Array ( [0] => {{short description|Enzyme that cleaves other proteins into smaller peptides}} [1] => [[File:TEV protease summary.png|thumb|250px|[[Ribbon diagram]] of a protease ([[TEV protease]]) complexed with its peptide substrate in black with catalytic residues in red.({{PDB|1LVB}})]] [2] => A '''protease''' (also called a '''peptidase''', '''proteinase''', or '''proteolytic enzyme'''){{cite web | url=https://www.britannica.com/science/proteolytic-enzyme | title=Proteolytic enzyme | Description, Types, & Functions | Britannica }} is an [[enzyme]] that [[catalysis|catalyzes]] [[proteolysis]], breaking down [[proteins]] into smaller [[polypeptide]]s or single [[amino acid]]s, and spurring the formation of new protein products.{{cite journal | vauthors = López-Otín C, Bond JS | title = Proteases: multifunctional enzymes in life and disease | journal = The Journal of Biological Chemistry | volume = 283 | issue = 45 | pages = 30433–30437 | date = November 2008 | pmid = 18650443 | pmc = 2576539 | doi = 10.1074/jbc.R800035200 | doi-access = free }} They do this by cleaving the [[peptide bonds]] within proteins by [[hydrolysis]], a reaction where [[water]] breaks [[Covalent bond|bonds]]. Proteases are involved in numerous biological pathways, including [[Digestion#Protein digestion|digestion]] of ingested proteins, [[protein catabolism]] (breakdown of old proteins),{{cite journal | vauthors = King JV, Liang WG, Scherpelz KP, Schilling AB, Meredith SC, Tang WJ | title = Molecular basis of substrate recognition and degradation by human presequence protease | journal = Structure | volume = 22 | issue = 7 | pages = 996–1007 | date = July 2014 | pmid = 24931469 | pmc = 4128088 | doi = 10.1016/j.str.2014.05.003 }}{{cite journal | vauthors = Shen Y, Joachimiak A, Rosner MR, Tang WJ | title = Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism | journal = Nature | volume = 443 | issue = 7113 | pages = 870–874 | date = October 2006 | pmid = 17051221 | pmc = 3366509 | doi = 10.1038/nature05143 | bibcode = 2006Natur.443..870S }} and [[cell signaling]]. [3] => [4] => In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of [[year]]s.{{cite journal | vauthors = Radzicka A, Wolfenden R | title = Rates of Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases | journal = Journal of the American Chemical Society | volume = 118 | issue = 26 | pages = 6105–6109 | date = July 1996 | doi = 10.1021/ja954077c | quote = To assess the relative proficiencies of enzymes that catalyze the hydrolysis of internal and C-terminal peptide bonds [...]}} Proteases can be found in all forms of life and [[virus]]es. They have independently [[convergent evolution|evolved multiple times]], and different classes of protease can perform the same reaction by completely different [[catalytic mechanism]]s. [5] => [6] => ==Classification== [7] => [8] => ===Based on catalytic residue=== [9] => Proteases can be classified into seven broad groups:{{cite journal | vauthors = Oda K | title = New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases | journal = Journal of Biochemistry | volume = 151 | issue = 1 | pages = 13–25 | date = January 2012 | pmid = 22016395 | doi = 10.1093/jb/mvr129 | name-list-style = vanc | doi-access = free }} [10] => * [[Serine protease]]s - using a [[serine]] [[Alcohol (chemistry)|alcohol]] [11] => * [[Cysteine protease]]s - using a [[cysteine]] [[thiol]] [12] => * [[Threonine protease]]s - using a [[threonine]] [[secondary alcohol]] [13] => * [[Aspartic protease]]s - using an [[Aspartic acid|aspartate]] [[carboxylic acid]] [14] => * [[Glutamic protease]]s - using a [[Glutamic acid|glutamate]] [[carboxylic acid]] [15] => * [[Metalloprotease]]s - using a [[metal]], usually [[zinc]] [16] => * [[Asparagine peptide lyases]] - using an [[asparagine]] to perform an [[elimination reaction]] (not requiring water) [17] => [18] => Proteases were first grouped into 84 families according to their evolutionary relationship in 1993, and classified under four catalytic types: [[Serine protease|serine]], [[Cysteine protease|cysteine]], [[Aspartic protease|aspartic]], and [[Metalloprotease|metallo]]proteases.{{cite journal | vauthors = Rawlings ND, Barrett AJ | title = Evolutionary families of peptidases | journal = The Biochemical Journal | volume = 290 | issue = Pt 1 | pages = 205–218 | date = February 1993 | pmid = 8439290 | pmc = 1132403 | doi = 10.1042/bj2900205 }} The [[Threonine protease|threonine]] and [[Glutamic protease|glutamic]] proteases were not described until 1995 and 2004 respectively. The mechanism used to cleave a [[peptide bond]] involves making an [[amino acid]] residue that has the cysteine and threonine (proteases) or a water molecule (aspartic, glutamic and metalloproteases) nucleophilic so that it can attack the peptide [[carbonyl]] group. One way to make a [[nucleophile]] is by a [[catalytic triad]], where a [[histidine]] residue is used to activate [[serine]], [[cysteine]], or [[threonine]] as a nucleophile. This is not an evolutionary grouping, however, as the nucleophile types have [[catalytic triad|evolved convergently]] in different [[protein superfamily|superfamilies]], and some superfamilies show divergent evolution to multiple different nucleophiles. Metalloproteases, aspartic, and glutamic proteases utilize their active site residues to activate a water molecule, which then attacks the scissile bond.{{cite journal |first1=Laura E. |last1=Sanman |title=Activity-Based Profiling of Proteases |journal=Annual Review of Biochemistry |date=June 2014 |volume=83 |pages=249–273 |doi=10.1146/annurev-biochem-060713-035352 |pmid=24905783 |url=https://doi.org/10.1146/annurev-biochem-060713-035352}} [19] => [20] => ==== Peptide lyases ==== [21] => A seventh catalytic type of proteolytic enzymes, [[asparagine peptide lyase]], was described in 2011. Its proteolytic mechanism is unusual since, rather than [[hydrolysis]], it performs an [[elimination reaction]].{{cite journal | vauthors = Rawlings ND, Barrett AJ, Bateman A | title = Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes | journal = The Journal of Biological Chemistry | volume = 286 | issue = 44 | pages = 38321–38328 | date = November 2011 | pmid = 21832066 | pmc = 3207474 | doi = 10.1074/jbc.M111.260026 | doi-access = free }} During this reaction, the catalytic [[asparagine]] forms a cyclic chemical structure that cleaves itself at asparagine residues in proteins under the right conditions. Given its fundamentally different mechanism, its inclusion as a peptidase may be debatable. [22] => [23] => ===Based on evolutionary phylogeny=== [24] => An up-to-date classification of protease evolutionary [[protein superfamily|superfamilies]] is found in the MEROPS database.{{cite journal | vauthors = Rawlings ND, Barrett AJ, Bateman A | title = MEROPS: the peptidase database | journal = Nucleic Acids Research | volume = 38 | issue = Database issue | pages = D227–D233 | date = January 2010 | pmid = 19892822 | pmc = 2808883 | doi = 10.1093/nar/gkp971 }} In this database, proteases are classified firstly by 'clan' ([[protein superfamily|superfamily]]) based on structure, mechanism and catalytic residue order (e.g. the [[PA clan]] where P indicates a mixture of nucleophile families). Within each 'clan', proteases are classified into [[protein family|families]] based on sequence similarity (e.g. the S1 and C3 families within the PA clan). Each family may contain many hundreds of related proteases (e.g. [[trypsin]], [[elastase]], [[thrombin]] and [[Streptogrisin A|streptogrisin]] within the S1 family). [25] => [26] => Currently more than 50 clans are known, each indicating an independent evolutionary origin of proteolysis. [27] => [28] => ===Based on optimal pH=== [29] => Alternatively, proteases may be classified by the optimal [[pH]] in which they are active: [30] => [31] => *''Acid proteases'' [32] => *''Neutral proteases'' involved in [[type 1 hypersensitivity]]. Here, it is released by [[mast cell]]s and causes activation of [[complement system|complement]] and [[kinins]].{{cite book | last1 = Mitchell | first1 = Richard Sheppard | last2 = Kumar | first2 = Vinay | last3 = Abbas | first3 = Abul K. | last4 = Fausto | first4 = Nelson | name-list-style = vanc |title=Robbins Basic Pathology |publisher=Saunders |location=Philadelphia |year= 2007|pages=122 |isbn=978-1-4160-2973-1 | edition = 8th }} This group includes the [[calpains]]. [33] => *''[[Basic proteases]]'' (or ''alkaline proteases'') [34] => [35] => ==Enzymatic function and mechanism== [36] => [[File:Protease mechanism summary.svg|thumb|upright=2.4|A comparison of the two [[hydrolysis|hydrolytic]] mechanisms used for [[proteolysis]]. [[Enzyme]] is shown in black, [[Substrate (biochemistry)|substrate]] protein in red and [[water]] in blue. The top panel shows 1-step [[hydrolysis]] where the enzyme uses an [[acid]] to [[Chemical polarity|polarise]] water, which then hydrolyses the substrate. The bottom panel shows 2-step hydrolysis where a residue within the enzyme is activated to act as a [[nucleophile]] (Nu) and attack the substrate. This forms an intermediate where the enzyme is covalently linked to the N-terminal half of the substrate. In a second step, water is activated to hydrolyse this intermediate and complete catalysis. Other enzyme residues (not shown) donate and accept hydrogens and electrostatically stabilise charge build-up along the reaction mechanism.]] [37] => {{see also|Catalytic triad}} [38] => Proteases are involved in [[digestion|digesting]] long protein chains into shorter fragments by splitting the [[peptide bonds]] that link [[amino acid]] residues. Some detach the terminal amino acids from the protein chain ([[exopeptidases]], such as [[aminopeptidase]]s, [[carboxypeptidase A]]); others attack internal peptide bonds of a protein ([[endopeptidases]], such as [[trypsin]], [[chymotrypsin]], [[pepsin]], [[papain]], [[elastase]]). [39] => [40] => ===Catalysis=== [41] => [[Catalysis]] is achieved by one of two mechanisms: [42] => *Aspartic, glutamic, and metallo-proteases activate a water molecule, which performs a nucleophilic attack on the peptide bond to hydrolyze it. [43] => *Serine, threonine, and cysteine proteases use a nucleophilic residue (usually in a [[catalytic triad]]). That residue performs a nucleophilic attack to [[covalent]]ly link the protease to the substrate protein, releasing the first half of the product. This covalent acyl-enzyme intermediate is then hydrolyzed by activated water to complete catalysis by releasing the second half of the product and regenerating the free enzyme [44] => [45] => ===Specificity=== [46] => Proteolysis can be highly [[enzyme promiscuity|promiscuous]] such that a wide range of protein substrates are hydrolyzed. This is the case for digestive enzymes such as [[trypsin]], which have to be able to cleave the array of proteins ingested into smaller peptide fragments. Promiscuous proteases typically bind to a single amino acid on the substrate and so only have specificity for that residue. For example, [[trypsin]] is specific for the sequences ...K\... or ...R\... ('\'=cleavage site).{{cite journal | vauthors = Rodriguez J, Gupta N, Smith RD, Pevzner PA | title = Does trypsin cut before proline? | journal = Journal of Proteome Research | volume = 7 | issue = 1 | pages = 300–305 | date = January 2008 | pmid = 18067249 | doi = 10.1021/pr0705035 }} [47] => [48] => Conversely some proteases are highly specific and only cleave substrates with a certain sequence. Blood clotting (such as [[thrombin]]) and viral polyprotein processing (such as [[TEV protease]]) requires this level of specificity in order to achieve precise cleavage events. This is achieved by proteases having a long binding cleft or tunnel with several pockets that bind to specified residues. For example, [[TEV protease]] is specific for the sequence ...ENLYFQ\S... ('\'=cleavage site).{{cite journal | vauthors = Renicke C, Spadaccini R, Taxis C | title = A tobacco etch virus protease with increased substrate tolerance at the P1' position | journal = PLOS ONE | volume = 8 | issue = 6 | pages = e67915 | date = 2013-06-24 | pmid = 23826349 | pmc = 3691164 | doi = 10.1371/journal.pone.0067915 | doi-access = free | bibcode = 2013PLoSO...867915R }} [49] => [50] => ===Degradation and autolysis=== [51] => Proteases, being themselves proteins, are cleaved by other protease molecules, sometimes of the same variety. This acts as a method of regulation of protease activity. Some proteases are less active after autolysis (e.g. [[TEV protease]]) whilst others are more active (e.g. [[trypsinogen]]). [52] => [53] => ==Biodiversity of proteases== [54] => Proteases occur in all organisms, from [[prokaryote]]s to [[eukaryote]]s to [[viruses]]. These enzymes are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades (e.g., the [[coagulation|blood-clotting [55] => cascade]], the [[complement system]], [[apoptosis]] pathways, and the invertebrate prophenoloxidase-activating cascade). Proteases can either break specific peptide bonds (''limited proteolysis''), depending on the [[amino acid]] sequence of a protein, or completely break down a peptide to amino acids (''unlimited proteolysis''). The activity can be a destructive change (abolishing a protein's function or digesting it to its principal components), it can be an activation of a function, or it can be a signal in a signalling pathway. [56] => [57] => ===Plants=== [58] => [59] => Plant genomes encode hundreds of proteases, largely of unknown function. Those with known function are largely involved in [[development (biology)|developmental]] regulation.{{cite journal | vauthors = van der Hoorn RA | title = Plant proteases: from phenotypes to molecular mechanisms | journal = Annual Review of Plant Biology | volume = 59 | pages = 191–223 | year = 2008 | pmid = 18257708 | doi = 10.1146/annurev.arplant.59.032607.092835 | hdl-access = free | hdl = 11858/00-001M-0000-0012-37C7-9 }} Plant proteases also play a role in regulation of [[photosynthesis]].{{cite journal | vauthors = Zelisko A, Jackowski G | title = Senescence-dependent degradation of Lhcb3 is mediated by a thylakoid membrane-bound protease | journal = Journal of Plant Physiology | volume = 161 | issue = 10 | pages = 1157–1170 | date = October 2004 | pmid = 15535125 | doi = 10.1016/j.jplph.2004.01.006 }} [60] => [61] => ===Animals=== [62] => Proteases are used throughout an organism for various metabolic processes. Acid proteases secreted into the stomach (such as [[pepsin]]) and serine proteases present in the [[duodenum]] ([[trypsin]] and [[chymotrypsin]]) enable us to digest the protein in food. Proteases present in blood serum ([[thrombin]], [[plasmin]], [[Hageman factor]], etc.) play an important role in blood-clotting, as well as lysis of the clots, and the correct action of the immune system. Other proteases are present in leukocytes ([[elastase]], [[cathepsin G]]) and play several different roles in metabolic control. Some [[snake venoms]] are also proteases, such as [[pit viper]] [[haemotoxin]] and interfere with the victim's blood clotting cascade. Proteases determine the lifetime of other proteins playing important physiological roles like hormones, antibodies, or other enzymes. This is one of the fastest "switching on" and "switching off" regulatory mechanisms in the physiology of an organism. [63] => [64] => By a complex cooperative action, proteases can catalyze [[biochemical cascade|cascade]] reactions, which result in rapid and efficient amplification of an organism's response to a physiological signal. [65] => [66] => ===Bacteria=== [67] => [[Bacteria]] secrete proteases to [[hydrolyse]] the peptide bonds in proteins and therefore break the proteins down into their constituent [[amino acid]]s. Bacterial and fungal proteases are particularly important to the global [[carbon]] and [[nitrogen]] cycles in the recycling of proteins, and such activity tends to be regulated by nutritional signals in these organisms.{{cite journal | vauthors = Sims GK | year = 2006 | title = Nitrogen Starvation Promotes Biodegradation of N-Heterocyclic Compounds in Soil | url = https://naldc-legacy.nal.usda.gov/naldc/download.xhtml?id=6863&content=PDF | journal = Soil Biology & Biochemistry | volume = 38 | issue = 8 | pages = 2478–2480 | doi = 10.1016/j.soilbio.2006.01.006 | access-date = 2018-12-29 | archive-date = 2021-04-28 | archive-url = https://web.archive.org/web/20210428115940/https://naldc-legacy.nal.usda.gov/naldc/download.xhtml?id=6863&content=PDF | url-status = dead }} The net impact of nutritional regulation of protease activity among the thousands of species present in soil can be observed at the overall microbial community level as proteins are broken down in response to carbon, nitrogen, or sulfur limitation.{{cite journal | vauthors = Sims GK, Wander MM | year = 2002 | title = Proteolytic activity under nitrogen or sulfur limitation | journal = Appl. Soil Ecol. | volume = 568 | issue = 3 | pages = 1–5 | doi = 10.1016/S0929-1393(01)00192-5 | bibcode = 2002AppSE..19..217S }} [68] => [69] => Bacteria contain proteases responsible for general protein quality control (e.g. the AAA+ [[proteasome]]) by degrading [[protein denaturation|unfolded or misfolded proteins]]. [70] => [71] => A secreted bacterial protease may also act as an exotoxin, and be an example of a [[virulence factor]] in bacterial [[pathogenesis]] (for example, [[Staphylococcus aureus#Toxins|exfoliative toxin]]). Bacterial exotoxic proteases destroy extracellular structures. [72] => [73] => ===Viruses=== [74] => The genomes of some [[viruses]] encode one massive [[polyprotein]], which needs a protease to cleave this into functional units (e.g. the [[hepatitis C virus]] and the [[picornavirus]]es).{{cite journal | vauthors = Tong L | title = Viral proteases | journal = Chemical Reviews | volume = 102 | issue = 12 | pages = 4609–4626 | date = December 2002 | pmid = 12475203 | doi = 10.1021/cr010184f | name-list-style = vanc }} These proteases (e.g. [[TEV protease]]) have high specificity and only cleave a very restricted set of substrate sequences. They are therefore a common target for [[Protease inhibitor (pharmacology)|protease inhibitor]]s.{{cite journal | vauthors = Skoreński M, Sieńczyk M | title = Viral proteases as targets for drug design | journal = Current Pharmaceutical Design | volume = 19 | issue = 6 | pages = 1126–1153 | date = 2013 | pmid = 23016690 | doi = 10.2174/13816128130613 }}{{cite journal | vauthors = Kurt Yilmaz N, Swanstrom R, Schiffer CA | title = Improving Viral Protease Inhibitors to Counter Drug Resistance | journal = Trends in Microbiology | volume = 24 | issue = 7 | pages = 547–557 | date = July 2016 | pmid = 27090931 | pmc = 4912444 | doi = 10.1016/j.tim.2016.03.010 }} [75] => [76] => === Archaea === [77] => [[Archaea]] use proteases to regulate various cellular processes from [[Cell signaling|cell-signaling]], [[metabolism]], [[secretion]] and protein quality control.{{cite journal | vauthors = Giménez MI, Cerletti M, De Castro RE | title = Archaeal membrane-associated proteases: insights on Haloferax volcanii and other haloarchaea | journal = Frontiers in Microbiology | volume = 6 | pages = 39 | date = 2015 | pmid = 25774151 | pmc = 4343526 | doi = 10.3389/fmicb.2015.00039 | doi-access = free }}{{cite journal | vauthors = Maupin-Furlow JA | title = Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme | journal = Emerging Topics in Life Sciences | volume = 2 | issue = 4 | pages = 561–580 | date = December 2018 | pmid = 32953999 | pmc = 7497159 | doi = 10.1042/ETLS20180025 | editor-first = Nicholas P. | editor-last = Robinson }} Only two ATP-dependent proteases are found in archaea: the membrane associated LonB protease and a soluble [[Proteasome|20S proteosome]] complex . [78] => [79] => ==Uses== [80] => {{main|Proteases (medical and related uses)}} [81] => The field of protease research is enormous. Since 2004, approximately 8000 [[Scientific paper|papers]] related to this field were published each year.{{cite book| first1 = Alan J | last1 = Barrett | first2 = Neil D | last2 = Rawlings | first3 = J Fred | last3 = Woessnerd | name-list-style = vanc |title=Handbook of proteolytic enzymes|year=2004|publisher=Elsevier Academic Press|location=London, UK|isbn=978-0-12-079610-6|edition=2nd}} Proteases are used in industry, [[medicine]] and as a basic biological research tool.{{cite book| veditors = Hooper NM |title=Proteases in biology and medicine|year=2002|publisher=Portland Press|location=London|isbn=978-1-85578-147-4}}{{cite journal|last1=Feijoo-Siota|first1=Lucía|last2=Villa | first2 = Tomás G. | name-list-style = vanc |title=Native and Biotechnologically Engineered Plant Proteases with Industrial Applications|journal=Food and Bioprocess Technology|date=28 September 2010|volume=4|issue=6|pages=1066–1088|doi=10.1007/s11947-010-0431-4|s2cid=84748291}} [82] => [83] => Digestive proteases are part of many [[laundry detergent]]s and are also used extensively in the bread industry in [[bread improver]]. A variety of proteases are used medically both for their native function (e.g. controlling blood clotting) or for completely artificial functions (''e.g.'' for the targeted degradation of pathogenic proteins). Highly specific proteases such as [[TEV protease]] and [[thrombin]] are commonly used to cleave [[fusion protein]]s and [[affinity tag]]s in a controlled fashion. [84] => Protease-containing plant-solutions called ''[[Rennet#Vegetable|vegetarian rennet]]'' have been in use for hundreds of years in [[Europe]] and the [[Middle East]] for making [[Cheese#Cultural attitudes|kosher and halal Cheeses]]. Vegetarian rennet from ''[[Withania coagulans]]'' has been in use for thousands of years as a [[Ayurveda|Ayurvedic]] remedy for digestion and diabetes in the Indian subcontinent. It is also used to make [[Paneer]]. [85] => [86] => ==Inhibitors== [87] => {{main|Protease inhibitor (biology)|Protease inhibitor (pharmacology)}} [88] => The activity of proteases is inhibited by [[protease inhibitor (biology)|protease inhibitor]]s.{{cite journal | vauthors = Southan C | title = A genomic perspective on human proteases as drug targets | journal = Drug Discovery Today | volume = 6 | issue = 13 | pages = 681–688 | date = July 2001 | pmid = 11427378 | doi = 10.1016/s1359-6446(01)01793-7 }} One example of protease inhibitors is the [[serpin]] superfamily. It includes [[alpha 1-antitrypsin]] (which protects the body from excessive effects of its own [[inflammation|inflammatory]] proteases), [[alpha 1-antichymotrypsin]] (which does likewise), [[C1-inhibitor]] (which protects the body from excessive protease-triggered activation of its own [[complement system]]), [[antithrombin]] (which protects the body from excessive [[coagulation]]), [[plasminogen activator inhibitor 1|plasminogen activator inhibitor-1]] (which protects the body from inadequate coagulation by blocking protease-triggered [[fibrinolysis]]), and [[neuroserpin]].{{cite journal | vauthors = Puente XS, López-Otín C | title = A genomic analysis of rat proteases and protease inhibitors | journal = Genome Research | volume = 14 | issue = 4 | pages = 609–622 | date = April 2004 | pmid = 15060002 | pmc = 383305 | doi = 10.1101/gr.1946304 }} [89] => [90] => Natural protease inhibitors include the family of [[lipocalin]] proteins, which play a role in cell regulation and differentiation. [[Lipophilic]] ligands, attached to lipocalin proteins, have been found to possess tumor protease inhibiting properties. The natural [[protease inhibitor (biology)|protease inhibitor]]s are not to be confused with the [[protease inhibitor (pharmacology)|protease inhibitor]]s used in antiretroviral therapy. Some [[virus (biology)|virus]]es, with [[HIV/AIDS]] among them, depend on proteases in their reproductive cycle. Thus, [[protease inhibitor (pharmacology)|protease inhibitor]]s are developed as [[Antiviral drug|antiviral]] therapeutic agents. [91] => [92] => Other natural protease inhibitors are used as defense mechanisms. Common examples are the [[trypsin inhibitor]]s found in the seeds of some plants, most notable for humans being soybeans, a major food crop, where they act to discourage predators. Raw soybeans are [[Soybean#Nutrition|toxic]] to many animals, including humans, until the protease inhibitors they contain have been denatured. [93] => [94] => == See also == [95] => {{colbegin}} [96] => * [[Ligase]] [97] => *Protease [98] => **[[cysteine protease|cysteine-]] [99] => **[[serine protease|serine-]] [100] => **[[threonine protease|threonine-]] [101] => **[[aspartic protease|aspartic-]] [102] => **[[glutamic protease|glutamic-]] [103] => **[[metalloprotease|metallo-]] [104] => * [[PA clan]] [105] => * [[Convergent evolution]] [106] => * [[Proteolysis]] [107] => * [[Catalytic triad]] [108] => * [[The Proteolysis Map]] [109] => * [[Proteases in angiogenesis]] [110] => * [[Intramembrane protease]]s [111] => * [[Protease inhibitor (pharmacology)]] [112] => * [[Protease inhibitor (biology)]] [113] => * [[TopFIND]] - database of protease specificity, substrates, products and inhibitors [114] => * [[MEROPS]] - Database of protease evolutionary groups [115] => {{colend}} [116] => [117] => == References == [118] => {{Reflist}} [119] => [120] => == External links == [121] => {{Wiktionary}} [122] => {{Library resources box [123] => |onlinebooks=no [124] => |by=no}} [125] => * [http://www.protease.org/ International Proteolysis Society] [126] => * [http://merops.sanger.ac.uk/ MEROPS - the peptidase database] {{Webarchive|url=https://web.archive.org/web/20061114180435/http://merops.sanger.ac.uk/ |date=2006-11-14 }} [127] => * [http://www.sciencegateway.org/resources/protease.htm List of protease inhibitors] [128] => * [http://www.expasy.org/tools/peptidecutter/ Protease cutting predictor] [129] => * [http://www.expasy.org/tools/peptidecutter/peptidecutter_enzymes.html List of proteases and their specificities] (see also [http://www.expasy.org/cgi-bin/lists?peptidas.txt] {{Webarchive|url=https://web.archive.org/web/20110430181829/http://expasy.org/cgi-bin/lists?peptidas.txt |date=2011-04-30 }}) [130] => * [https://web.archive.org/web/20081121051237/http://www.proteolysis.org/ Proteolysis MAP from Center for Proteolytic Pathways] [131] => * [https://web.archive.org/web/20110903233056/http://cutdb.burnham.org/ Proteolysis Cut Site database - curated expert annotation from users] [132] => * [https://web.archive.org/web/20081222011039/http://substrate.burnham.org/ Protease cut sites graphical interface] [133] => * [http://clipserve.clip.ubc.ca/topfind TopFIND protease database covering cut sites, substrates and protein termini] [134] => * {{MeshName|Proteases}} [135] => [136] => {{Proteases}} [137] => {{Enzymes}} [138] => {{Portal bar|Biology|border=no}} [139] => [140] => {{Authority control}} [141] => [142] => [[Category:Proteases| ]] [143] => [[Category:EC 3.4|*]] [144] => [[Category:Post-translational modification]] [] => )
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Protease

A protease is an enzyme that aids in the breakdown of proteins into smaller peptides or amino acids. These enzymes play crucial roles in various biological processes, including digestion, cellular signaling, and protein regulation.

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These enzymes play crucial roles in various biological processes, including digestion, cellular signaling, and protein regulation. Proteases are found in all living organisms, from bacteria to animals and plants. They are classified into different groups based on their mechanism of action, known as catalytic types. The most common types include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. Each type of protease has its specific substrates and physiological functions. Abnormalities in protease activity can lead to various diseases, such as cancer, Alzheimer's disease, and autoimmune disorders. Proteases are also important targets for the development of therapeutic drugs.

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