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HydrolasesEscherichia coli ProteinsEpoxide HydrolasesEscherichia coliGlycoside HydrolasesEscherichia coli InfectionsMolecular Sequence DataAmino Acid SequenceBacterial ProteinsCarboxylic Ester HydrolasesGenes, BacterialLactase-Phlorizin HydrolaseCloning, MolecularEscherichia coli O157Base SequenceAdenosylhomocysteinaseSubstrate SpecificityDNA, BacterialAmidohydrolasesPlasmidsMutationKineticsgamma-Glutamyl HydrolaseEscherichia coli K12Acetyl-CoA HydrolaseSequence Homology, Amino AcidThiolester HydrolasesGene Expression Regulation, BacterialHydrolysisRecombinant ProteinsEscherichiaPalmitoyl-CoA HydrolaseN-Acetylmuramoyl-L-alanine AmidaseLysosomesAdhesins, Escherichia coliOperonBinding SitesModels, MolecularHydrogen-Ion ConcentrationSequence AlignmentGalactosidasesRNA, BacterialTemperatureCatalysisChromosomes, BacterialElectrophoresis, Polyacrylamide GelPyrophosphatasesPeptide HydrolasesGlucuronidaseCrystallography, X-RayN-Glycosyl HydrolasesRestriction MappingGenetic Complementation TestSequence Analysis, DNAAcid PhosphataseMolecular WeightMutagenesis, Site-DirectedCatalytic Domainbeta-Glucosidasebeta-GalactosidaseCellulaseEnzyme StabilityProtein ConformationAllophanate HydrolaseGenesBacterial Outer Membrane ProteinsHexosaminidasesColiphagesCulture MediaXylosidasesEndo-1,4-beta XylanasesAcid Anhydride HydrolasesSterol EsteraseProtein BindingXylansMannosephosphatesProtein Structure, TertiaryEsterasesUbiquitin ThiolesteraseAnti-Bacterial AgentsAcetylglucosaminidasePhylogenyRecombinant Fusion ProteinsTranscription, GeneticCell WallEnterotoxigenic Escherichia coliStructure-Activity RelationshipMucolipidosesbeta-MannosidaseShiga-Toxigenic Escherichia coliSpecies SpecificityCarrier ProteinsCarboxylesteraseDNA PrimersReceptor, IGF Type 2alpha-L-FucosidaseBacteriolysisAminopeptidasesBacterial ToxinsEnteropathogenic Escherichia coli

ColiGlycoside hydrolase family 43Epoxide hydrolasesEnzymeSubstratesCatalyticBacterialDegradationFamilyStructure

Coli4

• The glutamine synthetase deadenylylating enzyme system from Escherichia coli. (wikipedia.org)
• The axhD3 gene was cloned and expressed in Escherichia coli . (megazyme.com)
• Trpm2 −/− mice were intraperitoneally injected with Escherichia coli . (asahq.org)
• 3. Åkesson, M., Nordberg Karlsson E., Hagander, P., Axelsson, J.-P. and Tocaj, A. ( 1999 ) Acetate formation and dissolved oxygen responses to feed transients in Escherichia coli cultivations. (lu.se)

Glycoside hydrolase family 432

• The second ORF was the axhD3 gene belonging to glycoside hydrolase family 43. (megazyme.com)
• The presence of all epitopes can be differentially modulated in vitro using glycoside hydrolase family 43 and family 51 arabinofuranosidases. (megazyme.com)

Epoxide hydrolases1

• It differs from the previously described epoxide hydrolases (EC 3.3.2.4, EC 3.3.2.6, EC 3.3.2.7, EC 3.3.2.9 and EC 3.3.2.10) as it is not inhibited by 2-bromo-4'-nitroacetophenone, diethyl pyrocarbonate, 4-fluorochalcone oxide or 1,10-phenanthroline. (cathdb.info)

Enzyme4

• This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. (wikipedia.org)
• Using structural and chemical biology, mass spectrometry, and cell-based assays, we establish that piperazine-containing GUS inhibitors intercept the glycosyl-enzyme catalytic intermediate of these retaining glycosyl hydrolases. (sdsc.edu)
• Dienelactone hydrolase (DLH), an enzyme from the beta-ketoadipate pathway, catalyzes the hydrolysis of dienelactone to maleylacetate. (inrae.fr)
• β-galactosidase , also called lactase , beta-gal or β-gal , is a glycoside hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides through the breaking of a glycosidic bond . (wikidoc.org)

Substrates1

• 98th percentile) transcripts, including acetone carboxylase and cell-wall-associated hydrolases with unknown substrates (numerous lesser expressed cell-wall-associated hydrolases targeted peptidoglycan). (frontiersin.org)

Catalytic2

• The karrikin-1 (KAR1) ligand sits in the opening to the active site abutting a helical domain insert but distal from the canonical catalytic triad (Ser95-His246-Asp217) of α/β-hydrolases, consistent with the lack of detectable hydrolytic activity by purified KAI2. (nih.gov)
• The Cys-His-Asp catalytic triad found in dienelactone hydrolase (DLH) is unusual for several reasons. (inrae.fr)

Bacterial1

• Many of the most highly expressed hydrolases belonged to a Ca . Bathyarchaeota strain and may have been associated with recycling of bacterial biomass. (frontiersin.org)

Degradation1

• Dienelactone hydrolases play a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway. (inrae.fr)

Family3

• The first ORF showed high homology with xylanases belonging to family 8 of the glycoside hydrolases and this gene was designated xylA . (megazyme.com)
• The research focus is within the area "enzymes of extremophilic microorganisms", especially concerning thermostable glycoside hydrolases (including representatives from GH-family 1, 3, 10, 12 and 13). (lu.se)
• 2016) Construction of the first thermostable β-glucosynthase derived from glycoside hydrolase family 3. (lu.se)

Structure1

• The structure of dienelactone hydrolase (DLH) from Pseudomonus sp. (inrae.fr)