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  • activities
  • Three cysteine-dependent proteolytic activities were separated from a homogenate of mouse calvaria by a fractionation procedure involving (NH4)2SO4 precipitation, gel filtration and ion-exchange chromatography. (biochemj.org)
  • proteins
  • Cysteine proteases , also known as thiol proteases , are enzymes that degrade proteins . (wikipedia.org)
  • For decades, cysteine-based reactions with maleimides and alkyl halides are the primary methods for selectively tagging proteins with fluorescent dyes, affinity and radio labels, drug molecules, and polymers and nanocomposites. (mit.edu)
  • The goal of this thesis is to develop new cysteine arylation reactions to generate sulfur-sp² carbon bonds on proteins. (mit.edu)
  • This entry represents a cysteine-rich domain found in the TACI family of proteins. (ebi.ac.uk)
  • Biochemical analyses of recombinant plant SAT and OAS-TL indicate that the reversible association of the proteins in the cysteine synthase complex (CSC) controls cellular sulfur homeostasis. (mendeley.com)
  • The reactivity is enhanced when the thiol is ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell. (wikipedia.org)
  • The thiol group also has a high affinity for heavy metals, so that proteins containing cysteine, such as metallothionein, will bind metals such as mercury, lead and cadmium tightly. (wikipedia.org)
  • GCL enzymatic activity is influenced by numerous factors, including cellular expression of the GCL subunit proteins, access to substrates (cysteine is typically limiting in the production of γ-GC), the degree of negative feedback inhibition by GSH, and functionally relevant post-translational modifications to specific sites on the GCL subunits. (wikipedia.org)
  • Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins. (wikipedia.org)
  • Cysteine residues are typically oxidised to cystine in proteins, as the formation of disulfide bonds plays an important role in protein folding and the stabilisation of tertiary structure - this is particularly important with proteins secreted to the extracellular medium such as CRISPs. (wikipedia.org)
  • glutathione
  • Cysteine can form glutathione (along with glutamic acid and glycine), a powerful antioxidant and detoxifier that functions in many enzyme systems. (healthy.net)
  • Glutamate cysteine ligase (GCL) catalyzes the first and rate-limiting step in the production of the cellular antioxidant glutathione (GSH), involving the ATP-dependent condensation of cysteine and glutamate to form the dipeptide gamma-glutamylcysteine (γ-GC). (wikipedia.org)
  • nucleophilic
  • First, through a nucleophilic aromatic substitution (SNAr) mechanism, fluorinated aromatic reagents are used for the regioselective arylation of a single cysteine in the presence of many. (mit.edu)
  • protease
  • Reaction mechanism of the cysteine protease mediated cleavage of a peptide bond. (wikipedia.org)
  • Examples of protease inhibitors include: Serpins Stefins IAPs Currently there is no widespread use of cysteine proteases as approved and effective anthelmintics but research into the subject is a promising field of study. (wikipedia.org)
  • molecules
  • Organometallic palladium reagents are used to synthesize linker-free ADCs where the drug molecules are directly linked to cysteine thiols in antibodies. (mit.edu)
  • ligase
  • The systematic name of this enzyme class is L-cysteine:tRNACys ligase (AMP-forming). (wikipedia.org)
  • Phosphopantothenate-cysteine ligase from the bacterium Escherichia coli uses cytidine triphosphate (CTP) as an energy donor, whilst the human isoform uses adenosine triphosphate (ATP). (wikipedia.org)
  • Glutamate cysteine ligase is a heterodimeric holoenzyme composed of two protein subunits that are coded by independent genes located on separate chromosomes: Glutamate cysteine ligase catalytic subunit (GCLC, ~73 kDa) possesses all of substrate and cofactor binding sites and is responsible for all of the catalysis. (wikipedia.org)
  • Glutamate cysteine ligase modifier subunit (GCLM, ~31 kDa) has no enzymatic activity on its own but increases the catalytic efficiency of GCLC when complexed in the holoenzyme. (wikipedia.org)
  • thiols
  • The second approach utilizes organometallic palladium reagents to chemoselectively install electron-neutral and electron-rich aryls on cysteine thiols. (mit.edu)
  • Using bispalladium reagents, macrocyclic peptides bearing aryl linkers are synthesized via crosslinking of two cysteine thiols. (mit.edu)
  • metabolic
  • Although classified as a non-essential amino acid , in rare cases, cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes . (wikipedia.org)
  • antioxidant
  • Cysteine is becoming even more important as a useful antioxidant-detoxifier-protector with the increasing pollution and toxicity of this industrial age. (healthy.net)
  • synthesis
  • Cysteine synthesis. (wikipedia.org)
  • However, the relevance of CSC formation in each compartment for flux control of cysteine synthesis remains controversial. (mendeley.com)
  • Here, we demonstrate the interaction between mitochondrial SAT3 and OAS-TL C in planta by FRET and establish the role of the mitochondrial CSC in the regulation of cysteine synthesis. (mendeley.com)
  • hydrolysis
  • The majority of L -cysteine is obtained industrially by hydrolysis of animal materials, such as poultry feathers or hog hair. (wikipedia.org)
  • Following this technology, L -cysteine is produced by the hydrolysis of racemic 2-amino-Δ 2 -thiazoline-4-carboxylic acid using Pseudomonas thiazolinophilum . (wikipedia.org)
  • nucleophile
  • For superfamilies , P = superfamily containing a mixture of nucleophile class families, C = purely cysteine proteases. (wikipedia.org)
  • Within each superfamily, families are designated by their catalytic nucleophile (C = cysteine proteases). (wikipedia.org)
  • high affinity
  • Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding. (ebi.ac.uk)
  • heavy metals
  • Cysteine in sufficient levels will bind with metals-preferentially, the heavy metals lead, mercury, and cadmium bond most strongly-thus, cysteine aids the body's elimination of them. (healthy.net)