AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation Science
Cysteine DioxygenaseCysteineSulfur CompoundsTaurineDioxygenasesCarboxy-LyasesSulfatesPyruvate KinaseGlutathionePyruvate Dehydrogenase ComplexPyruvic AcidPyruvatesPyruvate DecarboxylasePyruvate OxidaseCysteine EndopeptidasesEnergy MetabolismPyruvate Dehydrogenase (Lipoamide)Cysteine ProteasesLipid MetabolismGlucoseMolecular Sequence DataOxidation-ReductionAmino Acid SequenceKineticsLactatesPyruvate Dehydrogenase (Lipoamide)-PhosphataseLiverGlycolysisCysteine Proteinase InhibitorsCysteine SynthaseLactic AcidCitric Acid CycleMetabolismPhosphoenolpyruvateCarbon IsotopesDisulfidesAcetatesMalatesThiamine PyrophosphateEscherichia coliDichloroacetic AcidSulfhydryl CompoundsPyruvate Dehydrogenase Complex Deficiency DiseaseMutationOxaloacetic AcidAdenosine TriphosphateBase SequenceOxygen ConsumptionDihydrolipoyllysine-Residue AcetyltransferaseBinding SitesMagnetic Resonance SpectroscopyMutagenesis, Site-DirectedMitochondriaNADChromatography, High Pressure LiquidHydrogen-Ion ConcentrationGluconeogenesisFatty AcidsOxaloacetatesSequence Homology, Amino AcidAlanineRecombinant ProteinsCystineMetabolic Networks and PathwaysCarbon RadioisotopesCarbon DioxideKetoglutaric AcidsL-Lactate DehydrogenaseKetone OxidoreductasesSubstrate SpecificityBiotransformationRats, Inbred StrainsInsulinModels, BiologicalCloning, MolecularAnaerobiosisDecarboxylationModels, MolecularStarvationSulfurCoenzyme AKeto AcidsCathepsinsCulture MediaIsoenzymesCarbonProtein BindingCitratesProtein ConformationBacterial ProteinsAcetoacetatesAcetyltransferasesTime FactorsMicrosomes, LiverCytochrome P-450 Enzyme SystemCells, CulturedHydroxybutyratesSulfhydryl ReagentsCystatinsProtein Structure, Tertiary
SerineGlutathioneBiosynthesisMethionine metabolismGlycineOxidationAspartate and glutamate metabolismHistidineGlutamateEnzymesProteinKinasePhenylalanineNitrogenGlycolysisNucleotideThreonine metabolismOxidative stressPurineArginineAmino AcidsPhotosynthesisResiduesGlutamineEnergy metabolismProteinsBeta-Alanine meDisulfideMetabolicFructosePathwaysMicrobialGlucose metabolismSecondary metabolitesAcetatePathwayRedoxGluconeogenesisDehydrogenaseCellularCerebral metabolismResidueGlycolytic
Serine6
  • The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction L-serine = pyruvate + NH3 (overall reaction) (1a) L-serine = 2-aminoprop-2-enoate + H2O (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous) (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous) This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. (wikipedia.org)
  • The systematic name of this enzyme class is L-serine ammonia-lyase (pyruvate-forming). (wikipedia.org)
  • This enzyme participates in glycine, serine, threonine and cysteine metabolism. (wikipedia.org)
  • Microorganisms (and plants) make cysteine from serine using H 2 S as the sulphur source. (stackexchange.com)
  • CBS catalyses the generation of cystathionine from the substrates homocysteine and serine and liberates H 2 S from a combination of cysteine and homocysteine. (hindawi.com)
  • Glycine, serine and threonine metabolism 22 of 317 pathways' ## [1] 'Querying. (tu-dortmund.de)
Glutathione5
Biosynthesis6
Methionine metabolism2
  • Cysteine and methionine metabolism 23 of 317 pathways' ## [1] 'Querying. (tu-dortmund.de)
  • A number of defects in methionine metabolism lead to accumulation of homocysteine (and its dimer, homocystine) with adverse effects including thrombotic tendency, lens dislocation, and central nervous system and skeletal abnormalities. (msdmanuals.com)
Glycine1
  • Amino acid metabolism has extremely extensive effects in cancer cells, including, but not limited to, (1) establishing amino acid pools as building blocks, especially the production of non-essential amino acids … An overview of the metabolism of the sulfur amino acids is depicted in Fig. The outline of glycine metabolism is depicted in Fig. Oxidation via TCA cycle to produce energy (about 10-15% of body needs). (slimwithlynne.com)
Oxidation4
  • Glucose oxidation produces pyruvate which can undergo transamination to alanine. (medmuv.com)
  • Pyruvate oxidation - where did the hydrogen come from? (stackexchange.com)
  • Cysteine is the most important redox-responsive amino acid within proteins largely due to the wide range of oxidation states that sulfur can occupy-so called, "sulfur switches" [ 4 ]. (hindawi.com)
  • Methanethiol (CH3 SH) - Is an organosulfur compound derived from cysteine oxidation. (metabolichealing.com)
Aspartate and glutamate metabolism1
Histidine1
Glutamate2
Enzymes8
  • In garlic, the major flavor precursor is sulfur-alk(en)yl cysteine sulfoxide (ACSO, alliin), which is degraded by alliinase enzymes upon tissue disruption to give pyruvate, ammonia, and thiosulfinate. (springeropen.com)
  • Key enzymes involved in thallium toxicity include pyruvate kinase and succinate dehydrogenase. (medscape.com)
  • In pancreatic β cells exposed to endoplasmic reticulum (ER) stress, elevated H2S promotes the sulfhydration of enzymes in energy metabolism and stimulates glycolytic flux. (pharmaceuticalintelligence.com)
  • We propose that transcriptional and translational reprogramming by the Integrated Stress Response (ISR) in pancreatic β cells is coupled to metabolic alternations triggered by sulfhydration of key enzymes in intermediary metabolism. (pharmaceuticalintelligence.com)
  • The main generation of H 2 S in cutaneous tissue mostly depends on enzymatic routes using L-cysteine and homocysteine by two pyridoxal-5 - phosphate-dependent enzymes, cystathionine β -synthase (CBS) and cystathionine γ -lyase (CSE). (hindawi.com)
  • After, we will learn about how the function of Enzymes in amino acid metabolism. (studysmarter.co.uk)
  • Partial breakdown into lactic acid or ethanol and CO2 Note: Bacteria have many different pathways for carbohydrate metabolism based on the enzymes they are able to produce. (studylib.net)
  • 6-phosphofructokinase (PFK1) and pyruvate kinase M2 (PKM2), enzymes that catalyze irreversible, rate-limiting steps in glycolysis, were directly phosphorylated and inhibited by cyclin D3-CDK6, suggesting that cyclin D3-CDK6 may have a unique role in glucose metabolism. (aacrjournals.org)
Protein14
  • The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. (embl.de)
  • The protein encoded by this gene catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. (origene.com)
  • 2015). In the latter, an oxidized cysteine residue included glutathionylated, 60 sulfenylated and nitrosylated on a protein reacts with the sulfide anion to form a cysteine persulfide. (pharmaceuticalintelligence.com)
  • 2012). Despite great progress in bioinformatics and advanced mass spectroscopic techniques (MS), identification of different cysteine-based protein modifications has been slow compared to other post-translational modifications. (pharmaceuticalintelligence.com)
  • The biological significance of the Cys150 modification by H2S is not well-studied, but H2S could serve as a biological switch for protein function acting via oxidative modification of specific cysteine residues in response to redox homeostasis (Paul and Snyder, 2012). (pharmaceuticalintelligence.com)
  • Within an individual protein there may be a number of cysteines which could allow for multiple thiol modifications. (hindawi.com)
  • Cysteines often form part of active sites, allowing for the protein to be switched on or off depending on redox state. (hindawi.com)
  • Interactions with other proteins or molecules are another feature of cysteines that can affect protein activity. (hindawi.com)
  • Thus, reversible cysteine modifications can influence protein activity and the relative quantification of the status of the thiol can potentially provide valuable insights into protein activity where the protein exists in a range of redox states. (hindawi.com)
  • Now, Guo and García have revealed that a protein called SIR-2.1, which regulates metabolism in worms, also helps to protect the animals from the effects of aging. (elifesciences.org)
  • Urea is the end product of protein metabolism (amino acid metabolism). (slimwithlynne.com)
  • Protein metabolism is more appropriately learnt as metabolism of amino acids. (slimwithlynne.com)
  • Out of the twenty standard protein-producing amino acids… The principal fates of the essential amino acid methionine are incorporation into polypeptide chains, and use in the production of cysteine and α-ketobutyrate via the reaction pathway involving the … During fasting these carbons are converted to glucose in the liver and kidney, or to ketone bodies in the liver. (slimwithlynne.com)
  • The genetic basis of HD is the expansion of a cysteine-adenosine-guanine (CAG) repeat encoding a polyglutamine tract in the N-terminus of the protein product called huntingtin. (medscape.com)
Kinase1
  • Allosterically regulated proteins that require an activator are sometimes based on a thiol exchange interaction involving cysteines, for example, pyruvate kinase uses fructose bisphosphate (FBPs) as a heterotrophic activator and it contains a cysteine in its FBP binding site [ 8 ]. (hindawi.com)
Phenylalanine1
Nitrogen2
Glycolysis1
  • Moreover, brain energy metabolism was demonstrated to be compartmentalized in neurons and astrocytes, and astrocytic glycolysis was proposed to serve the energetic demands of glutamatergic activity. (frontiersin.org)
Nucleotide1
Threonine metabolism1
  • At T1, the significantly more abundant enzyme-coding genes were related to threonine metabolism and those genes related to the glycolytic pathway, explained by the abundance of sugars in the medium. (frontiersin.org)
Oxidative stress1
  • S limitation leads to photosynthesis and carbon metabolism disturbances that could be responsible for the oxidative stress observed in the young leaves of oilseed rape. (biomedcentral.com)
Purine1
Arginine1
Amino Acids7
Photosynthesis1
Residues2
  • The sulfhydration of cysteine residues in proteins is an important mechanism involved in diverse biological processes. (pharmaceuticalintelligence.com)
  • Reactive cysteine residues in proteins have high nucleophilicity and low pKa values and serve as a major target for oxidative modifications, which can vary depending on the subcellular environment, including the type and intensity of intracellular or environmental cues. (pharmaceuticalintelligence.com)
Glutamine1
  • OXPHOS can be sustained by amino acid (AA) metabolism in AML LSC, with cysteine and glutamine being two of the most important AAs involved in the process [ 10 ] . (encyclopedia.pub)
Energy metabolism4
  • Since the mid-twentieth century the idea that brain energy metabolism is coupled to neuronal activity has emerged, and a number of studies supported this hypothesis. (frontiersin.org)
  • In this context, 1 H MRS has allowed the measurements of energy metabolism-related compounds, whose concentrations can vary under different brain activation states. (frontiersin.org)
  • Here, we review state-of-the-art MR methods to study brain function and metabolism in vivo , and their contribution to the current understanding of how astrocytic energy metabolism supports glutamatergic activity and cerebral function. (frontiersin.org)
  • [13] CoA is important in energy metabolism for pyruvate to enter the tricarboxylic acid cycle (TCA cycle) as acetyl-CoA, and for α-ketoglutarate to be transformed to succinyl-CoA in the cycle. (wikipedia.org)
Proteins4
  • Reversible cysteine modifications allow for potential redox regulation of proteins. (hindawi.com)
  • Our method allows for the identification of the proteins, identification of redox-sensitive cysteines within proteins, and quantification of the redox status of individual cysteine-containing peptides. (hindawi.com)
  • Indeed, it has been demonstrated that cysteines are characterized by the most extreme conservation pattern, being highly conserved in functional positions of proteins but poorly conserved otherwise [ 5 ]. (hindawi.com)
  • In proteins where cysteine is not within the active site, activity can be modulated by changing conformation or by influencing its regulatory role, for example, iron sulfur complexes (ISCs) in aconitase possess cysteines required for its activity [ 7 ]. (hindawi.com)
Beta-Alanine me1
Disulfide1
  • Reversible modification of cysteines such as disulfide bond formation, glutathionylation, and nitrosylation may also be a means of protection from further, generally irreversible, modifications to sulfinic (-SO 2 H) or sulfonic (-SO 3 H) acids [ 9 ]. (hindawi.com)
Metabolic3
  • Although these techniques tackle the coupling between neuronal activity and metabolism, they lack chemical specificity and fail in providing information on neuronal and glial metabolic pathways underlying those processes. (frontiersin.org)
  • Nutrition Metabolism Analysis includes the study of a wide range of metabolic indicators which reveal the root cause behind your weight and health problems. (mydiagnostics.in)
  • Mitochondria are central hubs for cellular metabolism, coordinating a variety of metabolic reactions crucial for human health. (biomed.news)
Fructose1
Pathways11
Microbial1
  • At T2, the genes linked to the metabolism of ceramides and hopanoids lipids were clearly dominant, which are associated with the resistance of microbial species to extreme temperatures and pH values. (frontiersin.org)
Glucose metabolism2
  • Their inhibition leads to impaired glucose metabolism and disrupts the Krebs cycle, leading to decreased ATP production. (medscape.com)
  • Although the adult human brain represents only 2% of the total body weight, it consumes up to 20% of the total glucose metabolism under normal resting physiological conditions (e.g. (frontiersin.org)
Secondary metabolites1
  • In addition, S is present within many plant secondary metabolites possessing various functions in plant metabolism [ 1 ]. (biomedcentral.com)
Acetate1
Pathway1
  • Thus, the glycolytic system is the most important pathway to understand in the metabolism of cancer cells. (dojindo.com)
Redox1
  • We propose application of iTRAQ reagents in combination with a previous thiol selection method to relatively quantify the redox state of cysteines both within and between samples in a single analysis. (hindawi.com)
Gluconeogenesis1
Dehydrogenase1
  • Wild-type p53 itself acts by regulating and promoting the tricarboxylic acid (TCA) cycle, for instance by enhancing cytochrome c oxidase assembly (SCO2) expression to maintain cytochrome c oxidase complex and increasing Parkin levels in cells, which increases pyruvate dehydrogenase E1α1 (PDHA1), a critical component of the pyruvate dehydrogenase complex [ 11 ] . (encyclopedia.pub)
Cellular1
  • Cysteine, a thiol-containing amino acid, is crucial for the synthesis of sulfur-containing biomolecules that control multiple essential cellular activities. (biomed.news)
Cerebral metabolism1
Residue2
  • This interferes with cysteine residue cross-linking reducing keratin formation. (medscape.com)
  • 2009). Sulfhydrated GAPDH at Cys150 exhibits an increase in its catalytic activity, in contrast to the inhibitory effects of nitrosylation or glutathionylation of the same cysteine residue (Mustafa et al. (pharmaceuticalintelligence.com)
Glycolytic1
  • A recurring characteristic of cancer cell metabolism is that cancer cells generally prefer to produce ATP via the glycolytic system despite that system being less efficient than mitochondrial oxidative phosphorylation (Warburg effect). (dojindo.com)