Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
A chromogenic substrate that permits direct measurement of peptide hydrolase activity, e.g., papain and trypsin, by colorimetry. The substrate liberates p-nitroaniline as a chromogenic product.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.
A membrane-bound metalloendopeptidase that may play a role in the degradation or activation of a variety of PEPTIDE HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Genetic mutations that result in loss of function of this protein are a cause of HYPOPHOSPHATEMIC RICKETS, X-LINKED DOMINANT.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
Peptide hydrolases that contain at the active site a SERINE residue involved in catalysis.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.
A biologically active tridecapeptide isolated from the hypothalamus. It has been shown to induce hypotension in the rat, to stimulate contraction of guinea pig ileum and rat uterus, and to cause relaxation of rat duodenum. There is also evidence that it acts as both a peripheral and a central nervous system neurotransmitter.
A 25-kDa peptidase produced by Staphylococcus simulans which cleaves a glycine-glcyine bond unique to an inter-peptide cross-bridge of the STAPHYLOCOCCUS AUREUS cell wall. EC
The process of cleaving a chemical compound by the addition of a molecule of water.
A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
The rate dynamics in chemical or physical systems.
Peptides composed of two amino acid units.
A potent natriuretic and vasodilatory peptide or mixture of different-sized low molecular weight PEPTIDES derived from a common precursor and secreted mainly by the HEART ATRIUM. All these peptides share a sequence of about 20 AMINO ACIDS.
Peptides composed of between two and twelve amino acids.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Thiazepines are heterocyclic chemical compounds containing a seven-membered ring with one nitrogen atom, one sulfur atom, and two carbon-carbon double bonds, which are not commonly found in nature but can be synthesized for potential use in pharmaceuticals or as building blocks in organic chemistry.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Proteins prepared by recombinant DNA technology.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A key enzyme in SPHINGOLIPIDS biosynthesis, this enzyme catalyzes the pyridoxal-5'-phosphate-dependent condensation of L-SERINE and PALMITOYL COENZYME A to 3-dehydro-D-sphinganine. The enzyme consists of two different subunits.
A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
An eleven-amino acid neurotransmitter that appears in both the central and peripheral nervous systems. It is involved in transmission of PAIN, causes rapid contractions of the gastrointestinal smooth muscle, and modulates inflammatory and immune responses.
A nonapeptide messenger that is enzymatically produced from KALLIDIN in the blood where it is a potent but short-lived agent of arteriolar dilation and increased capillary permeability. Bradykinin is also released from MAST CELLS during asthma attacks, from gut walls as a gastrointestinal vasodilator, from damaged tissues as a pain signal, and may be a neurotransmitter.
A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.
One of the endogenous pentapeptides with morphine-like activity. It differs from MET-ENKEPHALIN in the LEUCINE at position 5. Its first four amino acid sequence is identical to the tetrapeptide sequence at the N-terminal of BETA-ENDORPHIN.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in SOIL and WATER. Its organisms are also found in raw meats, MILK and other FOOD, hospital environments, and human clinical specimens. Some species are pathogenic in humans.
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992)
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A condition of an abnormally low level of PHOSPHATES in the blood.
A serotype of botulinum toxins that has specificity for cleavage of SYNAPTOSOMAL-ASSOCIATED PROTEIN 25.
Aryl CYCLOPENTANES that are a reduced (protonated) form of INDENES.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Peptidoglycan is a complex, cross-linked polymer of carbohydrates and peptides that forms the rigid layer of the bacterial cell wall, providing structural support and protection while contributing to the bacterium's susceptibility or resistance to certain antibiotics.
The sum of the weight of all the atoms in a molecule.
Endoproteases that contain proteolytic core domains and ATPase-containing regulatory domains.
Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC and EC

Identification of APC2, a homologue of the adenomatous polyposis coli tumour suppressor. (1/8246)

The adenomatous polyposis coli (APC) tumour-suppressor protein controls the Wnt signalling pathway by forming a complex with glycogen synthase kinase 3beta (GSK-3beta), axin/conductin and betacatenin. Complex formation induces the rapid degradation of betacatenin. In colon carcinoma cells, loss of APC leads to the accumulation of betacatenin in the nucleus, where it binds to and activates the Tcf-4 transcription factor (reviewed in [1] [2]). Here, we report the identification and genomic structure of APC homologues. Mammalian APC2, which closely resembles APC in overall domain structure, was functionally analyzed and shown to contain two SAMP domains, both of which are required for binding to conductin. Like APC, APC2 regulates the formation of active betacatenin-Tcf complexes, as demonstrated using transient transcriptional activation assays in APC -/- colon carcinoma cells. Human APC2 maps to chromosome 19p13.3. APC and APC2 may therefore have comparable functions in development and cancer.  (+info)

Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D. (2/8246)

The crystal structure of profactor D, determined at 2.1 A resolution with an Rfree and an R-factor of 25.1 and 20.4%, respectively, displays highly flexible or disordered conformation for five regions: N-22, 71-76, 143-152, 187-193 and 215-223. A comparison with the structure of its mature serine protease, complement factor D, revealed major conformational changes in the similar regions. Comparisons with the zymogen-active enzyme pairs of chymotrypsinogen, trypsinogen and prethrombin-2 showed a similar distribution of the flexible regions. However, profactor D is the most flexible of the four, and its mature enzyme displays inactive, self-inhibited active site conformation. Examination of the surface properties of the N-terminus-binding pocket indicates that Ile16 may play the initial positioning role for the N-terminus, and Leu17 probably also helps in inducing the required conformational changes. This process, perhaps shared by most chymotrypsinogen-like zymogens, is followed by a factor D-unique step, the re-orientation of an external Arg218 to an internal position for salt-bridging with Asp189, leading to the generation of the self-inhibited factor D.  (+info)

The virulence plasmid-encoded impCAB operon enhances survival and induced mutagenesis in Shigella flexneri after exposure to UV radiation. (3/8246)

Upon exposure to UV radiation, Shigella flexneri SA100 displayed survival and mutation frequencies comparable to those of Escherichia coli AB1157, which contains a functional UmuDC error-prone DNA repair system. Survival of SA100 after UV irradiation was associated with the presence of the 220-kb virulence plasmid, pVP. This plasmid encodes homologues of ImpA and ImpB, which comprise an error-prone DNA repair system encoded on plasmid TP110 that was initially identified in Salmonella typhimurium, and ImpC, encoded upstream of ImpA and ImpB. Although the impB gene was present in representatives of all four species of Shigella, not all isolates tested contained the gene. Shigella isolates that lacked impB were more sensitive to UV radiation than isolates that contained impB. The nucleotide sequence of a 2.4-kb DNA fragment containing the imp operon from S. flexneri SA100 pVP was 96% identical to the imp operon from the plasmid TP110. An SA100 derivative with a mutation in the impB gene had reduced survival following UV irradiation and less UV-induced mutagenesis relative to the parental strain. We also found that S. flexneri contained a chromosomally encoded umuDC operon; however, the umuDC promoter was not induced by exposure to UV radiation. This suggests that the imp operon but not the umuDC operon contributes to survival and induced mutagenesis in S. flexneri following exposure to UV radiation.  (+info)

Alternating antineutrophil cytoplasmic antibody specificity: drug-induced vasculitis in a patient with Wegener's granulomatosis. (4/8246)

We describe a patient who presented with Wegener's granulomatosis associated with antineutrophil cytoplasmic antibodies (ANCA) directed against proteinase 3 (PR3) with a cytoplasmic immunofluorescence pattern (cANCA), whose ANCA type changed to antimyeloperoxidase antibodies with a perinuclear immunofluorescence pattern (pANCA) when treated with propylthiouracil, and changed back to anti-PR3 antibodies with cANCA after the medication was discontinued. The patient developed flares of vasculitis symptoms associated with rises in either type of ANCA. Tests for antimyeloperoxidase ANCA were repeatedly negative before the drug was started, strongly implicating the drug as the cause of the episode. This case demonstrates that patients with idiopathic ANCA-positive vasculitis may quickly develop a superimposed drug-associated ANCA-positive vasculitis. Iatrogenic vasculitis should be suspected when a patient with idiopathic vasculitis with one type of ANCA develops the other type of ANCA.  (+info)

An Arabidopsis 14-3-3 protein can act as a transcriptional activator in yeast. (5/8246)

The 14-3-3 proteins are a group of highly conserved and widely distributed eukaryotic proteins with diverse functions. One 14-3-3 protein, AFT1 from Arabidopsis thaliana, was found to be able to activate transcription in yeast. When fused to the DNA-binding domain of a bacterial protein LexA, AFT1 can activate transcription of reporter genes that contain LexA operator sequences in their promoters. Although the in vivo function of AFT1 is not completely known, its similarity to previously identified proteins found in transcription complexes of Arabidopsis and maize suggests that AFT1 and some other 14-3-3 proteins may activate gene expression in other systems as well.  (+info)

Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects. (6/8246)

The mosquito-borne dengue viruses are widespread human pathogens causing dengue fever, dengue hemorrhagic fever, and dengue shock syndrome, placing 40% of the world's population at risk with no effective treatment. The viral genome is a positive strand RNA that encodes a single polyprotein precursor. Processing of the polyprotein precursor into mature proteins is carried out by the host signal peptidase and by NS3 serine protease, which requires NS2B as a cofactor. We report here the crystal structure of the NS3 serine protease domain at 2.1 A resolution. This structure of the protease combined with modeling of peptide substrates into the active site suggests identities of residues involved in substrate recognition as well as providing a structural basis for several mutational effects on enzyme activity. This structure will be useful for development of specific inhibitors as therapeutics against dengue and other flaviviral proteases.  (+info)

Bile duct epithelial cells exposed to alpha-naphthylisothiocyanate produce a factor that causes neutrophil-dependent hepatocellular injury in vitro. (7/8246)

The acute hepatotoxicity induced by alpha-naphthylisothiocyanate (ANIT) in rats is manifested as neutrophil-dependent necrosis of bile duct epithelial cells (BDECs) and hepatic parenchymal cells. This hepatotoxicity mirrors that of drug-induced cholangiolitic hepatitis in humans. Since BDECs are primary targets of ANIT-induced toxicity, we hypothesized that after exposure to ANIT, BDECs produce a factor(s) that causes neutrophil chemotaxis and neutrophil-dependent hepatocellular injury. To test this hypothesis BDECs were isolated from male Sprague Dawley rats and incubated with ANIT (6.25, 12.5, 25, or 50 microM) or vehicle for 24 h. The conditioned medium (CM) was collected and placed in the bottom chamber of a two-chambered chemotaxis system, while isolated neutrophils were placed in the top chamber. Chemotaxis was indicated by neutrophil migration through a membrane to the bottom chamber. CM from BDECs exposed to each concentration of ANIT was chemotactic, whereas CM from vehicle-treated BDECs was not. ANIT alone caused a modest degree of chemotaxis at 50 microM. The conditioned media were added to isolated hepatocytes or to hepatocyte-neutrophil cocultures and incubated for 24 h. Hepatocyte toxicity was indicated by alanine aminotransferase release into the culture medium. CM from vehicle-treated BDECs did not cause hepatocyte killing in either hepatocyte-neutrophil cocultures or hepatocyte cultures. In contrast, the addition of CM from ANIT-treated BDECs (CM-BDEC-A) to hepatocyte-neutrophil cocultures resulted in hepatocyte killing. The same CM was not cytotoxic to hepatocyte cultures devoid of neutrophils. The hepatocyte killing could not be explained by residual ANIT in the CM, which was below the limit of detection (< or = 0.5 microM). The addition of antiproteases afforded protection against neutrophil-dependent hepatocellular injury induced by CM-BDEC-A. These results indicate that ANIT causes BDECs to release a factor(s) that attracts neutrophils and stimulates them to injure hepatocytes in vitro.  (+info)

Subtilisin-like proprotein convertases, PACE4 and PC8, as well as furin, are endogenous proalbumin convertases in HepG2 cells. (8/8246)

Serum albumin is synthesized as a larger precursor form, proalbumin, which undergoes proteolytic processing at a dibasic site by a hepatic proprotein convertase within the secretory pathway to generate the mature form. Although furin, a member of the subtilisin-like proprotein convertase (SPC) family, was thought to be the only candidate hepatic convertase for proalbumin, SPC family members other than furin were recently suggested to also be involved in proalbumin processing. This study was designed to identify the endogenous proprotein convertases involved in proalbumin processing. Since human hepatoma HepG2 cells are highly differentiated and produce major plasma proteins, this cell line was used as a model for hepatocytes. Northern blot analysis revealed that PACE4, furin and PC8 of the SPC family were expressed in HepG2 cells as well as in the liver. Ribonuclease protection assay showed that PACE4A-II mRNA is the major transcript in HepG2 cells among the PACE4 isoforms. The coexpression studies showed that furin, PACE4A-II and PC8 were all able to convert proalbumin to albumin correctly. To elucidate the roles of these endogenous SPC family members in proalbumin processing, the antisense RNA for PACE4, furin and PC8 was stably expressed in HepG2 cells, respectively. The expression of each antisense RNA resulted in approximately 30% inhibition of endogenous proalbumin processing. We therefore concluded that PACE4 and PC8, as well as furin, are involved in the processing of proalbumin in HepG2 cells, and that these SPC family members are functionally redundant in this processing.  (+info)

Serine endopeptidases are a type of enzymes that cleave peptide bonds within proteins (endopeptidases) and utilize serine as the nucleophilic amino acid in their active site for catalysis. These enzymes play crucial roles in various biological processes, including digestion, blood coagulation, and programmed cell death (apoptosis). Examples of serine endopeptidases include trypsin, chymotrypsin, thrombin, and elastase.

Benzoylarginine nitroanilide is a synthetic peptide derivative that is often used as a substrate in enzyme assays, particularly for testing the activity of proteases (enzymes that break down proteins). Proteases cleave the peptide bond between benzoyl and arginine in the molecule, releasing p-nitroaniline, which can be easily measured spectrophotometrically. This allows researchers to quantify the activity of protease enzymes in a sample. It is also known as Benzoyl-L-arginine ρ-nitroanilide hydrochloride or BAPNA.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Neprilysin (NEP), also known as membrane metallo-endopeptidase or CD10, is a type II transmembrane glycoprotein that functions as a zinc-dependent metalloprotease. It is widely expressed in various tissues, including the kidney, brain, heart, and vasculature. Neprilysin plays a crucial role in the breakdown and regulation of several endogenous bioactive peptides, such as natriuretic peptides, bradykinin, substance P, and angiotensin II. By degrading these peptides, neprilysin helps maintain cardiovascular homeostasis, modulate inflammation, and regulate neurotransmission. In the context of heart failure, neprilysin inhibitors have been developed to increase natriuretic peptide levels, promoting diuresis and vasodilation, ultimately improving cardiac function.

Serine is an amino acid, which is a building block of proteins. More specifically, it is a non-essential amino acid, meaning that the body can produce it from other compounds, and it does not need to be obtained through diet. Serine plays important roles in the body, such as contributing to the formation of the protective covering of nerve fibers (myelin sheath), helping to synthesize another amino acid called tryptophan, and taking part in the metabolism of fatty acids. It is also involved in the production of muscle tissues, the immune system, and the forming of cell structures. Serine can be found in various foods such as soy, eggs, cheese, meat, peanuts, lentils, and many others.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Thiorphan is not a medical condition or disease, but rather a synthetic medication. It is a potent inhibitor of membrane-bound metalloendopeptidases, also known as neprilysin enzymes. These enzymes are responsible for breaking down certain peptides in the body, including some hormones and neurotransmitters.

Thiorphan has been used in research to study the role of these enzymes in various physiological processes. It is also being investigated as a potential therapeutic agent for conditions such as hypertension, heart failure, and Alzheimer's disease. However, it is not currently approved for clinical use in humans.

Therefore, there is no medical definition of 'Thiorphan' as a condition or disease.

PHEX (Phosphate Regulating Endopeptidase Homolog, X-Linked) is a gene that encodes for an enzyme called phosphate regulating neutral endopeptidase. This enzyme is primarily expressed in osteoblasts, which are cells responsible for bone formation.

The main function of the PHEX protein is to regulate the levels of a hormone called fibroblast growth factor 23 (FGF23) by breaking it down. FGF23 plays an essential role in maintaining phosphate homeostasis by regulating its reabsorption in the kidneys and its absorption from the gut.

Inactivating mutations in the PHEX gene can lead to X-linked hypophosphatemia (XLH), a genetic disorder characterized by low levels of phosphate in the blood, impaired bone mineralization, and rickets. In XLH, the production of FGF23 is increased due to the lack of regulation by PHEX, leading to excessive excretion of phosphate in the urine and decreased absorption from the gut. This results in hypophosphatemia, impaired bone mineralization, and other skeletal abnormalities.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

Serine proteinase inhibitors, also known as serine protease inhibitors or serpins, are a group of proteins that inhibit serine proteases, which are enzymes that cut other proteins in a process called proteolysis. Serine proteinases are important in many biological processes such as blood coagulation, fibrinolysis, inflammation and cell death. The inhibition of these enzymes by serpin proteins is an essential regulatory mechanism to maintain the balance and prevent uncontrolled proteolytic activity that can lead to diseases.

Serpins work by forming a covalent complex with their target serine proteinases, irreversibly inactivating them. The active site of serpins contains a reactive center loop (RCL) that mimics the protease's target protein sequence and acts as a bait for the enzyme. When the protease cleaves the RCL, it gets trapped within the serpin structure, leading to its inactivation.

Serpin proteinase inhibitors play crucial roles in various physiological processes, including:

1. Blood coagulation and fibrinolysis regulation: Serpins such as antithrombin, heparin cofactor II, and protease nexin-2 control the activity of enzymes involved in blood clotting and dissolution to prevent excessive or insufficient clot formation.
2. Inflammation modulation: Serpins like α1-antitrypsin, α2-macroglobulin, and C1 inhibitor regulate the activity of proteases released during inflammation, protecting tissues from damage.
3. Cell death regulation: Some serpins, such as PI-9/SERPINB9, control apoptosis (programmed cell death) by inhibiting granzyme B, a protease involved in this process.
4. Embryonic development and tissue remodeling: Serpins like plasminogen activator inhibitor-1 (PAI-1) and PAI-2 regulate the activity of enzymes involved in extracellular matrix degradation during embryonic development and tissue remodeling.
5. Neuroprotection: Serpins such as neuroserpin protect neurons from damage by inhibiting proteases released during neuroinflammation or neurodegenerative diseases.

Dysregulation of serpins has been implicated in various pathological conditions, including thrombosis, emphysema, Alzheimer's disease, and cancer. Understanding the roles of serpins in these processes may provide insights into potential therapeutic strategies for treating these diseases.

Cysteine endopeptidases are a type of enzymes that cleave peptide bonds within proteins. They are also known as cysteine proteases or cysteine proteinases. These enzymes contain a catalytic triad consisting of three amino acids: cysteine, histidine, and aspartate. The thiol group (-SH) of the cysteine residue acts as a nucleophile and attacks the carbonyl carbon of the peptide bond, leading to its cleavage.

Cysteine endopeptidases play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They are involved in many physiological and pathological conditions, such as apoptosis, immune response, and cancer. Some examples of cysteine endopeptidases include cathepsins, caspases, and calpains.

It is important to note that these enzymes require a reducing environment to maintain the reduced state of their active site cysteine residue. Therefore, they are sensitive to oxidizing agents and inhibitors that target the thiol group. Understanding the structure and function of cysteine endopeptidases is crucial for developing therapeutic strategies that target these enzymes in various diseases.

Metalloendopeptidases are a type of enzymes that cleave peptide bonds in proteins, specifically at interior positions within the polypeptide chain. They require metal ions as cofactors for their catalytic activity, typically zinc (Zn2+) or cobalt (Co2+). These enzymes play important roles in various biological processes such as protein degradation, processing, and signaling. Examples of metalloendopeptidases include thermolysin, matrix metalloproteinases (MMPs), and neutrophil elastase.

Serine proteases are a type of enzyme that cleaves peptide bonds in proteins. They have a serine residue in their active site that plays a crucial role in the catalytic mechanism. These enzymes are involved in various biological processes, including blood coagulation, fibrinolysis, inflammation, cell death, and hormone activation. Some examples of serine proteases include trypsin, chymotrypsin, thrombin, and elastase. They play a significant role in disease processes such as cancer, Alzheimer's disease, and emphysema.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Glycopeptides are a class of antibiotics that are characterized by their complex chemical structure, which includes both peptide and carbohydrate components. These antibiotics are produced naturally by certain types of bacteria and are effective against a range of Gram-positive bacterial infections, including methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococci (VRE).

The glycopeptide antibiotics work by binding to the bacterial cell wall precursor, preventing the cross-linking of peptidoglycan chains that is necessary for the formation of a strong and rigid cell wall. This leads to the death of the bacteria.

Examples of glycopeptides include vancomycin, teicoplanin, and dalbavancin. While these antibiotics have been used successfully for many years, their use is often limited due to concerns about the emergence of resistance and potential toxicity.

Neurotensin is a neuropeptide that is widely distributed in the central nervous system and the gastrointestinal tract. It is composed of 13 amino acids and plays a role as a neurotransmitter or neuromodulator in various physiological functions, including pain regulation, temperature regulation, and feeding behavior. Neurotensin also has been shown to have potential roles in the development of certain diseases such as cancer and neurological disorders. It exerts its effects by binding to specific receptors, known as neurotensin receptors (NTSR1, NTSR2, and NTSR3), which are widely distributed throughout the body.

Lysostaphin is not a disease or condition, but rather a bacteriolytic enzyme produced by certain strains of Staphylococcus species. It is an endopeptidase that specifically targets and cleaves the pentaglycine cross-bridge in the cell wall peptidoglycan of Staphylococcus aureus, leading to bacterial lysis and death. Lysostaphin has been studied for its potential therapeutic use in treating Staphylococcus aureus infections, including those caused by methicillin-resistant Staphylococcus aureus (MRSA) strains.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Aspartic acid endopeptidases are a type of enzyme that cleave peptide bonds within proteins. They are also known as aspartyl proteases or aspartic proteinases. These enzymes contain two catalytic aspartic acid residues in their active site, which work together to hydrolyze the peptide bond.

Aspartic acid endopeptidases play important roles in various biological processes, including protein degradation, processing, and activation. They are found in many organisms, including viruses, bacteria, fungi, plants, and animals. Some well-known examples of aspartic acid endopeptidases include pepsin, cathepsin D, and HIV protease.

Pepsin is a digestive enzyme found in the stomach that helps break down proteins in food. Cathepsin D is a lysosomal enzyme that plays a role in protein turnover and degradation within cells. HIV protease is an essential enzyme for the replication of the human immunodeficiency virus (HIV), which causes AIDS. Inhibitors of HIV protease are used as antiretroviral drugs to treat HIV infection.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

A dipeptide is a type of molecule that is formed by the condensation of two amino acids. In this process, the carboxyl group (-COOH) of one amino acid combines with the amino group (-NH2) of another amino acid, releasing a water molecule and forming a peptide bond.

The resulting molecule contains two amino acids joined together by a single peptide bond, which is a type of covalent bond that forms between the carboxyl group of one amino acid and the amino group of another. Dipeptides are relatively simple molecules compared to larger polypeptides or proteins, which can contain hundreds or even thousands of amino acids linked together by multiple peptide bonds.

Dipeptides have a variety of biological functions in the body, including serving as building blocks for larger proteins and playing important roles in various physiological processes. Some dipeptides also have potential therapeutic uses, such as in the treatment of hypertension or muscle wasting disorders.

Atrial natriuretic factor (ANF), also known as atrial natriuretic peptide (ANP), is a hormone that is primarily produced and secreted by the atria of the heart in response to stretching of the cardiac muscle cells due to increased blood volume. ANF plays a crucial role in regulating body fluid homeostasis, blood pressure, and cardiovascular function.

The main physiological action of ANF is to promote sodium and water excretion by the kidneys, which helps lower blood volume and reduce blood pressure. ANF also relaxes vascular smooth muscle, dilates blood vessels, and inhibits the renin-angiotensin-aldosterone system (RAAS), further contributing to its blood pressure-lowering effects.

Defects in ANF production or action have been implicated in several cardiovascular disorders, including heart failure, hypertension, and kidney disease. Therefore, ANF and its analogs are being investigated as potential therapeutic agents for the treatment of these conditions.

Oligopeptides are defined in medicine and biochemistry as short chains of amino acids, typically containing fewer than 20 amino acid residues. These small peptides are important components in various biological processes, such as serving as signaling molecules, enzyme inhibitors, or structural elements in some proteins. They can be found naturally in foods and may also be synthesized for use in medical research and therapeutic applications.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Thiazepines are not a recognized term in medical terminology or pharmacology. It appears that you may have misspelled "thiazepines," which also does not have a specific medical meaning. However, "thiazepine" is a chemical compound with a specific structure, and it is the core structure of some drugs such as thiazepine derivatives. These derivatives are often used for their sedative, hypnotic, anticonvulsant, and muscle relaxant properties.

If you meant to ask about "thiazide" or "thiazide diuretics," I would be happy to provide a definition:

Thiazides are a class of diuretic medications that act on the distal convoluted tubule in the kidney, promoting sodium and chloride excretion. This also leads to increased water excretion (diuresis) and decreased extracellular fluid volume. Thiazide diuretics are primarily used to treat hypertension and edema associated with heart failure or liver cirrhosis. Common thiazide diuretics include hydrochlorothiazide, chlorthalidone, and indapamide.

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Carboxypeptidases are a group of enzymes that catalyze the cleavage of peptide bonds at the carboxyl-terminal end of polypeptides or proteins. They specifically remove the last amino acid residue from the protein chain, provided that it has a free carboxyl group and is not blocked by another chemical group. Carboxypeptidases are classified into two main types based on their catalytic mechanism: serine carboxypeptidases and metallo-carboxypeptidases.

Serine carboxypeptidases, also known as chymotrypsin C or carboxypeptidase C, use a serine residue in their active site to catalyze the hydrolysis of peptide bonds. They are found in various organisms, including animals and bacteria.

Metallo-carboxypeptidases, on the other hand, require a metal ion (usually zinc) for their catalytic activity. They can be further divided into several subtypes based on their structure and substrate specificity. For example, carboxypeptidase A prefers to cleave hydrophobic amino acids from the carboxyl-terminal end of proteins, while carboxypeptidase B specifically removes basic residues (lysine or arginine).

Carboxypeptidases have important roles in various biological processes, such as protein maturation, digestion, and regulation of blood pressure. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

Cathepsin B is a lysosomal cysteine protease that plays a role in various physiological processes, including intracellular protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor (procathepsin B) and activated upon cleavage of the propeptide by other proteases or autocatalytically. Cathepsin B has a wide range of substrates, including collagen, elastin, and various intracellular proteins. Its dysregulation has been implicated in several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Serine C-palmitoyltransferase (SCPT) is an enzyme responsible for the rate-limiting step in the biosynthesis of sphingolipids, a type of lipid found in cell membranes. Sphingolipids play crucial roles in signal transduction and cell regulation. The enzyme catalyzes the condensation of serine and palmitoyl-CoA to form 3-ketosphinganine, which is then reduced to sphinganine and further modified to produce various sphingolipids. There are two main forms of SCPT, known as SCPT1 and SCPT2, which differ in their subcellular localization and substrate specificity. Defects in the genes encoding these enzymes can lead to serious inherited disorders affecting multiple organ systems, such as hereditary sensory neuropathy type 1 (HSAN1) and forms of ichthyosis.

I'm sorry for any confusion, but "Isoflurophate" does not appear to be a recognized term in medical or scientific literature. It is possible that there may be a spelling error or typo in the term you are looking for. If you meant "Isoflurane," which is a commonly used anesthetic in medical and surgical procedures, I can provide a definition for that.

Isoflurane: A volatile halogenated ether liquid used as an inhalational general anesthetic agent. It has a rapid onset and offset of action, making it useful for both induction and maintenance of anesthesia. Isoflurane is also known to have bronchodilatory properties, which can be beneficial in patients with reactive airway disease or asthma.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Aminopeptidases are a group of enzymes that catalyze the removal of amino acids from the N-terminus of polypeptides and proteins. They play important roles in various biological processes, including protein degradation, processing, and activation. Aminopeptidases are classified based on their specificity for different types of amino acids and the mechanism of their action. Some of the well-known aminopeptidases include leucine aminopeptidase, alanyl aminopeptidase, and arginine aminopeptidase. They are widely distributed in nature and found in various tissues and organisms, including bacteria, plants, and animals. In humans, aminopeptidases are involved in several physiological functions, such as digestion, immune response, and blood pressure regulation.

Substance P is an undecapeptide neurotransmitter and neuromodulator, belonging to the tachykinin family of peptides. It is widely distributed in the central and peripheral nervous systems and is primarily found in sensory neurons. Substance P plays a crucial role in pain transmission, inflammation, and various autonomic functions. It exerts its effects by binding to neurokinin 1 (NK-1) receptors, which are expressed on the surface of target cells. Apart from nociception and inflammation, Substance P is also involved in regulating emotional behaviors, smooth muscle contraction, and fluid balance.

Bradykinin is a naturally occurring peptide in the human body, consisting of nine amino acids. It is a potent vasodilator and increases the permeability of blood vessels, causing a local inflammatory response. Bradykinin is formed from the breakdown of certain proteins, such as kininogen, by enzymes called kininases or proteases, including kallikrein. It plays a role in several physiological processes, including pain transmission, blood pressure regulation, and the immune response. In some pathological conditions, such as hereditary angioedema, bradykinin levels can increase excessively, leading to symptoms like swelling, redness, and pain.

Exopeptidases are a type of enzyme that break down peptides or proteins by cleaving off one amino acid at a time from the end of the protein or peptide chain. There are two main types of exopeptidases: aminopeptidases, which remove amino acids from the N-terminus (the end of the chain with a free amino group), and carboxypeptidases, which remove amino acids from the C-terminus (the end of the chain with a free carboxyl group).

Exopeptidases play important roles in various biological processes, including protein degradation and turnover, digestion, and processing of peptide hormones and neuropeptides. They are also involved in the pathogenesis of certain diseases, such as cancer and neurodegenerative disorders, where they can contribute to the accumulation of abnormal proteins and toxic protein fragments.

Exopeptidases are found in various organisms, including bacteria, fungi, plants, and animals. They are also used in biotechnology and research, for example, in the production of pharmaceuticals, food ingredients, and diagnostic tools.

Enkephalins are naturally occurring opioid peptides in the body that bind to opiate receptors and help reduce pain and produce a sense of well-being. There are two major types of enkephalins: Met-enkephalin and Leu-enkephalin, which differ by only one amino acid at position 5 (Leucine or Methionine).

Leu-enkephalin, also known as YGGFL, is a type of enkephalin that contains the amino acids Tyrosine (Y), Glycine (G), Glycine (G), Phenylalanine (F), and Leucine (L) in its sequence. It is involved in pain regulation, mood, and other physiological processes.

Leu-enkephalin is synthesized from a larger precursor protein called proenkephalin and is stored in the secretory vesicles of neurons. When released into the synaptic cleft, Leu-enkephalin can bind to opioid receptors on neighboring cells, leading to various physiological responses.

Leu-enkephalin has a shorter half-life than Met-enkephalin due to its susceptibility to enzymatic degradation by peptidases. However, it still plays an essential role in modulating pain and other functions in the body.

Flavobacterium is a genus of Gram-negative, rod-shaped bacteria that are widely distributed in various environments such as water, soil, and associated with plants and animals. They are facultative anaerobes, which means they can grow in the presence or absence of oxygen. Some species of Flavobacterium are known to cause opportunistic infections in humans, particularly in individuals with compromised immune systems. These infections can include respiratory tract infections, wound infections, and bacteremia (bloodstream infections). However, Flavobacterium infections are relatively rare in healthy individuals.

It's worth noting that while some species of Flavobacterium have been associated with human disease, many others are important members of the microbial community in various environments and play beneficial roles in biogeochemical cycles and food webs.

Subtilisins are a group of serine proteases that are produced by certain bacteria, including Bacillus subtilis. They are named after the bacterium and the Latin word "subtilis," which means delicate or finely made. Subtilisins are alkaline proteases, meaning they work best in slightly basic conditions.

Subtilisins have a broad specificity for cleaving peptide bonds and can hydrolyze a wide range of protein substrates. They are widely used in industry for various applications such as detergents, food processing, leather treatment, and biotechnology due to their ability to function at high temperatures and in the presence of denaturing agents.

In medicine, subtilisins have been studied for their potential use in therapeutic applications, including as anti-inflammatory agents and in wound healing. However, more research is needed to fully understand their mechanisms of action and potential benefits.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

Thermolysin is not a medical term per se, but it is a bacterial enzyme that is often used in biochemistry and molecular biology research. Here's the scientific or biochemical definition:

Thermolysin is a zinc metalloprotease enzyme produced by the bacteria Geobacillus stearothermophilus. It has an optimum temperature for activity at around 65°C, and it can remain active in high temperatures, which makes it useful in various industrial applications. Thermolysin is known for its ability to cleave peptide bonds, particularly those involving hydrophobic residues, making it a valuable tool in protein research and engineering.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Hypophosphatemia is a medical condition characterized by abnormally low levels of phosphate (phosphorus) in the blood, specifically below 2.5 mg/dL. Phosphate is an essential electrolyte that plays a crucial role in various bodily functions such as energy production, bone formation, and maintaining acid-base balance.

Hypophosphatemia can result from several factors, including malnutrition, vitamin D deficiency, alcoholism, hormonal imbalances, and certain medications. Symptoms of hypophosphatemia may include muscle weakness, fatigue, bone pain, confusion, and respiratory failure in severe cases. Treatment typically involves correcting the underlying cause and administering phosphate supplements to restore normal levels.

Botulinum toxins type A are neurotoxins produced by the bacterium Clostridium botulinum and related species. These toxins act by blocking the release of acetylcholine at the neuromuscular junction, leading to muscle paralysis. Botulinum toxin type A is used in medical treatments for various conditions characterized by muscle spasticity or excessive muscle activity, such as cervical dystonia, blepharospasm, strabismus, and chronic migraine. It is also used cosmetically to reduce the appearance of wrinkles by temporarily paralyzing the muscles that cause them. The commercial forms of botulinum toxin type A include Botox, Dysport, and Xeomin.

"Indans" is not a recognized medical term or abbreviation in the field of medicine or pharmacology. It's possible that you may be referring to "indanes," which are chemical compounds that contain a indane ring structure, consisting of two benzene rings fused in an angular arrangement. Some indane derivatives have been studied for their potential medicinal properties, such as anti-inflammatory and analgesic effects. However, it's important to note that the medical use and efficacy of these compounds can vary widely and should be evaluated on a case-by-case basis under the guidance of a qualified healthcare professional.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Peptidoglycan is a complex biological polymer made up of sugars and amino acids that forms a crucial component of the cell walls of bacteria. It provides structural support and protection to bacterial cells, contributing to their shape and rigidity. Peptidoglycan is unique to bacterial cell walls and is not found in the cells of other organisms, such as plants, animals, or fungi.

The polymer is composed of linear chains of alternating units of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM), which are linked together by glycosidic bonds. The NAM residues contain short peptide side chains, typically consisting of four amino acids, that cross-link adjacent polysaccharide chains, forming a rigid layer around the bacterial cell.

The composition and structure of peptidoglycan can vary between different species of bacteria, which is one factor contributing to their diversity. The enzymes responsible for synthesizing and degrading peptidoglycan are important targets for antibiotics, as inhibiting these processes can weaken or kill the bacterial cells without affecting host organisms.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

ATP-dependent endopeptidases are a type of enzyme that require ATP (adenosine triphosphate) to catalyze the hydrolysis of peptide bonds within proteins. These enzymes are also known as ATP-dependent proteases or protein-breaking enzymes, and they play important roles in various cellular processes such as protein quality control, regulation of signaling pathways, and programmed cell death (apoptosis).

The ATP-dependent endopeptidases use the energy from ATP to unfold and translocate proteins into their active sites for degradation. They are typically composed of multiple subunits that form a large protein complex, including a catalytic core and regulatory domains. The regulation of these enzymes is critical for maintaining cellular homeostasis, as dysregulation can lead to various diseases such as neurodegenerative disorders, cancer, and infectious diseases.

Examples of ATP-dependent endopeptidases include the proteasome, which plays a central role in protein degradation in eukaryotic cells, and ClpP, which is involved in protein quality control in bacteria.

Carboxypeptidases A are a group of enzymes that play a role in the digestion of proteins. They are found in various organisms, including humans, and function to cleave specific amino acids from the carboxyl-terminal end of protein substrates. In humans, Carboxypeptidase A is primarily produced in the pancreas and secreted into the small intestine as an inactive zymogen called procarboxypeptidase A.

Procarboxypeptidase A is activated by trypsin, another proteolytic enzyme, to form Carboxypeptidase A1 and Carboxypeptidase A2. These enzymes have different substrate specificities, with Carboxypeptidase A1 preferentially cleaving aromatic amino acids such as phenylalanine and tyrosine, while Carboxypeptidase A2 cleaves basic amino acids such as arginine and lysine.

Carboxypeptidases A play a crucial role in the final stages of protein digestion by breaking down large peptides into smaller di- and tripeptides, which can then be absorbed by the intestinal epithelium and transported to other parts of the body for use as building blocks or energy sources.

IgA-specific+serine+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... IgA protease (EC, IgA-specific serine endopeptidase, IgA proteinase, IgA-specific proteinase, immunoglobulin A ... where the X in the sequence preferably is a Proline or Serine; the Y = Threonine, Serine or Alanine; and Z preferably is ...
Serine Endopeptidases: Advances in Research and Application: 2011 Edition. ScholarlyEditions. 2012. ISBN 978-1-4649-2658-7.[ ...
The extracellular matrix is degraded by serine endopeptidases and metalloproteinases. The syncytiotrophoblast can then invade ... The embryo releases serine proteases which causes the epithelial cell membrane to depolarize and activates the epithelial ... and by serine proteases. The collagenases digest Types I, II, III, VII and X collagen. The gelatinases exist in two forms; one ...
It is the type serine endopeptidase of MEROPS family S8. The structure of subtilisin has been determined by X-ray ... Subtilisins belong to subtilases, a group of serine proteases that - like all serine proteases - initiate the nucleophilic ... It is structurally unrelated to the chymotrypsin-clan of serine proteases, but uses the same type of catalytic triad in the ... Polgár L (1987). "Structure and function of serine proteases". In Brocklehurst K, Neuberger A (eds.). Hydrolytic enzymes. ...
... "serine-type endopeptidase activity" (GO:0004252)". Amigo. Gene Ontology Consortium. Retrieved 2018-10-17. "GO:0008236 serine- ... Assembled in the genome of the clavibacter michiganensis specie, It is a putative serine protease gene that belongs to the ... This is possible due to the catalytic triad in their active site of their protein sequence: Aspartate, Serine and Histidine ( ... Universal protein resource accession number A5CU31 for "sbtB - Putative serine protease, peptidase family S8A - Clavibacter ...
"Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases". Biochemical and Biophysical Research ... paired-basic endopeptidase, yeast cysteine proteinase F, paired-basic endopeptidase, andrenorphin-Gly-generating enzyme, ... Kexin (EC is a prohormone-processing protease, specifically a yeast serine peptidase, found in the budding yeast (S ... Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (February 1989). "Characterization of KEX2-encoded endopeptidase from yeast ...
... s (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the ... Serine Peptidase Serine Proteases site at Saint Louis University (SLU) Serine+proteases at the U.S. National Library of ... The serine -OH attacks the carbonyl carbon, and the nitrogen of the histidine accepts the hydrogen from the -OH of the [serine ... Serine proteases are paired with serine protease inhibitors, which turn off their activity when they are no longer needed.[self ...
It is a serine endopeptidase (protease group S1, PA clan). Factor X is synthesized in the liver and requires vitamin K for its ... Factor X is an enzyme, a serine endopeptidase, which plays a key role at several stages of the coagulation system. Factor X is ... Factor Xa is inactivated by protein Z-dependent protease inhibitor (ZPI), a serine protease inhibitor (serpin). The affinity of ... "Complementary DNA cloning and kinetic characterization of a novel intracellular serine proteinase inhibitor: mechanism of ...
S. epidermidis glutamyl endopeptidase GluSE Also called S. epidermidis serine protease (Esp). S. warneri glutamyl endopeptidase ... subtilis glutamyl endopeptidase GluBS Enterococcus E. faecalis glutamyl endopeptidase SprE Glutamyl endopeptidase is in at ... Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been ... Birktoft, Jens J.; Breddam, Klaus (1994). "[8] Glutamyl endopeptidases". Proteolytic Enzymes: Serine and Cysteine Peptidases. ...
... 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site ... Studies of human pancreatic elastase 1 have shown that this serine protease maps to the chromosomal region 12q13 and it is ... Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains ... or serine elastase. The first isozyme, pancreatic elastase 1, was initially thought to be expressed in the pancreas. However it ...
It is the zymogen form of factor XIIa, an enzyme (EC of the serine protease (or serine endopeptidase) class. In ... Chung DW, Fujikawa K, McMullen BA, Davie EW (May 1986). "Human plasma prekallikrein, a zymogen to a serine protease that ...
13 KD serine protease, or 24KD endopeptidase.[which?] Angiostatin is known to bind many proteins, especially to angiomotin and ...
... (EC, plant Leu-proteinase, leucine-specific serine proteinase, leucine endopeptidase, spinach ... Leucyl+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.21). ... Aducci P, Ascenzi P, Ballio A (October 1986). "Esterolytic Properties of Leucine-Proteinase, the Leucine-Specific Serine ... serine proteinase (leucine specific), spinach leucine-specific serine proteinase, Leu-proteinase) is an enzyme. This enzyme ...
Sendai virus uses activating proteases that are serine endopeptidases represented by tryptase beta 2-(TPSB2),WikiGenes - ... For example, transmembrane serine protease 2 (TMPRSS2), which is an F-protein-processing enzyme, is often overexpressed in ... Not all cancer cells have cell entry receptors for the virus and not all cancer cells express virus processing serine proteases ... This activation requires F0 cleavage by host serine protease before the virus adsorbtion (see the section "proteolytic cleavage ...
... serine endopeptidases MeSH D08.811.277.656.300.760.030 - acrosin MeSH D08.811.277.656.300.760.176 - chymotrypsin MeSH D08.811. ... endopeptidase clp MeSH D08.811.277.656.149.500 - protease la MeSH D08.811.277.656.300 - endopeptidases MeSH D08.811.277.656. ... endopeptidase clp MeSH D08.811.277.656.300.760.247 - endopeptidase k MeSH D08.811.277.656.300.760.284 - enteropeptidase MeSH ... Serine-type D-Ala-D-Ala carboxypeptidase MeSH D08.811.277.656.350.245.280 - gamma-glutamyl hydrolase MeSH D08.811.277.656. ...
... may refer to: IgA specific serine endopeptidase, an enzyme IgA-specific metalloendopeptidase, an enzyme This set ...
... such as Val-Val This Escherichia coli serine endopeptidase is essential for the clearance of denatured proteins from the inner- ... Pallen MJ, Wren BW (October 1997). "The HtrA family of serine proteases". Molecular Microbiology. 26 (2): 209-21. doi:10.1046/j ... is an endopeptidase". Journal of Bacteriology. 172 (4): 1791-7. doi:10.1128/jb.172.4.1791-1797.1990. PMC 208670. PMID 2180903. ... a large serine protease containing multiple subunits". Archives of Biochemistry and Biophysics. 224 (2): 543-54. doi:10.1016/ ...
... staphylococcal serine proteinase) is an extracellular bacterial serine protease of the glutamyl endopeptidase I family that was ... Glutamyl endopeptidase is in S. aureus expressed from the gene sspA within the operon ssp. Downstream of sspA, the operon also ... Glutamyl endopeptidase is expressed as a zymogen that, in order to become fully active, has been modified both through ... Glutamyl endopeptidase can inhibit the activation of targets within the complement system. It is indicated to cause inhibition ...
... is a large cytosolic enzyme that belongs to a distinct class of serine peptidases. It was first described ... Prolyl endopeptidase is a cytosolic prolyl endopeptidase that cleaves peptide bonds on the C-terminal side of prolyl residues ... prolyl+endopeptidase,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Prolyl Endopeptidase entry ... "Entrez Gene: PREP prolyl endopeptidase". Oliveira EB, Martins AR, Camargo AC (May 1976). "Isolation of brain endopeptidases: ...
... pancreatic endopeptidase E EC pancreatic elastase II EC IgA-specific serine endopeptidase EC u ... Ste24 endopeptidase EC S2P endopeptidase EC ADAM 17 endopeptidase EC ADAMTS13 endopeptidase EC ... ADAM10 endopeptidase EC ADAMTS-4 endopeptidase EC anthrax lethal factor endopeptidase EC ... Now covered by the microbial serine proteinases EC (subtilisin), EC (oryzin), EC (endopeptidase K ...
... (EC, E. coli cytoplasmic proteinase, proteinase So, Escherichia coli serine proteinase So) is an ... Endopeptidase+So at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (CS1: long ... Chung CH, Goldberg AL (April 1983). "Purification and characterization of protease So, a cytoplasmic serine protease in ... or Bz-Arg-OEt This is an Escherichia coli cytoplasmic endopeptidase. Goldberg AL, Swamy KH, Chung CH, Larimore FS (1981). ...
... exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases". The EMBO ... Cathepsin C functions as a key enzyme in the activation of granule serine peptidases in inflammatory cells, such as elastase ... Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin ...
... a lysine-specific serine protease". The Journal of Biological Chemistry. 264 (7): 3832-9. doi:10.1016/S0021-9258(19)84926-8. ... Lysyl+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.21). ... Lysyl endopeptidase (EC, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, ... "BRENDA - Information on EC - lysyl endopeptidase". Retrieved 2018-05-28. "Caseinase ...
Tritirachium album serine proteinase, Tritirachium album proteinase K) is a broad-spectrum serine protease. The enzyme was ... In molecular biology, Proteinase K (EC, protease K, endopeptidase K, Tritirachium alkaline proteinase, ... Temperatures above 65 °C, trichloroacetic acid (TCA) or the serine protease-inhibitors AEBSF, PMSF or DFP inhibit the activity ... Proteinase K is inhibited by serine protease inhibitors such as phenylmethylsulfonyl fluoride (PMSF), ...
Endopeptidase Clp ATP-dependent Clp protease proteolytic subunit Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, ... In molecular biology, the CLP protease family is a family of serine peptidases belong to the MEROPS peptidase family S14 (ClpP ... endopeptidase family, clan SK). ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin ...
... (EC, ATP-dependent serine proteinase, lon proteinase, protease La, proteinase La, ATP-dependent lon ... Endopeptidase+La at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (Articles with ... serine protease La) is an enzyme. This enzyme catalyses hydrolysis of proteins in the presence of ATP. This enzyme is a product ... proteinase, ATP-dependent protease La, Escherichia coli proteinase La, Escherichia coli serine proteinase La, gene lon protease ...
... similar to serine proteases). Papain-like proteases are usually endopeptidases, but some members of the group are also, or even ... serine, and aspartic proteases). In humans, there are 11 cysteine cathepsins: B, C, F, H, K, L, O, S, V, X, and W. Most ...
... (EC, cholesterol-binding proteinase, proteinase E, cholesterol-binding serine proteinase, ... Pancreatic+endopeptidase+E at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.21) ...
This protein is an essential component to form the protein complex of Clp protease (Endopeptidase Clp). Enzyme ClpP is a highly ... conserved serine protease present throughout bacteria and also found in the mitochondria and chloroplasts of eukaryotic cells. ... CLP protease family Endopeptidase Clp Protease Transfer-messenger RNA GRCh38: Ensembl release 89: ENSG00000125656 - Ensembl, ...
... serine, and threonine proteases Nafamostat - inhibitor of trypsin, tryptase, and various other serine proteases Pacifastins - ... An endopeptidase inhibitor is a drug that inhibits one or more endopeptidase enzymes. Endopeptidases are one of two types of ... Endopeptidases cleave peptide bonds of non-terminal amino acids (that is, they cut proteins/peptides into two chains), whereas ... Some examples of endopeptidase inhibitors include the following: Neprilysin inhibitors Selective neprilysin inhibitors ...
IgA-specific+serine+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... IgA protease (EC, IgA-specific serine endopeptidase, IgA proteinase, IgA-specific proteinase, immunoglobulin A ... where the X in the sequence preferably is a Proline or Serine; the Y = Threonine, Serine or Alanine; and Z preferably is ...
Mathieu P, Villemot JP, Stoltz JF, Scheck F, Garnier LF (June 1996). "[Antiaggregant effect and tolerance of calcium carbasalate administrated immediately after aorto-coronary bypass. Results of a double-blind versus placebo study]". Pathologie-Biologie. 44 (6): 571-80. PMID 8977914 ...
Serine Endopeptidases / analysis * Smoking / adverse effects* * Sputum* / chemistry * Sputum* / cytology * Tryptases Substances ...
Serine Endopeptidases * TMPRSS3 protein, human Supplementary concepts * Nonsyndromic Deafness Grants and funding * PI17/00572/ ...
enables serine-type endopeptidase activity ISO Inferred from Sequence Orthology. more info ...
enables serine-type endopeptidase inhibitor activity IEA Inferred from Electronic Annotation. more info ... Predicted to enable serine-type endopeptidase inhibitor activity. Predicted to be involved in negative regulation of ... SPINK4 serine peptidase inhibitor Kazal type 4 [Homo sapiens] SPINK4 serine peptidase inhibitor Kazal type 4 [Homo sapiens]. ... KAZAL_FS; Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such ...
Categories: Serine Endopeptidases Image Types: Photo, Illustrations, Video, Color, Black&White, PublicDomain, ...
Trypsin-like serine proteases Functional Family. Enzyme Information. 3.4.21.-. Serine endopeptidases. ... The structure of the superantigen exfoliative toxin A suggests a novel regulation as a serine protease. ...
Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21). Digestive enzymes. *Enteropeptidase. *Trypsin ... It is a serine protease (EC found on endothelial cells, the cells that line the blood vessels. As an enzyme, it ... To be specific, tPA cleaves the zymogen plasminogen at its Arg561 - Val562 peptide bond, into the serine protease plasmin.[ ... Sheehan JJ, Tsirka SE (June 2005). "Fibrin-modifying serine proteases thrombin, tPA, and plasmin in ischemic stroke: a review ...
It is a serine endopeptidase .-Physiology:.... , plasminogen. * decrease antithrombin. Antithrombin. Antithrombin is a small ... It is an enzyme of the serine protease class. A recombinant form of human factor VIIa has U.S. Food and Drug Administration ... Factor IX is one of the serine proteases of the coagulation system; it belongs to peptidase family S1. Deficiency of this ...
serine-type endopeptidase inhibitor activity enables. IBA. MGI:101780 more .... 13792537. PMID:21873635. GO_Central. ... Predicted to enable serine-type endopeptidase inhibitor activity. Involved in positive regulation of biosynthetic process and ... serine (or cysteine) peptidase inhibitor, clade B, member 7 Serpinb7 serine (or cysteine) proteinase inhibitor, clade B, member ... Megsin; serine (or cysteine) peptidase inhibitor, clade B, member 7; serine (or cysteine) proteinase inhibitor, clade B ( ...
Molecular Function: serine-type endopeptidase inhibitor activity (GO:0004867). - Biological Process: response to wounding (GO: ...
Serine-type endopeptidase inhibitor activity. 229. Diseases. Name. # of Products. Disease mutation. 5332. ... This gene encodes a member of the serpin superfamily of serine proteinase inhibitors. The protein is primarily secreted by ...
Serine-type endopeptidase involved in vacuolar protein catabolism, response to starvation, and spore formation; localizes to ... Vacuolar proteinase B yscB with H3 N-terminal endopeptidase activity; serine protease of subtilisin family; involved in protein ...
serine-type endopeptidase activity (GO:0004252). This is a PFAM domain. For full annotation and more information, please see ... which itself is hydrogen-bonded to a serine. The sequences in the vicinity of the active site serine and histidine residues are ... The catalytic activity of the serine proteases from the trypsin family is provided by a charge relay system involving an ...
Serine proteases (serine endopeptidases) are defined as proteolytic enzymes with a serine residue in their active site; they ... The activity of all three serine proteases-factor Xa, thrombin, plasmin-is tightly regulated by circulating serpins (serine ... A structurally related serine protease is trypsin.. In the extrinsic coagulation process triggered by tissue factor, the ... Other serine proteases such as trypsin (in the intestine) are also released as zymogens (trypsinogen) that require proteolytic ...
Molecular Function: serine-type endopeptidase inhibitor activity (GO:0004867). - Biological Process: response to wounding (GO: ...
Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyzes post-proline peptide bonds in peptides that are ... BACKGROUND: Prolyl oligopeptidase (POP, EC is a serine peptidase that hydrolyzes post-proline peptide bonds in ...
Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases.. Mizuno K, Nakamura T, Ohshima T, ... This calcium-dependent serine endoprotease is concentrated in the trans-Golgi network, associated with membranes, and is not ... Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease.. Fuller RS, Brake A, Thorner J. ... PACE4 (paired basic amino acid cleaving system 4, SPC4) is a calcium-dependent serine endoprotease that can cleave precursor ...
Trypsin-ultra, Mass Spectrometry Grade is a serine endopeptidase, which selectively cleaves peptide bonds C-terminal to lysine ... Endoproteinase LysC is a serine endoproteinase, which cleaves peptide bonds at the carboxyl side of lysine. ...
0004252 serine-type endopeptidase activity), small molecule metabolic processes (GO:0009132 nucleoside diphosphate metabolic ...
Serine Endopeptidases. *RNA, Messenger. *Myocardium. *Molecular Sequence Data. *Mast Cells. *Immunology. *Humans ...
Serine Endopeptidases 1 * Serine proteinase 1 * Shell extracts 1 * Shell matrix 1 ...
Predicted to enable serine-type endopeptidase inhibitor activity. Predicted to act upstream of or within blood coagulation. ...
Serine-type endopeptidase activity. Specific Function. Factor Xa is a vitamin K-dependent glycoprotein that converts ... Factor Xa is needed to activate prothrombin (factor II) to thrombin (factor IIa). Thrombin is a serine protease that is ...
Serine-type endopeptidase activity. Specific Function. Factor Xa is a vitamin K-dependent glycoprotein that converts ...
Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, ... Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, ...
Serine Endopeptidases (1989-2004). Public MeSH Note:. 2005; ATP-DEPENDENT PROTEASE was indexed under SERINE ENDOPEPTIDASES and ...
  • IgA protease (EC, IgA-specific serine endopeptidase, IgA proteinase, IgA-specific proteinase, immunoglobulin A protease, immunoglobulin A proteinase) is an enzyme. (
  • The structure of the superantigen exfoliative toxin A suggests a novel regulation as a serine protease. (
  • It is a serine protease ( EC ) found on endothelial cells , the cells that line the blood vessels . (
  • The prohormone-processing yeast KEX2 protease can act as an intracellular membrane protein or a soluble, secreted endopeptidase. (
  • Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease. (
  • Thrombin is a serine protease that is required to activate fibrinogen to fibrin, which is the loose meshwork that completes the clotting process. (
  • A serine protease found in the azurophil granules of NEUTROPHILS. (
  • The gene ontology (GO) terms associated with monooxygenase, iron binding, and passive transmembrane transporter activities were significantly enriched in four out of six resistant vs. susceptible comparisons while serine protease activity was elevated in all insecticide-resistant groups relative to the susceptible strain. (
  • An exciting finding is that in approximately half of the cases, there are recurrent chromosomal rearrangements resulting in the fusion of transmembrane protease serine 2 (TMPRSS2 ) and a member of the ETS family transcription factors , most commonly ERG . (
  • The catalytic activity of the serine proteases from the trypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which itself is hydrogen-bonded to a serine. (
  • Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases. (
  • They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation. (
  • Activates serine proteases such as elastase, cathepsin g and granzymes a and b. (
  • ClpP: a distinctive family of cylindrical energy-dependent serine proteases. (
  • Predicted to enable serine-type endopeptidase inhibitor activity. (
  • This gene encodes a member of the serpin superfamily of serine proteinase inhibitors. (
  • A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. (
  • Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues. (
  • Predicted to be involved in negative regulation of endopeptidase activity and response to xenobiotic stimulus. (
  • There is also an IgA-specific prolyl endopeptidase of serine-type (see EC ). (
  • Degradation of matrix extracellular phosphoglycoprotein (MEPE) and DMP-1 and release of acidic serine-rich and aspartate-rich MEPE-associated motif (ASARM) peptides are chiefly responsible for the hypophosphatemic rickets mineralization defect and changes in osteoblast-osteoclast differentiation. (
  • The product peptides derived from the endopeptidase activities of BoNTs are detected by matrix-assisted laser-desorption ionization time-of-flight mass spectrometry. (
  • Furin (PACE, paired basic amino acid cleaving enzyme, membrane associated receptor protein) is serine endoprotease responsible for processing a variety of substrates (proparathyroid hormone, transforming growth factor beta 1 precursor, proalbumin, pro-beta-secretase, membrane type-1 matrix metalloproteinase, beta subunit of pro-nerve growth factor and von Willebrand factor). (
  • Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known. (
  • X-linked hypophosphatemic rickets and autosomal recessive hypophosphatemic rickets are the result of mutations in PHEX (a phosphate-regulating gene with homologies to endopeptidases on the X chromosome) and dentin matrix protein 1 ( DMP1 ), respectively. (
  • Topoisomerase I-binding arginine-serine-rich prote. (
  • A serine endopeptidase that has specificity for cleavage at ARGININE. (
  • Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis. (
  • IgA protease (EC, IgA-specific serine endopeptidase, IgA proteinase, IgA-specific proteinase, immunoglobulin A protease, immunoglobulin A proteinase) is an enzyme. (
  • This gene encodes a member of the serpin superfamily of serine proteinase inhibitors. (
  • A serine protease which inactivates nucleases Biomolecule/Target: Proteinase K, Recombinant, NGS Grade Alternates names: Protease K, Endopeptidase K, Tritirachium. (
  • Aprotinin is a serine protease inhibitor used to reduce the risk for perioperative blood loss and the need for blood transfusion in high-risk patients during cardiopulmonary bypass for coronary artery bypass graft surgery. (
  • The human corticosteroid binding globulin gene is located on chromosome 14q31-q32.1 near two other serine protease inhibitor genes. (
  • Encodes AtSBT1.1, a subtilisin-like serine protease. (
  • We found that several putative ruminopeptins inhibited the S. aureus glutamyl endopeptidase SspA (also known as endoproteinase GluC or V8 protease). (
  • We targeted three human proteins namely ACE2, Interleukin-6, Transmembrane serine protease and NRP1 which are already reported to be damaged via Covid-19 proteins and upregulated in the post-Covid stage. (
  • This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a post-proline bond. (
  • histidine (His 57), serine (Ser 195) (hence the name "serine protease") and aspartic acid (Asp 102). (
  • Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. (
  • X-linked hypophosphatemic rickets and autosomal recessive hypophosphatemic rickets are the result of mutations in PHEX (a phosphate-regulating gene with homologies to endopeptidases on the X chromosome) and dentin matrix protein 1 (DMP1), respectively. (
  • Subtilisin is evolutionary unrelated to the chymotrypsin-clan, but shares the same catalytic mechanism utilising a catalytic triad , to create a nucleophilic serine . (
  • The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all serine protease enzymes. (
  • The serine has an -OH group that is able to act as a nucleophile , attacking the carbonyl carbon of the scissile peptide bond of the substrate. (
  • A pair of electrons on the histidine nitrogen has the ability to accept the hydrogen from the serine -OH group, thus coordinating the attack of the peptide bond . (