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Definition
 
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Cystathionine gamma-Lyase definition: A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.
Cysteine definition: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
cysteine definition: primary aminoacid with the side group -CH2SH, capable of forming disulfide bonds (cystine) with other cysteine residues to stabilize protein tertiary and oligomeric structure.
Cysteine definition: Amino acid with side chain -CH2SH.
Cysteine definition: A non-essential sulfur-containing amino acid in humans, related to cystine, Cysteine is important for protein synthesis, detoxification, and diverse metabolic functions. Found in beta-keratin, the main protein in nails, skin, and hair, Cysteine is important in collagen production, as well as skin elasticity and texture. Also required in the manufacture of amino acid taurine, Cysteine is a component of the antioxidant glutathione, and plays a role in the metabolism of essential biochemicals such as coenzyme A, heparin, and biotin. (NCI04)
Caspases definition: A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.
Caspase definition: The caspases are a family of proteases responsible for carrying out the cell death process. In a living cell, these proteases are kept inactive by proteins on the mitochondrial cell surface from the BcL-2 family. When a cell is exposed to cell death signals such as ischemia, chemotherapy or radiation, BcL-2 function is blocked and caspase activators initiate the cell death cascade.
Caspase definition: Caspases are a family of intracellular cysteine proteinases involved in inflammation and apoptosis. These enzymes appear to be involved in the initial signaling events, as well as the downstream proteolytic cleavages, that result in apoptotic cell death. They are specific for aspartic acid at the P1 position and are divided into two classes based on the lengths of their N-terminal pro-domains. Caspases-1, -2, -4, -5, -8, and -10 have long pro-domains; caspases-3, -6, -7, and -9 have short pro-domains. (from Science 1998. 281:1312 and Br Med Bull 1997. 53:478)
Cysteine Endopeptidases definition: 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.
Cysteine Synthase definition: 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 4.2.99.8.
Cysteine Dioxygenase definition: 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.
Caspase 10 definition: A long pro-domain caspase that contains a death effector domain in its pro-domain region. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS. Caspase 10 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
Caspase-10 definition: Caspase-10, encoded by the CASP10 gene, is a member of the cysteine-aspartic acid protease (caspase) family. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspase-10 is involved in the activation cascade of caspases responsible for apoptosis execution. It is recruited to both FAS- and TNFR-1 receptors in a FADD dependent manner. Caspase-10 cleaves and activates Caspases-3, -4, -6, -7, -8, and -9, and itself can be processed by Caspase-8. Mutations in the CASP10 gene are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome. Four alternatively spliced transcript variants encoding different isoforms have been described for this gene. (From LocusLink, Swiss-Prot and NCI)
Caspase-10 definition: Caspase-10 originally was identified as a novel ICE/CED-3 protease, designated FLICE2 (FADD (fas-associated via death domain)-like ICE 2). It has two death effector domains (DEDs) that bind to the DED in the adapter molecule FADD and recruits TNFR1 to form complexes with these receptors. Caspase-10 is therefore involved in the TNFR1 induced apoptosis. Caspase-10 cleaves and activates caspase-3, -4, -6, -7, -8, and -9, which causes the proteolytic cleavage of many key proteins such as PARP (poly (ADP-ribose) polymerase). Cleavage of PARP occurs in many different systems during apoptosis and is the hallmark of programmed cell death.
Caspase-5 definition: Caspase-5, encoded by the CASP5 Gene, is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. Overexpression of the active form of this enzyme has been shown to induce apoptosis in fibroblasts. Max, a central component of the Myc/Max/Mad transcription regulation network important for cell growth, differentiation, and apoptosis, is cleaved by this protein, which required Fas-mediated dephosphorylation of Max. The expression of this gene is regulated by interferon-gamma and lipopolysaccharide. (From LocusLink and NCI)
cysteine biosynthetic process definition: The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid. [GOC:go_curators]
cysteine biosynthetic process via S-sulfo-L-cysteine definition: The chemical reactions and pathways resulting in the formation of cysteine, via the intermediate S-sulfo-L-cysteine. [GOC:go_curators]
cysteine catabolic process definition: The chemical reactions and pathways resulting in the breakdown of cysteine, 2-amino-3-mercaptopropanoic acid. [GOC:go_curators]
L-cysteine catabolic process to pyruvate, using cysteine dioxygenase definition: The chemical reactions and pathways resulting in the breakdown into pyruvate of L-cystine, catalyzed by the enzyme cysteine dioxygenase (EC:1.13.11.20). [GOC:jl]
cysteine metabolic process definition: The chemical reactions and pathways involving cysteine, 2-amino-3-mercaptopropanoic acid. [GOC:go_curators]
cysteine transport definition: The directed movement of cysteine into, out of, within or between cells. [GOC:jl, ISBN:0198506732 "Oxford Dictionary of Biochemistry and Molecular Biology"]
cysteine export definition: The directed movement of cysteine out of a cell or organelle. [GOC:mlg]
Cysteine Proteases definition: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
Cysteine Proteinase definition: An enzyme that contains an unpaired cysteine in the active site which acts as a nucleophilic thiol to catalyze the proteolytic processing of other proteins or polypeptides.
 
 
frFrench
cystéine definition: Acide aminé dont le groupement latéral contient un groupement sulfhydryle (ou thiol), capable de former des ponts disulfure.