AnatomyOrganismsChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation ScienceHealth Care
CysteineCysteine DioxygenaseSulfur CompoundsTaurineDioxygenasesSulfatesCarboxy-LyasesGlutathioneAmino Acid SequenceMolecular Sequence DataCysteine EndopeptidasesDisulfidesCysteine ProteasesMutagenesis, Site-DirectedBinding SitesSulfhydryl CompoundsModels, MolecularBase SequenceOxidation-ReductionSequence Homology, Amino AcidProtein ConformationCysteine Proteinase InhibitorsKineticsCysteine SynthaseMutationRecombinant ProteinsProtein Structure, TertiaryEscherichia coliSulfhydryl ReagentsProtein BindingAmino Acid SubstitutionStructure-Activity RelationshipCloning, MolecularEthylmaleimideDithionitrobenzoic AcidSequence AlignmentLipid MetabolismCystineProtein Structure, SecondaryEnergy MetabolismSubstrate SpecificityChromatography, High Pressure LiquidDithiothreitolAmino AcidsPeptide FragmentsReducing AgentsBacterial ProteinsCatalysisCell LineConserved SequenceIodoacetamideElectrophoresis, Polyacrylamide GelPeptidesIodoacetic AcidHistidineHydrogen-Ion ConcentrationCatalytic DomainMass Spectrometry4-ChloromercuribenzenesulfonateAlanineIodoacetatesCathepsinsProtein Processing, Post-TranslationalMesylatesAlkylationLiverCrystallography, X-RayDimerizationPapainSulfurMagnetic Resonance SpectroscopyCattleTrypsinCystatinsProtein FoldingDNA, ComplementaryCircular DichroismDNA PrimersMutagenesisLipoylationMembrane ProteinsProteinsMolecular WeightZincPeptide MappingThioredoxinsHydrolysisCarbon-Sulfur LyasesSulfenic AcidsCell MembraneOxidoreductasesMethionineMolecular StructureRecombinant Fusion ProteinsPoint MutationTransfectionDNACathepsin LPlasmidsCathepsin B
Involving the reverFunctionally importantDisulfideProteinMethionineProteomicThiolKeap1LysineLipidPathwaysCovalentEnzymesPeptideApoptosisAmino acidsBone metabolismCoordinateCatalysisRedoxReactiveMicrobialCellularPeptidesCoding sequenceEnzymeLipidsSulfurArginineModificationUndergoCompoundsADVERSE REACTIONSGenesProcessesConjugatesHydrogenCoenzymeChemical reactionsCellActiveCatalyzeFoundMild
Involving the rever1
  • Our team has pioneered the field of redox biology, and is internationally recognized for its expertise in reactions involving the reversible oxidation of cysteine residues, iron, and the signaling by H 2 O 2 . (paris-saclay.fr)
Functionally important2
  • Intracellular thiol-disulfide balance is critical, in turn, for the activity of proteins with functionally important cysteine residues, which includes many Fe-binding enzymes. (grantome.com)
  • 2016). The identity of the DUOX1 cysteines targeted by these electrophiles is yet to be established, but these studies offer the exciting prospect that selective targeting of specific functionally important cysteines within DUOX1 may lead to inhibition of DUOX1, and could be exploited for the development of DUOX\selective inhibitors to treat allergic disorders such as asthma, allergic rhinitis, atopic dermatitis and conjunctivitis. (ees2010prague.org)
Disulfide5
  • During the process an intramolecular disulfide bond is formed between two L-cysteine residues of DsrC. (genome.jp)
  • The saposin B-type domain is characterised by six conserved cysteine residues involved in three disulfide bridges: one between helices 2 and 3, one between the first and the last helix and one from the N-terminal part of the first helix to the C terminus. (embl.de)
  • Th tripeptide glutathione (GSH) and glutaredoxin (Grx) proteins function together in both thiol redox control and iron homeostasis by catalyzing thiol-disulfide exchange reactions and participating in Fe-S cluster biogenesis pathways. (grantome.com)
  • Finally, a disulfide bond is formed between cysteine residues numbers 2 and 7. (wikidoc.org)
  • The human form of IAPP has the amino acid sequence KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY, with a disulfide bridge between cysteine residues 2 and 7. (wikidoc.org)
Protein13
  • In vivo, argpyrimidine is synthesized from a Methylglyoxal (MG) mediated modification on an arginine residue in a protein. (wikipedia.org)
  • Methylglyoxal is formed through the Polyol pathway, the degradation of triose phosphates from Glycolysis, acetone metabolism, protein Glycation, or Lipid peroxidation. (wikipedia.org)
  • Methylglyoxal then can modify Arginine, Cysteine, or Lysine amino acid residues within a protein. (wikipedia.org)
  • The Maillard Reaction occurs between the carbonyl group of a sugar and the amino group on a protein. (wikipedia.org)
  • The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. (genome.jp)
  • d) It is highly significant in the liver and kid-neys of birds which excrete uric acid as the end product of purine metabolism and also of protein and amino acid catabolism. (biologydiscussion.com)
  • Real‑time quantitative polymerase chain reaction (PCR) and western blot analyses were used to detect SPRY2 expression and miR‑21 protein expression levels. (spandidos-publications.com)
  • The SPRY2 protein contains 315 human amino acid residues (35 kDa), with the C-terminal residues 178-282 being rich in cysteine. (spandidos-publications.com)
  • Due to their reactivity and redox properties, these molecules engage into redox reactions that are at the heart of multiple life-essential cellular enzymatic, metabolic and synthetic processes: energy production, DNA synthesis and repair, protein translation, protein secretion, stress protection and homeostasis, cellular signaling and biological clocks control. (paris-saclay.fr)
  • They found [ 19 ], however, that three discrete chemical moieties in the viral protein, namely the cysteine, tyrosine, and tryptophan amino acid residues were able to react with ClO 2 rapidly. (akjournals.com)
  • A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine. (reactome.org)
  • PON1 is a glycosylated protein consisted of 354 amino acid residues with an apparent mass of 43-47 kDa. (biochemia-medica.com)
  • Mature protein retains hydrophobic signal sequence on the N-terminal region, from which only the initiator methionine residue is removed (2,4,5). (biochemia-medica.com)
Methionine2
Proteomic1
  • In this study, we present a highly efficient method for proteomic profiling of cysteine residues in complex proteomes and in living cells. (unige.ch)
Thiol2
  • Here we analyzed arsenic-Keap1 cysteine thiol interactions for Nrf2 activation. (cdc.gov)
  • Iron and thiol redox homeostasis are intimately connected in cellular metabolism. (grantome.com)
Keap12
  • Identification of critical cysteine residues of Keap1 in arsenic-sensing and suppression of Nrf2. (cdc.gov)
  • Our findings support the notion that arsenic binds to different sets of Keap1 cysteine residues to regulate divergent functions in Nrf2 signaling. (cdc.gov)
Lysine2
  • [4] At the C-terminus Carboxypeptidase E then removes the terminal lysine and arginine residues. (wikidoc.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)
Lipid1
  • In the cell, RNF213 was shown to be involved in fatty acid metabolism ( 11 ), and to associate with intracellular lipid droplets in a manner dependent on its E3 ligase and ATPase activities ( 12 ). (biorxiv.org)
Pathways1
  • Xiao and intestinal alterations indicative of mucosal dysbiosis (Grasberger IFN\ and IFN\ (Fink (Fink model of lung epithelial injury in mice (Gorissen redox\dependent regulation of cell signalling pathways, by reversible oxidation of functional cysteine residues. (ees2010prague.org)
Covalent1
  • It forms a covalent bond with a cysteine residue in the BTK active site, leading to inhibition of BTK enzymatic activity. (medscape.com)
Enzymes3
  • a) Enzymes that catalyse the removal of hy-drogen from a substrate but use only oxy-gen as a hydrogen acceptor to form water as a reaction product (with the exception of uricase and monoamine oxidase which form H 2 O 2 ). (biologydiscussion.com)
  • These results indicate that in vivo production of the GSH conjugates of (E)-2,4-diene VPA is most likely catalyzed by GST enzymes, with the esterified diene being essential for the conjugation reaction. (aspetjournals.org)
  • Accordingly, organisms protect themselves by the production of many classes of antioxidant enzymes, including superoxide dismutase and catalase (that catalyse reactions that lead ultimately to the conversion of ROS to water), and thioredoxins and peroxiredoxins (that use reversible oxidation of sulphydryl groups to remove ROS) [ 9 ]. (biomedcentral.com)
Peptide3
  • Amylin, or islet amyloid polypeptide ( IAPP ), is a 37-residue peptide hormone . (wikidoc.org)
  • Amylin also acts in bone metabolism, along with the related peptides calcitonin and calcitonin gene related peptide . (wikidoc.org)
  • Supporting Information: LC-MS characterization of GSH-MDI reaction products, Tables of peptides matched to albumin or modified albumin, and MS/MS data on the GSH-MDI modified albumin peptide containing residues 411-428. (cdc.gov)
Apoptosis1
  • In-depth study of small non-coding RNA molecules confirmed that microRNA (miR) has an important regulatory role in cell proliferation, differentiation, metabolism, apoptosis and development processes ( 3 ). (spandidos-publications.com)
Amino acids1
Bone metabolism1
  • Bone resorption occurs mainly on the bone surface, by the osteoclasts (OC) on bone metabolism in continuous absorption. (frontiersin.org)
Coordinate1
  • The 2 zinc finger motifs are able to tetrahedrally coordinate a zinc atom and are held by 4 cysteine (Cys) residues (see the image below, panel C). (medscape.com)
Catalysis1
  • Crystal structures of yCBS-cc in complex with enzymatic reaction intermediates have been captured, providing a structural basis for residues involved in catalysis. (rhea-db.org)
Redox3
  • Disruptions in redox regulation and iron metabolism have been implicated in numerous human diseases including cancer, neurodegenerative diseases, mitochondrial dysfunction disorders, and iron overload disorders. (grantome.com)
  • Redox Biology explores the cellular and physiological functions of biological molecules having distinctive chemical reactivity and redox properties, in particular oxygen and derived reduced species (hydrogen peroxide or H 2 O 2 , the superoxide anion or O 2 - ), iron and other biological redox metals, and the sulfur-containing amino acids methionine, with its S-methyl thioether side chain, and cysteine with its thiol (-SH) side chains. (paris-saclay.fr)
  • In the past, these reactions were essentially considered by their enzymology and studied in vitro , and in Redox Biology they are repositioned in the context of the cell. (paris-saclay.fr)
Reactive2
  • and hydrogen peroxide (http://www.guidetopharmacology.org/GRAC/LigandDisplayForward?ligandId=2448)] and secondary ROS comprising reactive metabolites formed by subsequent reactions of these primary ROS [e.g. with http://www.guidetopharmacology.org/GRAC/LigandDisplayForward?ligandId=2509 to form peroxynitrite (ONOO? (ees2010prague.org)
  • The mechanisms by which isocyanates cause asthma remain unclear, hampering disease prevention, diagnosis, and treatment.7 It is assumed the reactive nature of N=C=O groups underlies isocyanate asthma, with a hapten-based mechanism as the most obvious pathway to pathogenesis.8 However, the critical "self" reaction targets for isocyanate in vivo remain uncertain. (cdc.gov)
Microbial1
Cellular4
  • Our results demonstrate that curcumin covalently modifies several key players of cellular signaling and metabolism, most notably the enzyme casein kinase I gamma. (unige.ch)
  • (ii) the need for their strict cellular control due to the potential reactivity of reaction intermediates to avoid propagation of abnormal reactions that can lead to oxidative stress and cell death. (paris-saclay.fr)
  • As they pervade most if not all cellular processes, exploring these reactions in vivo requires integrated cellular approaches that consider the cell as a whole. (paris-saclay.fr)
  • 4] Glucocorticoids are involved in almost every cellular, molecular, and physiologic network of the organism and play a pivotal role in critical biologic processes, such as growth, reproduction, intermediary metabolism, immune and inflammatory reactions, and central nervous system and cardiovascular functions. (medscape.com)
Peptides1
  • Grisemycin, salinipeptin, and cypemycin belong to the linaridin class of ribosomally synthesized and posttranslationally modified peptides that contain multiple dehydrobutyrine and D-amino acid residues. (hokudai.ac.jp)
Coding sequence1
  • IAPP is processed from an 89-residue coding sequence . (wikidoc.org)
Enzyme2
  • The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. (genome.jp)
  • Serine protease, which is found in the digestive system, breaks down the proteins that help an enzyme catalyze in its chemical reaction. (vedantu.com)
Lipids1
  • Existing studies have confirmed that ferroptosis involves the metabolisms of the Fe, lipids, amino acid, each mechanism is mutually independent but interrelated, and they are formed a complex regulatory network. (frontiersin.org)
Sulfur1
  • In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1 in the right to left direction), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2 in the left to right direction) [1]. (genome.jp)
Arginine2
  • It is an advanced glycation end-product formed from arginine and methylglyoxal through the Maillard reaction. (wikipedia.org)
  • In the Methylglyoxal-mediated Maillard Reaction on arginine, a dihydroxy-imidazolidine intermediate is involved in the production of the argpyrimidine modification. (wikipedia.org)
Modification1
  • The modification of these side chains through the Maillard reaction forms Advanced glycation end-products (AGEs). (wikipedia.org)
Undergo2
  • The Amadori product can then undergo many further reactions to form various AGE products, which can also be further modified into different products. (wikipedia.org)
  • The side chain of Serine as a residue of proteins can undergo O-linked glycosylation. (vedantu.com)
Compounds2
  • Since it is a type of non-essential amino acid, it can be synthesized by the human body from many compounds via various chemical reactions. (vedantu.com)
  • The reactions between α-dicarbonyl compounds (MGO, GO, and 3-DG) and GSH were studied by LC-MS in a cell-free system. (ebsco.com)
ADVERSE REACTIONS1
  • To report SUSPECTED ADVERSE REACTIONS, contact AstraZeneca at 1-800-236-9933 or FDA at 1-800-FDA-1088 or www.fda.gov/medwatch. (drugs.com)
Genes2
  • The biosynthetic gene clusters of these linaridins lack obvious candidate genes for the dehydratase and epimerase required to introduce dehydrobutyrine and D-amino acid residues, respectively. (hokudai.ac.jp)
  • However, we previously demonstrated that the grisemycin (grm) cluster contained cryptic dehydratase and epimerase genes by heterologous expression of this biosynthetic gene cluster in Streptomyces lividans and proposed that two genes (grmH and grmL) with unknown functions catalyze dehydration and epimerization reactions. (hokudai.ac.jp)
Processes1
  • ACD is a of Risk from Existing Knowledge (DEREK) may be delayed (type IV) hypersensitivity reaction to an useful to some extent in the initial screening of exogenous chemical mediated by T-cell-related potential sensitization hazard of chemicals in processes (1-3). (cdc.gov)
Conjugates1
  • The production of the GSH conjugates was increased by 2-fold for reactions involving the sonic-disrupted mitoplasts, either from untreated or PB-treated rats. (aspetjournals.org)
Hydrogen1
  • CBAX1 and CBAX2 with different branching degrees, together with corn bran residue (CBR) were generated from corn bran after alkaline hydrogen peroxide (AHP) pretreatment and graded ethanol precipitation. (biomedcentral.com)
Coenzyme1
  • The pyridoxal 5'-phosphate (PLP) acts as a coenzyme for a large number of biochemical reactions. (bvsalud.org)
Chemical reactions1
  • Search chemical reactions in Rhea for this molecule. (rhea-db.org)
Cell2
Active4
  • Bone is an active metabolism tissue, which constantly undergoes bone remodeling. (frontiersin.org)
  • The active site is placed at the junction of the large and small domains and includes residues from both protomers of the homodimer. (bvsalud.org)
  • The mammalian saposins are synthesized as a single precursor molecule (prosaposin) which contains two saposin A-type domains in the extremities that are removed in the activation reaction, and four saposin B-type domains yielding the active saposins A, B, C and D after proteolytic cleavage. (embl.de)
  • Here we report the crystal structure of an active 242-residue C-terminal fragment of human p50rhoGAP. (embl-heidelberg.de)
Catalyze1
  • Partially purified GST was found to catalyze the conjugation reactions in a fashion similar to that of the isolated subcellular fractions. (aspetjournals.org)
Found2
  • Argpyrimidine is also found in food chemistry through the browning of food by the Maillard Reaction. (wikipedia.org)
  • Only the 1,6- addition product was found for the spontaneous conjugation reaction (control). (aspetjournals.org)
Mild1
  • This reaction proceeds fast, under mild physiological conditions, and with a very high degree of chemoselectivity. (unige.ch)