• NS2 is a 217 amino acids (aa) long cysteine-protease composed of a highly hydrophobic N-terminal membrane binding domain (MBD) and a C-terminal globular and cytosolic protease domain. (expasy.org)
  • In this study we report examples of MMTS application in experiments involving oxidoreductase (glyceraldehyde-3-phosphate dehydrogenase, GAPDH), redox-regulated protein (recoverin) and cysteine protease (triticain-α). (bvsalud.org)
  • Furthermore, using the example of the papain-like enzyme triticain-α, we report a novel application of MMTS as a protector of the primary structure of active cysteine protease during long-term purification and refolding procedures. (bvsalud.org)
  • Cruzain is the major cysteine protease involved in the survival of this parasite. (bvsalud.org)
  • One of these proteins is the fibroblast activation protein (FAP), a type II transmembrane serine protease with both dipeptidyl peptidase activity and endopeptidase activity ( 2 - 4 ). (snmjournals.org)
  • Caricain is regarded as a cysteine endopeptidase, that is, it functions through the action of a cysteine residue at its active site and it is capable of hydrolysing peptide bonds that are well within the N-terminus and C-terminus of the substrate. (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)
  • 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)
  • 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)
  • Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). (cathdb.info)
  • The propeptide domain contains a cysteine residue that binds zinc in the active site to form the cysteine switch. (periobasics.com)
  • Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. (embl.de)
  • Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. (embl.de)
  • Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. (embl.de)
  • These groups include: serine proteinases, cysteine (thiol) proteinases, aspartic proteinases, and matrix metalloproteinases (MMPs). (stratech.co.uk)
  • Metzincins are a ubiquitously expressed family of multi-domain zinc (II)-dependent endopeptidases (Stocker and Bode 1995 ), the members of which include well-known metalloproteases such as the matrix metalloproteases (MMPs) (Nagase and Woessner 1999 ), a disintegrin and metalloproteases (ADAMs) (White 2003 ), the ADAMs with a thrombospondin motif (ADAMTS) (Tang 2001 ), the bacterial serralysins (Nakahama et al. (evelinvahter.com)
  • Ubiquitin carboxyl-terminal hydrolases (UCH) ( EC 3.1.2.12 ) [ ( PUBMED:1647207 ) ] are thiol proteases that recognise and hydrolyse the peptide bond at the C-terminal glycine of ubiquitin. (embl.de)
  • Asparaginyl endopeptidases (AEPs) are cysteine proteases of the C13 family (clan CD) that cleave at the carboxyl-terminal side of Asx (Asp or Asn). (silverchair.com)
  • Launch Calpain 3 (CAPN3) belongs to a Rabbit polyclonal to CDH1 family group of Ca2+- turned on natural cysteine proteinases which have been discovered in a multitude of microorganisms as disparate as human beings and worms (1,2). (exposed-skin-care.net)
  • The power of the thiol proteinases to cleave a multitude of substrates in response to calcium mineral activation allows their involvement in a variety of cell processes offering cell motility, sign transduction, apoptosis, cell differentiation and legislation of the cytoskeleton (3). (exposed-skin-care.net)
  • Some of them can detach the terminal amino acids from the protein chain (exopeptidases, such as aminopeptidases, carboxypeptidase A), while others attack internal peptide bonds of a protein (endopeptidases, such as trypsin, chymotrypsin, pepsin, papain and elastase). (stratech.co.uk)
  • Asparaginyl endopeptidases (AEPs) are versatile enzymes that in biological systems are involved in producing three different catalytic outcomes for proteins, namely (i) routine cleavage by bond hydrolysis, (ii) peptide maturation, including macrocyclisation by a cleavage-coupled intramolecular transpeptidation and (iii) circular permutation involving separate cleavage and transpeptidation reactions resulting in a major reshuffling of protein sequence. (silverchair.com)
  • The binding of cysteine in the catalytic domain blocks the active zinc site, maintaining the latent or inactive state 4 . (periobasics.com)
  • The protein is 216 amino acids in length, and is 68% identical in sequence to papain, 65% to chymopapain and 81% to glycyl endopeptidase. (wikipedia.org)
  • S-Methyl methanethiosulfonate (MMTS) is used in experimental biochemistry for alkylating thiol groups of protein cysteines. (bvsalud.org)
  • Additional benefits include good accessibility of MMTS to buried protein cysteines due to its small size and the simplicity of the protection and deprotection procedures. (bvsalud.org)
  • We demonstrate that on the one hand MMTS can modify functional cysteines in the thiol enzyme GAPDH, thereby preventing thiol oxidation and reversibly inhibiting the enzyme, while on the other hand it can protect the redox-sensitive thiol group of recoverin from oxidation and such modification produces no impact on the activity of the protein. (bvsalud.org)
  • Covalent chromatography on thiol-Sepharose allows isolation of fully active caricain from the material obtained by cation exchange. (wikipedia.org)
  • Oxidized cysteine residues are highly reactive and can form functional covalent conjugates, of which the allosteric redox switch formed by the lysine-cysteine NOS bridge is an example. (hokudai.ac.jp)
  • The reagent can also be employed as an inhibitor of enzymatic activity, since nucleophilic cysteine thiolates are commonly present at active sites of various enzymes. (bvsalud.org)
  • Effect: May oxidize thiol groups in essential enzymes systems. (enzytec.com)
  • Cysteine peptidases with an intein-like fold are included in clan PD, which also includes asparagine lyases. (embl.de)
  • Its applications include mainly trapping of natural thiol-disulfide states of redox-sensitive proteins and proteins which have undergone S-nitrosylation. (bvsalud.org)
  • Based on the data, we propose new lines of MMTS employment in research, pharmaceuticals and biotechnology for reversible switching off of undesirable activity and antioxidant protection of proteins with functional thiol groups. (bvsalud.org)
  • As with some other plant cysteine endopeptidases, caricain exhibits charge heterogeneity. (wikipedia.org)
  • 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)
  • L-cysteine methyl ester was detected by UPLC-MS in stones from your CDME group only indicating that a CDME metabolite was incorporated into the crystal structure. (exposed-skin-care.net)
  • The active-site sulfur requires reduction for catalytic competence, and this is best achieved by the inclusion of low millimolar concentrations of cysteine in assay buffers. (wikipedia.org)
  • The highly basic character of caricain makes it relatively easy to separate from the other papaya cysteine endopeptidases in cation-exchange chromatography of preparations of commercially available papaya latex. (wikipedia.org)
  • Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. (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)
  • The peptidase family C21 domain is a papain-like proteinase with catalytic cysteine and histidine residues. (expasy.org)
  • CRPs are classified into different families according to the number of cysteine residues and their disulfide connectivity [ 4 ]. (biomedcentral.com)
  • Folding is driven by formation of the C3-C5 bridge and is supported by residues lying within the segment delimited by these cysteines. (cnr.it)
  • Data altogether support a mechanism whereby the Cripto-1 CFC domain refolds by virtue of long-range intramolecular interactions that involve residues close to cysteines of the second and third bridge. (cnr.it)
  • Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). (cathdb.info)
  • Mammalian metallothioneins (MTs) are small (6-7 kDa), intracellular, cysteine-rich, metal-binding proteins involved, inter alia, in the homeostasis of zinc and copper, detoxification of heavy metals, antioxidation against reactive oxygen species, and protection against DNA damage. (biomedcentral.com)
  • Mammalian metallothioneins (MTs) are a family of small (6-7 kDa), intracellular, cysteine-rich metal-binding proteins [ 1 ]. (biomedcentral.com)
  • Calpains are nonlysosomal intracellular cysteine proteases expressed ubiquitously in mammals and other organisms. (anaspec.com)
  • Jasmintides jS1 and jS2 from Jasminum sambac were previously identified as a novel family of cysteine-rich peptides (CRPs) with an unusual disulfide connectivity. (biomedcentral.com)
  • Peptidomic analysis, using fractionated mixtures of jasmintides and chemical derivatization of cysteine to pseudolysine, trypsin digestion and MS/MS sequencing, revealed an additional 86 jasmintides, some of which were post-translationally modified. (biomedcentral.com)
  • MMPs are Zn 2+ -dependent endopeptidases that cause degradation of different protein substrates in the extracellular matrix (ECM). (oaepublish.com)
  • The protein is 216 amino acids in length, and is 68% identical in sequence to papain, 65% to chymopapain and 81% to glycyl endopeptidase. (wikipedia.org)