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LyasesATP Citrate (pro-S)-LyaseChondroitin LyasesOxo-Acid-LyasesAldehyde-LyasesAdenylosuccinate LyasePectobacterium chrysanthemiPectinsChondroitinases and Chondroitin LyasesPolysaccharide-LyasesInterleukin-1betaPhycobiliproteinsCarbon-Oxygen LyasesHeparin LyaseChicorybeta 2-MicroglobulinErwiniaMolecular Sequence DataSubstrate SpecificityPolygalacturonaseAmino Acid SequenceReceptors, Adrenergic, betaIntegrin beta3Chondroitin ABC LyaseAlginatesDNA-(Apurinic or Apyrimidinic Site) LyasePhycobilinsHexuronic AcidsCloning, MolecularKineticsBase SequenceSteroid 17-alpha-HydroxylaseSequence Homology, Amino AcidRhodophytaSphingomonasTransforming Growth Factor betaIsocitrate LyaseRecombinant ProteinsGlucuronic AcidEscherichia coliCarbohydrate SequenceBacteroidesIntegrin alpha5beta1Integrin beta4Cytochromes c1Bacterial ProteinsFlavobacteriumBinding SitesHeveaChondroitin SulfatesUronic AcidsIntegrin alpha6beta4Sequence AlignmentIntegrin beta Chainsbeta 2-Glycoprotein IHydrogen-Ion ConcentrationStreptococcus anginosusElectrophoresis, Polyacrylamide GelN-Glycosyl HydrolasesSulfonium CompoundsCrystallography, X-RayIntegrin alpha4beta1GlycosaminoglycansModels, MolecularMutationGlyoxylatesDisaccharidesMalate SynthaseIntegrin alpha2beta1Receptors, Adrenergic, beta-2Amidine-LyasesIsoenzymesDermatan SulfateProtein ConformationGlycoside HydrolasesCatalysisPseudomonasMolecular WeightCarbohydrate ConformationCarbon-Nitrogen LyasesIntegrinsDNA GlycosylasesInterleukin-1Antigens, CD29RNA, MessengerIntegrin alpha6beta1Cells, CulturedOligosaccharidesDNA Polymerase betaGenes, BacterialCatalytic DomainCell LineChromatography, GelReceptors, Adrenergic, beta-1Phosphorus-Oxygen LyasesMeglutolMutagenesis, Site-DirectedCarbon-Sulfur LyasesProteus vulgarisIsocitrates
Carbon-carbonEnzymesClassFamilyCleaveEnzymeDegradationProteinBondsGroupDomainMain chain
Carbon-carbon1
  • more specifically the ox-acid-lyase or the carbon-carbon-lyases. (wikipedia.org)
Enzymes1
  • Therefore, the characterization of the endo-1,4-beta-xylanase, encoded by um06350.1, is a further step towards the biotechnological application of U . maydis and its enzymes. (biomedcentral.com)
Class1
  • The systematic name of this enzyme class is chorismate pyruvate-lyase (4-hydroxybenzoate-forming). (wikipedia.org)
Family1
Cleave2
  • It belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. (wikipedia.org)
  • There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. (unl.edu)
Enzyme3
  • The enzyme chorismate lyase (EC 4.1.3.40) catalyzes the first step in ubiquinone biosynthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in Escherichia coli and other Gram-negative bacteria. (wikipedia.org)
  • The systematic name of this enzyme class is chorismate pyruvate-lyase (4-hydroxybenzoate-forming). (wikipedia.org)
  • An enzyme that catalyzes the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups. (lookformedical.com)
Degradation1
  • The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. (unl.edu)
Protein1
  • Three bacterial pectate lyases, a pectin lyase from Aspergillus niger, thestructures of rhamnogalacturonase A from Aspergillus aculeatus, RGase A,and the P22-phage tailspike protein, TSP, display the right-handedparallel beta-helix architecture first seen in pectate lyase. (embl.de)
Bonds1
  • A natural high-viscosity mucopolysaccharide with alternating beta (1-3) glucuronide and beta (1-4) glucosaminidic bonds. (lookformedical.com)
Group3
  • A group of carbon-oxygen lyases. (lookformedical.com)
  • P. fraxinea belongs to the Polyporales, a group of strong wood decayers, and is known to aggressively attack and fell standing hardwood trees all over the world. (hokudai.ac.jp)
  • S.A, an international company leader in clinical diagnostic reagents belonging to the Werfen group. (ibecbarcelona.eu)
Domain1
  • This is the first structure of a polygalacturonase andcomprises a 10 turn right-handed parallel beta-helix domain with two loopregions forming a "tunnel like" substrate-binding cleft. (embl.de)
Main chain1
  • The functional similarity, that the enzymes all bindalpha-galactose containing polymers at an equivalent site involving PB1and its two flanking turn regions, further supports divergent evolution.We suggest that the stacking of the coils and the unusual nearperpendicular junction of PB2 and PB3 make the parallel beta-helix foldespecially likely to maintain similar main chain conformations duringdivergent evolution even after all vestige of similarity in primarystructure has vanished. (embl.de)