cysteine In A Sentence
Learn how to use cysteine in a sentence and make better sentences with `cysteine` by reading cysteine sentence examples.
- Pevonedistat forms a stable covalent adduct with NEDD8 in the NAE catalytic pocket of UBA3 by reacting with thioester-linked NEDD8 bound to the enzyme' s catalytic cysteine.
- Covalent binding of disulfiram to the thiol blocks the binding of one of the cysteine residues with iodoacetamide, thereby inactivating the enzyme and significantly lowering catalytic activity.
- The cowpox L-18 processing by the cysteine protease caspase-1.
- The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases.
- In this process, methylglyoxal reacts with free amino groups of lysine and arginine and with thiol groups of cysteine forming AGEs.
- It also contains leucine-rich repeats with conserved cysteine-rich flanking sequences.
- A number of pyridoxal-dependent enzymes involved in the metabolism of cysteine, homocysteine and methionine have been shown to be evolutionary related.
- Lamin A is further processed to remove the last 15 amino acids and its farnesylated cysteine.
- It has since been shown to inhibit many cysteine peptidases such as papain, cathepsin B, cathepsin L, calpain and staphopain.
- This allows for the binding of the substrate ACV to the deprotonated thiol group of the cysteine residue.
- In eukaryotes, a plant serpin inhibits both metacaspases and a papain-like cysteine protease.
- The sulfhydryl group ( SH ) of cysteine serves as a proton donor and is responsible for its biological activity.
- A cross bridge between 6-hydroxy-tryptophan and cysteine allows the formation of a second " inner loop ".
- She was nice and converter cysteine we had a group or 7 and were a bit indecisive.
- For families are designated by their catalytic nucleophile ( C = cysteine proteases ).
- The cysteine sulfinic acid-dependent pathway of taurine metabolism follows the synthesis of hypotaurine ( 2-aminoethane sulfinate ), which is subsequently oxidized to taurine.
- Its active center is a [ Fe 2 S 2 ] cluster, where the iron atoms are tetrahedrally coordinated both by inorganic sulfur atoms and by sulfurs of four conserved cysteine ( Cys ) residues.
- L - cysteine is a, neutral, genetically coded amino acid, derived from cystine and found in most proteins.
- LMO2 encodes a cysteine-rich, two LIM domain protein that is required for yolk sac erythropoiesis.
- Other nutrients that assist in detoxifying the body, including methionine, cysteine, and other amino acids, may also be helpful.
- This gene encodes a cytokine member of the cystine knot superfamily, characterized by nine conserved cysteines and a cysteine knot region.
- Soybeans also contain biologically active or metabolic proteins, such as enzymes, trypsin inhibitors, hemagglutinins, and cysteine proteases very similar to papain.
- Group I PLA2 contain a cysteine at position 11 forming a disulphide bridge with a cysteine at position 77.
- In proteins, Zinc ions are often coordinated to the amino acid side chains of aspartic acid, glutamic acid, cysteine and histidine.
- The most common reaction with amino acids is cysteine oxidation.
- Tripeptide aldehyde. Reversible competitive inhibitor of serine and cysteine proteases. Inhibits also phospholipase D and C activation in rat hepatocytes.
- The product of this gene contains a cysteine rich region and exists as a heterodimer with another polymerase subunit, POLR2J . These two subunits form a core subassembly unit of the polymerase.
- The six cysteine residues are absolutely conserved throughout the cyclotide suite and presumably contribute to the preservation of the CCK motif.
- Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis.
- It is generally assumed that arsenates bind to cysteine residues in proteins.
- At the time he proposed that the compound was a dipeptide of glutamic acid and cysteine.
- Leupeptin is an organic compound produced by actinomycetes, which inhibits cysteine and threonine proteases.
- This enzyme participates in methionine metabolism and cysteine metabolism.
- Agitoxin consists of a triple-stranded antiparallel cysteine side chains connect the beta-sheet and the helix via disulphide bonds to form the core of the molecule.
- The antischistosomal activity of the antimonials were reduced by adding SDD, cysteine, sodium gluconate, sodium citrate or sodium tartrate.
- For protein labeling, Cy3 and Cy5 dyes sometimes bear typically a succinimidyl group to react with amines, or a maleimide group to react with a sulfhydryl group of cysteine residues.
- Papain protects papaya trees from herbivorous insects : role of cysteine proteases in latex.
- We have used the paradigm of rational design from structural information to engineer more potent cysteine proteinase inhibitors offer.
- The EMI domain possesses six highly conserved cysteine residues, which likely form disulphide bonds.
- Beets contain betaines which may function to reduce the concentration of homocysteine, a homolog of the naturally occurring amino acid cysteine.
- It cannot be isolated in the routine culture media because of the need for sulfhydryl group donors ( such as cysteine ).
- Objective : To determine N - acetyl - L - cysteine in compound amino acid injection by spectrophotometry.
- For example, the addition and removal of the fatty acid palmitic acid to cysteine residues in some signaling proteins causes the proteins to attach and then detach from cell membranes.
- In the first step, the Gly116 residue of Atg8 binds to a cysteine residue of ATG7 via a thioester bond in an ATP-dependent manner.
- The action of sodium sulfite is similar to that of cysteine.
- It is a fastidious, facultative intracellular bacterium which requires cysteine for growth.
- This enzyme exhibits cysteine protease activity with broad endopeptidase specificity.
- The characteristic latex also contains proteolytic enzymes and the phytocystatin chelidostatin, a cysteine protease inhibitor.
- It is formed by glutamate-cysteine ligase and used by glutathione synthetase to form glutathione.
- One the largest producer of L - cysteine HCl in the world.
- H 2 S is produced from l-cysteine by cystathionine-?-lyase ( CSE ) and MPST . l-cysteine-dependent production of H 2 S by MPST is a two-step reaction.
- The payload is the chemotherapy drug doxorubicin which is connected with a hydrazone linker to cysteine residues of the Lewis-Y specific ( chimeric ) monoclonal antibody BR96.
- The formation of cysteine is the direct coupling step between sulfur ( sulfur metabolism ) and nitrogen assimilation in plants.
- Allyl cysteine is currently being investigated as a potential cholesterol lowering agent and as a chemopreventive.
- The tidbit about methionine and cysteine in animal foods being dangerous and elevating homocysteine.
- [4Fe-4S ] cluster in the Ferredoxin-thioredoxin reductase catalytic ? subunit is surrounded by several cysteine residues.
- Acetate is subsequently transferred to a cysteine thiol of the Condensing Enzyme domain.
- Methionine is essential amino acid, whereas the cysteine and cystine are not.
- This cysteine residue contains a sulfhydryl functional group which allows the peptide to be easily conjugated to a carrier protein ( e . g.
- Cysteine is a kind of amino acid.
- The present invention discloses a colorimetric detection analysis method of cysteine.
- The strongest electrophile would then be the cyanide nitrogen, which, if attacked by water, would yield cyanic acid and the original cysteine.
- Intracellular thiols such as glutathione(GSH), cysteine(Cys), and homocysteine(Hcy) play a crucial role in maintaining biological redox homeostasis.
- TLR2 resides on the plasma membrane where it responds to lipid-containing PAMPs such as lipoteichoic acid and di-and tri-acylated cysteine-containing lipopeptides.
- Some amino acids, such as cysteine and methionine contain sulfur.
- :molybdenum cofactor + L-cysteine + 2 H + rightleftharpoons thio-molybdenum cofactor + L-alanine + H 2 O.
- A cysteine adduct is formed with the methylene group and this is the active form.
- The N-terminal cysteine-rich domain is " N "-Acetylgalactosamine and galactose residues sulphated at positions 3 and 4 of their pyranose rings.
- Transsulfuration, catalyzed by CBS, converts homocysteine to cystathionine, which cystathione gamma lyase converts to cysteine.
- TCEP is particularly useful when labeling cysteine residues with maleimides.
- The solid preparation is prepared by coating the solid preparation containing L-cysteine or salt thereof with coating film containing partial saponifiable matter of polyvinyl alcohol.
- Resistin, a plasma protein, belongs to a family of cysteine-rich secretory proteins. the formation of intramolecular disulfide bond is very important to its space-conformation and biological activity.
- OBJECTIVES: To purify a novel inhibitor of cysteine proteinases from naja atra venom and to investigate its anti-tumor cell invasiveness in vitro.
- Cysteine residues from MTs can capture harmful oxidant radicals like the superoxide and hydroxyl radicals.
- Chymopapain, one of the four cysteine proteinases of papaya latex, has milk clotting and proteolytic activity. It is mainly used to treat prolapsed intervertebral discs.
- During aging, alliin and allicin are converted to water-soluble compounds such as S-allyl cysteine and S-allyl mercaptocystine, which have little odor, are stable and survive cooking.
- Prenylcysteine lyase ( PCLase ) catalyzes the cleavage of prenylcysteine ( a protein modification ) to form an isoprenoid aldehyde and the freed cysteine residue on the protein target.
- Results showed that L - cysteine and kojic acid were better in the inhibition to apple PPO.
- The cysteine residue at 302 in ALDH1 and 200 in ALDH2 is implicated as a disulfiram binding site on the enzyme and serves as a disfulfiram sensitive thiol site.
- In structural terms, constitutive Class I ( TUBB ) and Class IVb ( TUBB2C ) ?-tubulins contain a cysteine at position 239, while ?III-tubulin has a cysteine at position 124.
- L-cysteine is a precursor to the biologic antioxidant glutathione.
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