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.
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.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
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.
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 subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
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.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
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).
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC
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.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
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.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
The process of cleaving a chemical compound by the addition of a molecule of water.
The rate dynamics in chemical or physical systems.
Peptides composed of two amino acid units.
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
A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
Compounds containing the -SH radical.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. (1/6256)

The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The first subdomain is an alpha-helix-beta-strand arrangement, whereas the second subdomain has a predominantly beta-strand arrangement. The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. This enables inhibitors based on the thyroglobulin type-1 domain fold, in contrast to the rather non-selective cystatins, to exhibit specificity for their target enzymes.  (+info)

C/EBPalpha regulates generation of C/EBPbeta isoforms through activation of specific proteolytic cleavage. (2/6256)

C/EBPalpha and C/EBPbeta are intronless genes that can produce several N-terminally truncated isoforms through the process of alternative translation initiation at downstream AUG codons. C/EBPbeta has been reported to produce four isoforms: full-length 38-kDa C/EBPbeta, 35-kDa LAP (liver-enriched transcriptional activator protein), 21-kDa LIP (liver-enriched transcriptional inhibitory protein), and a 14-kDa isoform. In this report, we investigated the mechanisms by which C/EBPbeta isoforms are generated in the liver and in cultured cells. Using an in vitro translation system, we found that LIP can be generated by two mechanisms: alternative translation and a novel mechanism-specific proteolytic cleavage of full-length C/EBPbeta. Studies of mice in which the C/EBPalpha gene had been deleted (C/EBPalpha-/-) showed that the regulation of C/EBPbeta proteolysis is dependent on C/EBPalpha. The induction of C/EBPalpha in cultured cells leads to induced cleavage of C/EBPbeta to generate the LIP isoform. We characterized the cleavage activity in mouse liver extracts and found that the proteolytic cleavage activity is specific to prenatal and newborn livers, is sensitive to chymostatin, and is completely abolished in C/EBPalpha-/- animals. The lack of cleavage activity in the livers of C/EBPalpha-/- mice correlates with the decreased levels of LIP in the livers of these animals. Analysis of LIP production during liver regeneration showed that, in this system, the transient induction of LIP is dependent on the third AUG codon and most likely involves translational control. We propose that there are two mechanisms by which C/EBPbeta isoforms might be generated in the liver and in cultured cells: one that is determined by translation and a second that involves C/EBPalpha-dependent, specific proteolytic cleavage of full-length C/EBPbeta. The latter mechanism implicates C/EBPalpha in the regulation of posttranslational generation of the dominant negative C/EBPbeta isoform, LIP.  (+info)

An antiviral mechanism of nitric oxide: inhibition of a viral protease. (3/6256)

Although nitric oxide (NO) kills or inhibits the replication of a variety of intracellular pathogens, the antimicrobial mechanisms of NO are unknown. Here, we identify a viral protease as a target of NO. The life cycle of many viruses depends upon viral proteases that cleave viral polyproteins into individual polypeptides. NO inactivates the Coxsackievirus protease 3C, an enzyme necessary for the replication of Coxsackievirus. NO S-nitrosylates the cysteine residue in the active site of protease 3C, inhibiting protease activity and interrupting the viral life cycle. Substituting a serine residue for the active site cysteine renders protease 3C resistant to NO inhibition. Since cysteine proteases are critical for virulence or replication of many viruses, bacteria, and parasites, S-nitrosylation of pathogen cysteine proteases may be a general mechanism of antimicrobial host defenses.  (+info)

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (4/6256)

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport.  (+info)

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. (5/6256)

The role of conformation-based quality control in the early secretory pathway is to eliminate misfolded polypeptides and unassembled multimeric protein complexes from the endoplasmic reticulum, ensuring the deployment of only functional molecules to distal sites. The intracellular fate of terminally misfolded human alpha1-antitrypsin was examined in hepatoma cells to identify the functional role of asparagine-linked oligosaccharide modification in the selection of glycoproteins for degradation by the cytosolic proteasome. Proteasomal degradation required physical interaction with the molecular chaperone calnexin. Altered sedimentation of intracellular complexes following treatment with the specific proteasome inhibitor lactacystin, and in combination with mannosidase inhibition, revealed that the removal of mannose from attached oligosaccharides abrogates the release of misfolded alpha1-antitrypsin from calnexin prior to proteasomal degradation. Intracellular turnover was arrested with kifunensine, implicating the participation of endoplasmic reticulum mannosidase I in the disposal process. Accelerated degradation occurred in a mannosidase-independent manner and was arrested by lactacystin, in response to the posttranslational inhibition of glucosidase II, demonstrating that the attenuated removal of glucose from attached oligosaccharides functions as the underlying rate-limiting step in the proteasome-mediated pathway. A model is proposed in which the removal of mannose from multiple attached oligosaccharides directs calnexin in the selection of misfolded alpha1-antitrypsin for degradation by the proteasome.  (+info)

Possible involvement of proteasomes (prosomes) in AUUUA-mediated mRNA decay. (6/6256)

We have identified a cellular target for proteasomal endonuclease activity. Thus, 20 S proteasomes interact with the 3'-untranslated region of certain cytoplasmic mRNAs in vivo, and 20 S proteasomes isolated from Friend leukemia virus-infected mouse spleen cells were found to be associated with a mRNA fragment showing great homology to the 3'-untranslated region of tumor necrosis factor-beta mRNA that contains AUUUA sequences. We furthermore demonstrate that 20 S proteasomes destabilize oligoribonucleotides corresponding to the 3'-untranslated region of tumor necrosis factor-alpha, creating a specific cleavage pattern. The cleavage reaction is accelerated with increasing number of AUUUA motifs, and major cleavage sites are localized at the 5' side of the A residues. These results strongly suggest that 20 S proteasomes could be involved in the destabilization of cytokine mRNAs such as tumor necrosis factor mRNAs and other short-lived mRNAs containing AUUUA sequences.  (+info)

Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia. (7/6256)

The formation of a persistently active cAMP-dependent protein kinase (PKA) is critical for establishing long-term synaptic facilitation (LTF) in Aplysia. The injection of bovine catalytic (C) subunits into sensory neurons is sufficient to produce protein synthesis-dependent LTF. Early in the LTF induced by serotonin (5-HT), an autonomous PKA is generated through the ubiquitin-proteasome-mediated proteolysis of regulatory (R) subunits. The degradation of R occurs during an early time window and appears to be a key function of proteasomes in LTF. Lactacystin, a specific proteasome inhibitor, blocks the facilitation induced by 5-HT, and this block is rescued by injecting C subunits. R is degraded through an allosteric mechanism requiring an elevation of cAMP coincident with the induction of a ubiquitin carboxy-terminal hydrolase.  (+info)

Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance. (8/6256)

PML/RARalpha is the leukemogenetic protein of acute promyelocytic leukemia (APL). Treatment with retinoic acid (RA) induces degradation of PML/RARalpha, differentiation of leukaemic blasts, and disease remission. However, RA resistance arises during RA treatment of APL patients. To investigate the phenomenon of RA resistance in APL, we generated RA-resistant sublines from APL-derived NB4 cells. The NB4.007/6 RA-resistant subline does not express the PML/RARalpha protein, although its mRNA is detectable at levels comparable to those of the parental cell line. In vitro degradation assays showed that the half-life of PML/RARalpha is less than 30 minutes in NB4.007/6 and longer than 3 hours in NB4. Treatment of NB4.007/6 cells with the proteasome inhibitors LLnL and lactacystin partially restored PML/RARalpha protein expression and resulted in a partial release of the RA-resistant phenotype. Similarly, forced expression of PML/RARalpha, but not RARalpha, into the NB4/007.6 cells restored sensitivity to RA treatment to levels comparable to those of the NB4 cells. These results indicate that constitutive degradation of PML/RARalpha protein may lead to RA resistance and that PML/RARalpha expression is crucial to convey RA sensitivity to APL cells.  (+info)

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.

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.

Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.

Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.

Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.

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.

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.

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.

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 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.

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).

Cysteine proteases are a type of enzymes that cleave peptide bonds in proteins, and they require a cysteine residue in their active site to do so. These enzymes play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They can be found in various tissues and organisms, including humans, where they are involved in many physiological and pathological conditions.

Cysteine proteases are characterized by a conserved catalytic mechanism that involves a nucleophilic attack on the peptide bond carbonyl carbon by the thiolate anion of the cysteine residue, resulting in the formation of an acyl-enzyme intermediate. This intermediate is then hydrolyzed to release the cleaved protein fragments.

Some examples of cysteine proteases include cathepsins, caspases, and calpains, which are involved in various cellular processes such as apoptosis, autophagy, and signal transduction. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, cysteine proteases have emerged as important therapeutic targets for the development of new drugs to treat these conditions.

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.

Cysteine proteinase inhibitors are a type of molecule that bind to and inhibit the activity of cysteine proteases, which are enzymes that cleave proteins at specific sites containing the amino acid cysteine. These inhibitors play important roles in regulating various biological processes, including inflammation, immune response, and programmed cell death (apoptosis). They can also have potential therapeutic applications in diseases where excessive protease activity contributes to pathology, such as cancer, arthritis, and neurodegenerative disorders. Examples of cysteine proteinase inhibitors include cystatins, kininogens, and serpins.

Cysteine dioxygenase (CDO) is an enzyme that catalyzes the conversion of the amino acid L-cysteine to L-cysteinesulfinic acid, which is the first step in the catabolism of L-cysteine. This reaction also generates molecular oxygen as a byproduct. CDO plays important roles in various biological processes such as neurotransmitter biosynthesis and oxidative stress response. It exists as two isoforms, CDO1 and CDO2, which are encoded by separate genes and have distinct tissue distributions and functions.

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.

Cysteine synthase is an enzyme involved in the biosynthesis of the amino acid cysteine. It catalyzes the reaction that combines O-acetylserine and hydrogen sulfide to produce cysteine and acetic acid. This enzyme plays a crucial role in maintaining the sulfur balance in cells, as cysteine is a sulfur-containing amino acid that is an important component of proteins and many other molecules in the body. There are two forms of cysteine synthase: one that is found in bacteria and plants, and another that is found in animals. The animal form of the enzyme is also known as cystathionine beta-synthase, and it has a broader specificity than the bacterial and plant forms, as it can also catalyze the reaction that produces cystathionine from serine and homocysteine.

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.

Disulfides are a type of organic compound that contains a sulfur-sulfur bond. In the context of biochemistry and medicine, disulfide bonds are often found in proteins, where they play a crucial role in maintaining their three-dimensional structure and function. These bonds form when two sulfhydryl groups (-SH) on cysteine residues within a protein molecule react with each other, releasing a molecule of water and creating a disulfide bond (-S-S-) between the two cysteines. Disulfide bonds can be reduced back to sulfhydryl groups by various reducing agents, which is an important process in many biological reactions. The formation and reduction of disulfide bonds are critical for the proper folding, stability, and activity of many proteins, including those involved in various physiological processes and diseases.

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.

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.

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.

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.

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.

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.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.

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.

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.

This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. The various forms of peptidase 1 ... which bind to the cysteine active site and block substrate access. The major kiwifruit cysteine proteinase inhibitor KCPI1 has ... As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the ... By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that ...
... is regarded as a cysteine endopeptidase, that is, it functions through the action of a cysteine residue at its active ... The highly basic character of caricain makes it relatively easy to separate from the other papaya cysteine endopeptidases in ... As with some other plant cysteine endopeptidases, caricain exhibits charge heterogeneity. This may be partly due to variation ... The specificities of three cysteine endopeptidases from papaya latex were found to be very similar. Caricain and chymopapain ...
The protein is a human cysteine cathepsin, a lysosomal cysteine protease with endopeptidase activity. The protein is a member ... a lysosomal cysteine protease with endopeptidase activity. It may play an important role in corneal physiology. This gene is ... 2005). "The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles". ... Santamaría I, Velasco G, Cazorla M, Fueyo A, Campo E, López-Otín C (April 1998). "Cathepsin L2, a novel human cysteine ...
Takahashi K, Nishii W, Shibata C (2012). "The digestive fluid of Drosera indica contains a cysteine endopeptidase ("droserain ... The names cephalotusin, dionaeasin and droserasin have been proposed for similar aspartic endopeptidases originating from the ...
... it contains a cysteine endopeptidase mixture especially present in immature fruits that is used commercially by the ...
... clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Lett. 441 (3): 361-5. doi:10.1016/S0014-5793(98) ... 1999). "An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation". Nature. 396 (6712): 695-9. ... Tanaka T, Inazawa J, Nakamura Y (Dec 1996). "Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and ... This gene encodes a cysteine protease, legumain, that has a strict specificity for hydrolysis of asparaginyl bonds. This enzyme ...
... is synthesized as an inactive zymogen. AEP and other cysteine peptidase are activated when pH changes ... Legumain is a cysteine protease from the C13 family of the CD clan of proteases (MEROPS). It uses a catalytic triad of Cysteine ... hence also called cysteine protease). It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 ... clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Letters. 441 (3): 361-5. doi:10.1016/S0014-5793(98) ...
... is cleaved by several proteases including Separase and Calcium-dependent cysteine endopeptidase Calpain-1 during mitosis ... and its dissolution by the cysteine protease Separase at the metaphase to anaphase transition results in the separation of ...
Shows weak endopeptidase activity Cathepsin X is a cysteine cathepsin, a lysosomal cysteine peptidase of family C1 (papain ... Santamaría I, Velasco G, Pendás AM, Fueyo A, López-Otín C (July 1998). "Cathepsin Z, a novel human cysteine proteinase with a ... Nägler DK, Ménard R (August 1998). "Human cathepsin X: a novel cysteine protease of the papain family with a very short ... Cathepsin X (EC, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ...
... is also known to play a role in axon regeneration and has an additional DISC1-modulated function as a cysteine endopeptidase. ...
Birktoft, Jens J.; Breddam, Klaus (1994). "[8] Glutamyl endopeptidases". Proteolytic Enzymes: Serine and Cysteine Peptidases. ... subtilis glutamyl endopeptidase GluBS Enterococcus E. faecalis glutamyl endopeptidase SprE Glutamyl endopeptidase is in at ... S. epidermidis glutamyl endopeptidase GluSE Also called S. epidermidis serine protease (Esp). S. warneri glutamyl endopeptidase ... Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been ...
Glutamyl endopeptidase proteolytically activates the zymogen of the cysteine protease staphopain B (staphopain A is activated ... 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 ...
The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases Cysteine+endopeptidases at the U.S. ... In fact, the latex of dozens of different plant families are known to contain cysteine proteases. Cysteine proteases are used ... Plant cysteine proteases isolated from these plants have been found to have high proteolytic activities that are known to ... Cysteine proteases are used as feed additives for livestock to improve the digestibility of proteins and amino acids. Protease ...
... prolyl endopeptidase and a barley glutamine-specific cysteine endopeptidase (EP-B2)) that degrade the putative 33-mer peptide ...
... cysteine endopeptidases MeSH D08.811.277.656.300.215.096 - bromelains MeSH D08.811.277.656.300.215.120 - calpain 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 ... 300.066 - aspartic endopeptidases MeSH D08.811.277.656.300.066.180 - cathepsin d MeSH D08.811.277.656.300.066.185 - cathepsin e ...
... paired-basic endopeptidase, yeast cysteine proteinase F, paired-basic endopeptidase, andrenorphin-Gly-generating enzyme, ... Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (October 1988). "Yeast KEX2 genes encodes an endopeptidase homologous to ... Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (February 1989). "Characterization of KEX2-encoded endopeptidase from yeast ... "Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast ...
This enzyme is secreted cysteine endopeptidase from the bacterium Porphyromonas gingivalis. Gingipain Gingipain K Chen Z, ... arginine-specific cysteine protease, arginine-specific gingipain, arginine-specific gingivain, RGP-1, RGP) is an enzyme. This ... Potempa J, Polanowski A, Wikstrom M, Travis J (September 1992). "Purification and characterization of a 50-kDa cysteine ... a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase ...
This cysteine endopeptidase is encoded by adenoviruses. Webster A, Hay RT, Kemp G (January 1993). "The adenovirus protease is ...
... (EC, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine ... Bazan JF, Fletterick RJ (November 1988). "Viral cysteine proteases are homologous to the trypsin-like family of serine ... TEV protease uses a cysteine as its catalytic nucleophile (as do many other viral proteases). Covalent catalysis is performed ...
Buttle DJ, Kembhavi AA, Sharp SL, Shute RE, Rich DH, Barrett AJ (July 1989). "Affinity purification of the novel cysteine ... Glycyl+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.22). ... Glycyl endopeptidase (EC, papaya peptidase B, papaya proteinase IV, glycine-specific proteinase, chymopapain, Papaya ...
It is a member of the cysteine cathepsin family of cysteine proteases, which has 11 members. As one of the 11 cathepsins, ... It is an exopeptidase with strict carboxypeptidase activity, while most other cathepsins are endopeptidases. Cathepsin Z has an ... a cysteine protease with the proregion covalently linked to the active site cysteine". Journal of Molecular Biology. 295 (4): ... Santamaría I, Velasco G, Pendás AM, Fueyo A, López-Otín C (July 1998). "Cathepsin Z, a novel human cysteine proteinase with a ...
... inhibitor of cysteine proteases Camostat - inhibitor of trypsin and various other proteases Ecallantide - kallikrein inhibitor ... 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 ...
C-aaX in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the ... Ste24+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.24). ... Ste24 endopeptidase (EC is an enzyme. This enzyme catalyses the following chemical reaction The peptide bond ...
... calicivirus trypsin-like cysteine protease, calicivirus TCP, calicivirus 3C-like protease, calicivirus endopeptidase, rabbit ... Meyers G, Rossi C, Thiel HJ (2004). "Calicivirus endopeptidases". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of ... This enzyme catalyses the following chemical reaction Endopeptidase with a preference for cleavage when the P1 position is ... hemorrhagic disease virus 3C endopeptidase) is an enzyme. ...
... cysteine; G, glutamic acid; M, metallo; S, serine; T, threonine; and U, unknown. The serine, threonine and cysteine peptidases ... These endopeptidases include CAAX prenyl protease 1, which proteolytically removes the C-terminal three residues of ... There are two subgroups of metalloproteinases: Exopeptidases, metalloexopeptidases (EC number: 3.4.17). Endopeptidases, ...
This enzyme catalyses the following chemical reaction Broad endopeptidase specificity This enzyme belongs to the peptidase ... is an intracellular heterodimeric calcium-activated cysteine protease. ...
This endopeptidase has a length of 419 amino acid residues. The metalloproteinase disintegrin-like domain and the cysteine-rich ... The cysteine-rich domain was shown to have two sequences that cause an interaction which prevents alpha-2/beta-1 integrin ... Research suggests that the RSECD cysteine residue at positions 272-276 must be involved in a disulfide bond for the enzyme to ... This suggests that there may be an interaction between the disintegrin-like domain, and cysteine-rich domain of atrolysin A and ...
The enzyme lysyl endopeptidase was isolated from A. lyticus. Uniprot Straininfo of Achromobacter lyticus Uniprot Methods in ... 244 Proteolytic Enzymes: Serine and Cysteine Peptidases Serogrouping Single Colonies of Beta-hemolytic Streptococci with ...
... s (or papain-like (cysteine) peptidases; abbreviated PLP or PLCP) are a large protein family of cysteine ... Papain-like proteases are usually endopeptidases, but some members of the group are also, or even exclusively, exopeptidases. ... which includes cysteine, serine, and aspartic proteases). In humans, there are 11 cysteine cathepsins: B, C, F, H, K, L, O, S, ... Cysteine cathepsins are also part of the normal life cycle of the unicellular parasite Leishmania, where they function as ...
Serine, threonine, and cysteine proteases use a nucleophilic residue (usually in a catalytic triad). That residue performs a ... endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). Catalysis is achieved by one of two mechanisms: ... One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine, or ... The mechanism used to cleave a peptide bond involves making an amino acid residue that has the cysteine and threonine ( ...
This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. The various forms of peptidase 1 ... which bind to the cysteine active site and block substrate access. The major kiwifruit cysteine proteinase inhibitor KCPI1 has ... As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the ... By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that ...
enables calcium-dependent cysteine-type endopeptidase activity IBA Inferred from Biological aspect of Ancestor. more info ... enables calcium-dependent cysteine-type endopeptidase activity ISO Inferred from Sequence Orthology. more info ... Predicted to enable SNARE binding activity; calcium-dependent cysteine-type endopeptidase activity; and cytoskeletal protein ... enables cysteine-type peptidase activity IEA Inferred from Electronic Annotation. more info ...
Trematode cysteine endopeptidases.. Robinson, M., Brindley, P. J., McKerrow, J. H. & Dalton, J., 2013, Handbook of Proteolytic ... The cathepsin-like cysteine peptidases of trematodes of the genus Fasciola. Cwiklinski, K., Donnelly, S., Drysdale, O., ...
Cysteine protease inhibitor/serine-type endopeptidase inhibitor. M15. Y239. * In the 3D structure as revealed by using Jmol ... especially concerning the amino acids cysteine (Cys) and methionine (Met), whose side chains contain a sulfur atom [13,14,15]. ...
... and cysteine-type endopeptidase activity involved in the apoptotic signaling pathway. KEGG analysis showed that DEIOSGs were ... Molecular functions results suggested that DEIOSGs were notably linked to endopeptidase activity, heme binding, protease ...
The ability of G protein-coupled receptors (GPCRs) to initiate complex cascades of cellular signaling is governed by the sequential coupling of three main transducer proteins, G protein, GPCR kinase (GRK), and β-arrestin. Mounting evidence indicates these transducers all have distinct conformational preferences and binding modes. However, interrogating each transducers mechanism of interaction with GPCRs has been complicated by the interplay of transducer-mediated signaling events. For example, GRK-mediated receptor phosphorylation recruits and induces conformational changes in β-arrestin, which facilitates coupling to the GPCR transmembrane core. Here we compare the allosteric interactions of G proteins and β-arrestins with GPCRs transmembrane cores by using the enzyme sortase to ligate a synthetic phosphorylated peptide onto the carboxyl terminus of three different receptors. Phosphopeptide ligation onto the β2-adrenergic receptor (β2AR) allows stabilization of a high-affinity receptor ...
cysteine-type endopeptidase activity. IEP. Enrichment. MF. GO:0004198. calcium-dependent cysteine-type endopeptidase activity. ...
cysteine-type endopeptidase activity. GO:0008234. cysteine-type peptidase activity. GO:0008233. peptidase activity. ...
cysteine-type endopeptidase activity. IEP. Enrichment. MF. GO:0005506. iron ion binding. IEP. Enrichment. ...
calcium-dependent cysteine-type endopeptidase activity. GO:0005102. receptor binding. GO:0005246. calcium channel regulator ...
L), is a cysteine protease of the plant endopeptidase family. In terms of activity, this enzyme mimics the activity of the ...
Alternative Names: AEP; Asparaginyl endopeptidase; cysteine 1; Cysteine protease 1; EC; Legumain; LGMN; LGMN_HUMAN; ...
... ubiquitin-specific peptidases and many families of viral cysteine endopeptidases. Calpain is a protein of ancient origin with ... Calpain (EC is a Ca2+-dependent cysteine protease first isolated in 1978, with a pH optimum between 7.0 and 8.0. ... The catalytic domain is divided into two subdomains (2a and 2b) with the cysteine residue lying in domain 2a and the histidine ... and evolved from a gene fusion event between an N-terminal cysteine protease and a C-terminal calmodulin-like protein, an event ...
cysteine-type endopeptidase activity [IBA]. Gene Ontology Cellular Component. *cytoplasm [IBA]*extracellular vesicular exosome ...
The membrane-bound form of the protein can be cleaved by specific CYSTEINE ENDOPEPTIDASES to form a soluble ligand form. ...
Cysteine Endopeptidases. * Humans. * Inflammation. * Mice. * Models, Molecular. * Multienzyme Complexes. * Neoplasms. * Peptide ...
Cathepsin B, Cathepsin L, Cathepsins, Cell Line, Cysteine Endopeptidases, Enzyme Inhibitors, Hepacivirus, Humans, Hydrogen-Ion ...
CE: Cysteine (C) Peptidases*C48: Ulp1 endopeptidase. *M-: Metallo (M) Peptidases*M79: Prenyl protease 2 ...
Cysteine Endopeptidases, DNA-Binding Proteins, HCT116 Cells, Humans, Mice, Middle Aged, Mutation, Proto-Oncogene Proteins c- ...
Cysteine Endopeptidases *Enzyme Precursors. Plant Cell 1992 Mar;4(3):307-18 proaleurain EC 3.4.22.- *Cysteine Endopeptidases * ... Cysteine Endopeptidases *Enzyme Precursors Plant Proteins. Structure 1996 Oct 15;4(10):1193-203 promatrilysin EC 3.4.24.- * ... Enzyme Precursors *Aspartic Acid Endopeptidases. Nat Struct Biol 1999 Jan;6(1):32-7 procardosin A EC 3.4.23.- *Enzyme ... Enzyme Precursors *Serine Endopeptidases. Eur J Biochem 1997 Apr 15;245(2):392-7 procathepsin K, Ser(139)-. Ala(163) 0 * ...
It has been demonstrated that Trichomonas tenax presents proteolytic activity mediated by cysteine endopeptidases which ...
... cysteine-type endopeptidase activity;0.0253390788372475!GO:0006351;transcription, DNA-dependent;0.0254063787349221!GO:0043022; ... threonine endopeptidase activity;7.11399895366341e-08!GO:0015986;ATP synthesis coupled proton transport;7.11399895366341e-08!GO ... cysteine-type peptidase activity;0.00037935088191711!GO:0003729;mRNA binding;0.000409147122526055!GO:0008094;DNA-dependent ...
COVID-19 Drug Treatment , SARS-CoV-2 , Humans , Antiviral Agents/chemistry , Cysteine Endopeptidases/metabolism , Protease ...
... cysteine-type endopeptidase activity involved in execution phase of apoptosis ...
cysteine. *cysteine endopeptidase. *cysteine hydrochloride. *cysteine sulfinic acid. *cysteine test. *cysteine-type ...
  • Peptidase 1 (mite) (EC, also known as endopeptidase 1 (mite), is an enzyme found in various species of mites. (wikipedia.org)
  • Peptidase 1 is a cysteine protease belonging to the C1 protein family, with a structure similar to that of papain. (wikipedia.org)
  • As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the activation of other allergens. (wikipedia.org)
  • A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. (embl.de)
  • This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. (wikipedia.org)
  • By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that of actinidin and papain. (wikipedia.org)
  • Due to its cysteine protease structure, Der p 1 may be irreversibly inhibited by E-64 or iodoacetamide, which bind to the cysteine active site and block substrate access. (wikipedia.org)
  • Calpain (EC is a Ca 2+ -dependent cysteine protease first isolated in 1978, with a pH optimum between 7.0 and 8.0. (biomedcentral.com)
  • Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. (embl.de)
  • Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. (embl.de)
  • Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. (embl.de)
  • Cysteine peptidases with an intein-like fold are included in clan PD, which also includes asparagine lyases. (embl.de)
  • In only one family of cysteine peptidases, is the role of the general base assigned to a residue other than a histidine: in peptidases from family C89 (acid ceramidase) an arginine is the general base. (embl.de)
  • Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique to the clan. (embl.de)
  • Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. (embl.de)
  • Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. (embl.de)
  • Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. (embl.de)
  • The catalytic domain is divided into two subdomains (2a and 2b) with the cysteine residue lying in domain 2a and the histidine and asparagine in 2b. (biomedcentral.com)
  • The active site consists of a conserved triad of cysteine, asparagine and histidine. (biomedcentral.com)
  • The membrane-bound form of the protein can be cleaved by specific CYSTEINE ENDOPEPTIDASES to form a soluble ligand form. (childrensmercy.org)
  • it replaces the amino acid cysteine with a signal to stop protein production prematurely (written as Cys135Ter or C135X). (medlineplus.gov)
  • Matrix metalloproteinases (MMPs) are a group of structurally related endopeptidases that require a metal cofactor. (medscape.com)
  • Calpains are a family of cytosolic cysteine proteinases. (embl.de)
  • Leupeptin (Ac-Leu-Leu-Arg-al) is really a cell-permeable inhibitor of cysteine proteases. (bio2009.org)
  • 1998 Peptide aldehydes inhibit serine cysteine and threonine proteases. (bio2009.org)
  • 2000 to create Ac-LLR-amc (NC-002) would remove reactivity with lysosomal cysteine proteases keep specificity towards the trypsin-like sites rather than alter cell-permeability from the substance. (bio2009.org)
  • Importantly NC-002 the epoxyketone derivative of the cysteine protease inhibitor leupeptin does not inhibit lysosomal cysteine proteases (Fig. 2e). (bio2009.org)
  • Today, the matrix metalloproteinase (MMP) family, to which this collagenase belongs, has expanded to include 23 gene products in humans (Table 1 ), which encode zinc-dependent and calcium-dependent proteases that cleave within a polypeptide (endopeptidases). (biomedcentral.com)
  • Fmoc-Ala-Glu-Asn-Lys-NH2 is a selective asparagine endopeptidase (AEP) inhibitor peptide and suppresses amyloid precursor protein (APP) cleavage. (boykyo.com.cn)
  • Stops, prevents or reduces the activity of a cysteine-type endopeptidase involved in the apoptotic process. (cathdb.info)
  • From NCBI Gene: Involved in activation of cysteine-type endopeptidase activity. (nih.gov)
  • This was most likely the result of an increase in the gene expression and enzyme activity of L-cysteine desulfhydrase, which is responsible for H2S synthesis. (bvsalud.org)
  • Lysostaphin is a zinc-metalloprotease glycylglycine endopeptidase enzyme originally secreted by Staphylococcus simulans biovar staphylolyticus . (researchsquare.com)
  • ENDOPEPTIDASES which have a cysteine involved in the catalytic process. (nih.gov)
  • Cysteine protease ATG4A, also known as AUT-like 2 cysteine endopeptidase, plays a pivotal role in autophagy, mediating proteolytic activation and delipidation of ATG8 family proteins. (receptor.ai)
  • AEP, a pH-controlled cysteine proteinase, is activated during ageing and mediates APP proteolytic processing [1] . (boykyo.com.cn)