaline, and neutral proteases from diverse origins have been analyzed with the aim of studying their evolutionary relationships. Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes. Deciphering these secrets would enable us to exploit proteases for their applications in biotechnology.
2,159 citations
01 Jan 1998
TL;DR: (Abbreviated Contents Including Section Headings:)
Abstract: (Abbreviated Contents Including Section Headings:) Serine Peptidases. Serine Peptidases and Their Clans. Family S1 of Trypsin (Clan SA). Tissue Kallikrein and Its Relatives. Other Families of Clan SA. Clan SB Containing the Subtilisin Family. Clan SC Containing Peptidases with the Alpha/Beta Hydrolase Fold. Clan SE Containing Serine-Type D-Ala-D-Ala Peptidases. Clan SF Containing Peptidases with a Ser/Lys Catalytic Dyad. Clan SH Containing Herpesvirus Assemblins. Clan TA Containing N-Terminal Nucleophile Peptidases. Other Families of Serine Peptidases. Unsequenced Serine Peptidases. Cysteine Peptidases. Cysteine Peptidases and Their Clans. Clan CA Containing Papain and Its Relatives. Clan CC Containing Viral 'Papain Like' Cysteine Endopeptidases. Clan CB Containing the Nodavirus Coat Protein. Other Families of Aspartic Endopeptidases. Metallopeptidases. Metallopeptidases and Their Clans. Clan MA Containing Thermolysin and Its Relatives. Family M1 of Membrane Alanyl Aminopeptidase. Other Families of Clan MA. Family M3 of Thimet Oligopeptidase. Clan MB Containing 'Metzincins' (Clan MB). Family M10 of Interstitial Collagenase (Clan MB). Family M12 of Astacin (Clan MB). Introduction to the Reprolysins (Family M12). Clan MC Containing the Metallocarboxypeptidases. Clan MD Containing Zinc D-Ala-D-Ala-Carboxypeptidase. Clan ME Containing Pitrilysin and Its Relatives. Clan MF Containing Co-Catalytic Leucyl Amino-Peptidases. Clan MG Containing the Methionyl Aminopeptidase Family. Clan MH Containing Varied Co-Catalytic Metallopeptidases. Other Families of Metallopeptidases. Metallopeptidases of Unknown Sequence. Unclassified Peptidases. Peptidases of Unknown Catalytic Type. Subject Index.
1,969 citations
TL;DR: This review summarizes the current understanding of the cellular and molecular mechanisms regulating the inflammatory response following myocardial ischemia and reperfusion and concludes that by promoting more effective tissue repair, it may be possible to reduce the deleterious remodeling.
Abstract: One of the major therapeutic goals of modern cardiology is to design strategies aimed at minimizing myocardial necrosis and optimizing cardiac repair following myocardial infarction. However, a sound understanding of the biology is necessary before a specific intervention is pursued on a therapeutic basis. This review summarizes our current understanding of the cellular and molecular mechanisms regulating the inflammatory response following myocardial ischemia and reperfusion. Myocardial necrosis induces complement activation and free radical generation, triggering a cytokine cascade initiated by Tumor Necrosis Factor (TNF)-α release. If reperfusion of the infarcted area is initiated, it is attended by an intense inflammatory reaction. Interleukin (IL)-8 synthesis and C5a activation have a crucial role in recruiting neutrophils in the ischemic and reperfused myocardium. Neutrophil infiltration is regulated through a complex sequence of molecular steps involving the selectins and the integrins, which mediate leukocyte rolling and adhesion to the endothelium. Marginated neutrophils exert potent cytotoxic effects through the release of proteolytic enzymes and the adhesion with Intercellular Adhesion Molecule (ICAM)-1 expressing cardiomyocytes. Despite this potential injury, substantial evidence suggests that reperfusion enhances cardiac repair improving patient survival; this effect may be in part related to the inflammatory response. Monocyte Chemoattractant Protein (MCP)-1 is also markedly upregulated in the infarcted myocardium inducing recruitment of mononuclear cells in the injured areas. Monocyte-derived macrophages and mast cells may produce cytokines and growth factors necessary for fibroblast proliferation and neovascularization, leading to effective repair and scar formation. At this stage expression of inhibitory cytokines such as IL-10 may have a role in suppressing the acute inflammatory response and in regulating extracellular matrix metabolism. Fibroblasts in the healing scar undergo phenotypic changes expressing smooth muscle cell markers. Our previous review in this journal focused almost exclusively on reduction of the inflammatory injury. The current update is prompted by the potential therapeutic opportunity that the open vessel offers. By promoting more effective tissue repair, it may be possible to reduce the deleterious remodeling, that is the leading cause of heart failure and death. Elucidating the complex interactions and regulatory mechanisms responsible for cardiac repair may allow us to design effective inflammation-related interventions for the treatment of myocardial infarction.
1,966 citations