EC 3.4.21

Trypsin is a type of serine protease enzyme from the PA clan superfamily found in the digestive system of many vertebrates, where it begins the digestion of proteins by hydrolysis, cutting long chains of amino acids into smaller pieces. Trypsin is formed in the small intestine when its proenzyme, known as trypsinogen and produced by the pancreas, is activated. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine and arginine. It is widely used in numerous biotechnology applications in clinical and research laboratories. The enzymatic action of trypsin is commonly r

thumb|360px|alt=Schematic diagram of the blood coagulation and protein C pathways. In the blood coagulation pathway, thrombin acts to convert factor XI to XIa, VIII to VIIIa V to Va, fibrinogen to fibrin. In addition, thrombin promotes platelet activation and aggregation via activation of protease-activated receptors on the cell membrane of the platelet. Thrombin also cross over into the protein C pathway by converting protein C into APC. APC in turn converts factor V into Vi, and VIIIa into VIIIi. Finally APC activates PAR-1 and EPCR.|Role of thrombin in the blood coagulation cascade

Chymotrypsin (, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum, where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in thei

mammalian protein found in Homo sapiens

mammalian protein found in Homo sapiens

Plasmin is an important enzyme () present in blood that degrades many blood plasma proteins, including fibrin clots. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein (in the zymogen form of plasminogen) is encoded by the PLG gene.

mammalian protein found in Homo sapiens

mammalian protein found in Homo sapiens

thumb|right|Space-filling model of elastase thumb|200px|Crystals of porcine elastase

mammalian protein found in Homo sapiens

class of enzymes

Reelin, encoded by the RELN gene, is a large secreted extracellular matrix glycoprotein that helps regulate processes of neuronal migration and positioning in the developing brain by controlling cell–cell interactions. Besides this important role in early development, reelin continues to work in the adult brain. It modulates synaptic plasticity by enhancing the induction and maintenance of long-term potentiation. It also stimulates dendrite and dendritic spine development in the hippocampus, and regulates the continuing migration of neuroblasts generated in adult neurogenesis sites of the subv

mammalian protein found in Homo sapiens

Urokinase, also known as urokinase-type plasminogen activator (uPA), is a serine protease present in humans and other animals. The human urokinase protein was discovered, but not named, by McFarlane and Pilling in 1947. Urokinase was originally isolated from human urine, and it is also present in the blood and in the extracellular matrix of many tissues. The primary physiological substrate of this enzyme is plasminogen, which is an inactive form (zymogen) of the serine protease plasmin. Activation of plasmin triggers a proteolytic cascade that, depending on the physiological environment, parti

protein involved in the breakdown of blood clots

Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of digestive enzymes from the pancreas. Absence of enteropeptidase results in intestinal digestion impairment.

mammalian protein found in Homo sapiens

Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein (encoded by KLKB1 gene) has no known paralogue, while tissue kallikrein-related peptidases (KLKs) encode a family of fifteen closely related serine proteases. These genes are localised to chromosome 19q13, forming the largest contiguous cluster of proteases within the human genome. Kallikreins are responsible for the coordination of various physiological functions including blood pressure, semen liquefaction and skin desquamation.

Furin is a protease, a proteolytic enzyme activated by substrate presentation that in humans and other animals is encoded by the FURIN gene. Some proteins are inactive when they are first synthesized, and must have sections removed in order to become active. Furin cleaves these sections and activates the proteins. It was named furin because it was in the upstream region of an oncogene known as FES. The gene was known as FUR (FES Upstream Region) and therefore the protein was named furin. Furin is also known as PACE (Paired basic Amino acid Cleaving Enzyme). A member of family S8, furin is a su

Subtilisin is a protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis.

Granzymes are serine proteases released by cytoplasmic granules within cytotoxic T cells and natural killer (NK) cells. They induce programmed cell death (apoptosis) in the target cell, thus eliminating cells that have become cancerous or are infected with viruses or bacteria. Granzymes also kill bacteria and inhibit viral replication. In NK cells and T cells, granzymes are packaged in cytotoxic granules along with perforin. Granzymes can also be detected in the rough endoplasmic reticulum, golgi complex, and the trans-golgi reticulum. The contents of the cytotoxic granules function to permit

class of enzymes

Acrosin is a digestive enzyme that acts as a protease. In humans, acrosin is encoded by the ACR gene. Acrosin is released from the acrosome of spermatozoa as a consequence of the acrosome reaction. It aids in the penetration of the Zona Pellucida.

Tryptase () is the most abundant secretory granule-derived serine proteinase contained in mast cells and has been used as a marker for mast cell activation. Club cells contain tryptase, which is believed to be responsible for cleaving the hemagglutinin surface protein of influenza A virus, thereby activating it and causing the symptoms of flu.

Nattokinase (pronounced ) is an enzyme extracted and purified from a Japanese food called nattō. Nattō is produced by fermentation by adding the bacterium Bacillus subtilis var natto, which also produces the enzyme, to boiled soybeans. While other soy foods contain enzymes, it is only the nattō preparation that contains the specific nattokinase enzyme under the Japan Nattokinase Administration and Ministry of Health, Labour and Welfare.

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens

class of enzymes

mammalian protein found in Homo sapiens

Protein

class of enzymes

mammalian protein found in Homo sapiens

protein-coding gene in the species Homo sapiens

Fibrinolysin is an enzyme derived from plasma of bovine origin (plasmin) or extracted from cultures of certain bacteria. It is used locally only and exclusively together with the enzyme desoxyribonuclease (extracted from bovine pancreas). Fibrinolysin and desoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological Unit) fibrinolysin and 666 BUs desoxyribonuclease per gram.

Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds

class of enzymes

mammalian protein found in Homo sapiens

mammalian protein found in Homo sapiens

Chymases (, mast cell protease 1, skeletal muscle protease, skin chymotryptic proteinase, mast cell serine proteinase, skeletal muscle protease) are a family of serine proteases found primarily in mast cells, though also present in basophil granulocytes (e.g. alpha chymase mcpt8). Recently, Derakhshan et al. reported that a specific mast cell population expressed transcripts for Mcpt8. They show broad peptidolytic activity and are involved in a variety of functions. For example, chymases are released by connective tissue-type mast cells upon challenge with parasites and parasite antigens promo

thumb|right|270px|The classical and alternative complement pathways. thumb|right|270px|Complement-pathways. C3 convertase (C4bC2b, formerly C4b2a) belongs to family of serine proteases and is necessary in innate immunity as a part of the complement system which eventuate in opsonisation of particles, release of inflammatory peptides, C5 convertase formation and cell lysis.

Oryzin (, Aspergillus alkaline proteinase, aspergillopeptidase B, API 21, aspergillopepsin B, aspergillopepsin F, Aspergillus candidus alkaline proteinase, Aspergillus flavus alkaline proteinase, Aspergillus melleus semi-alkaline proteinase, Aspergillus oryzae alkaline proteinase, Aspergillus parasiticus alkaline proteinase, Aspergillus serine proteinase, Aspergillus sydowi alkaline proteinase, Aspergillus soya alkaline proteinase, Aspergillus melleus alkaline proteinase, Aspergillus sulphureus alkaline proteinase, prozyme, P 5380, kyorinase, seaprose S, semi-alkaline protease, sumizyme MP, pr

class of enzymes

Assemblin () is an enzyme with systematic name. This enzyme catalyses the following chemical reaction

class of enzymes

Cucumisin (, euphorbain, solanain, hurain, tabernamontanain) is an enzyme. This enzyme catalyzes hydrolysis of a wide range of proteins. It has been identified as an allergen in humans.

class of enzymes

protein-coding gene in the species Homo sapiens

class of enzymes

Kallikrein-related peptidase 7 (KLK7) is a serine protease that in humans is encoded by the KLK7 gene. KLK7 was initially purified from the epidermis and characterised as stratum corneum chymotryptic enzyme (SCCE). It was later identified as the seventh member of the human kallikrein family, which includes fifteen homologous serine proteases located on chromosome 19 (19q13).

protein-coding gene in the species Homo sapiens