AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation ScienceHealth Care
Protocatechuate-3,4-DioxygenaseHydroxybenzoatesDioxygenasesOxygenasesAcinetobacter InfectionsAcinetobacter baumanniiParabensVanillic AcidAcinetobacter calcoaceticusAdipatesCatechols4-Hydroxyphenylpyruvate DioxygenaseCatechol 1,2-DioxygenaseCatechol 2,3-DioxygenasePseudomonasCysteine DioxygenaseQuinic AcidBiodegradation, EnvironmentalTryptophan OxygenaseAcinetobacterBenzoatesGentisatesBenzoic AcidHomogentisate 1,2-DioxygenaseSphingomonas3-Hydroxyanthranilate 3,4-DioxygenaseOxidoreductases, O-DemethylatingComamonasHydrocarbons, AromaticChlorobenzoatesKynurenineGallic AcidPhthalic AcidsPseudomonas putidaGenes, BacterialBrevibacteriumComamonas testosteroniMolecular Sequence DataBurkholderiaBacterial ProteinsBenzaldehydesSequence Analysis, DNAIsonicotinic AcidsDNA, BacterialAmino Acid SequenceSubstrate SpecificityOxygen IsotopesTryptophanGene Expression Regulation, BacterialDecarboxylationRhodococcusEugenolCoumaric AcidsCarbapenemsCarboxy-LyasesCloning, MolecularBase SequenceDrug Resistance, Multiple, BacterialNitrobenzoatesCarboxylic Ester HydrolasesElectron Spin Resonance SpectroscopySpectrophotometryOperonAnti-Bacterial AgentsOxaloacetic AcidMultigene FamilyIronEscherichia coliColistinChlorobenzenesMixed Function OxygenasesRestriction MappingAlcaligenesKineticsCoenzyme A-TransferasesMitosporic FungiHomogentisic AcidToluenePlasmidsPhylogenyEnzyme InductionOxidation-ReductionMicrobial Sensitivity TestsAcetyl-CoA C-AcyltransferaseCross InfectionSoil MicrobiologyOxidoreductasesCell-Free SystemMutationSequence Homology, Amino AcidOpen Reading FramesMutagenesis, Insertionalbeta-LactamasesImipenemMolecular WeightCulture MediaAgrobacterium tumefaciensChromosomes, BacterialSpectrophotometry, UltravioletCrystallization
DegradationGeneShownProduceCatalyzesIsomersPathway
Degradation2
  • benK encodes a hydrophobic permease-like protein involved in benzoate degradation by Acinetobacter sp. (microbiologyresearch.org)
  • Moreover, two hydrolases (CouB1 and CouB2) homologous to the 3,4-dihydrocoumarin hydrolase in the fluorene degradation were found to accelerate the generation of melilotic acid (MA) from DHC. (bvsalud.org)
Gene1
  • Toxicologically, COU was proven hepatotoxic to individuals with mutations in the CYP2A6 gene and listed as a group 3 carcinogen by the International Agency for Research on Cancer and thus has raised increasing concerns. (bvsalud.org)
Shown1
  • The biosynthesis of catechin is shown below Leucocyanidin reductase (LCR) uses 2,3-trans-3,4-cis-leucocyanidin to produce (+)-catechin and is the first enzyme in the proanthocyanidin (PA) specific pathway. (wikipedia.org)
Produce1
  • CouC, a new member from the group A flavin monooxygenase, was heterologously expressed and purified, catalyzing the hydroxylation of MA to produce 3-(2,3-dihydroxyphenyl)propionate (DHPP). (bvsalud.org)
Catalyzes2
  • Chalcone synthase then catalyzes the condensation of 4-hydroxycinnamoyl CoA and three molecules of malonyl-CoA to form chalcone. (wikipedia.org)
  • Thereafter a dioxygenase catalyzes the formation of 4,5-dihydro-4,5-dihydroxyphthalate, which is oxidized by an NAD-dependent dehydrogenase to give 4,5-dihydroxyphthalate, Protocatechuate, formed by decarboxylation of 4,5-dihydroxyphthalate, is the substrate for ring cleavage enzymes. (nih.gov)
Isomers1
  • Isophthalate and terephthalate (anions) are readily used as carbon sources by aerobic bacteria, and preliminary evidence is consistent with catabolic routes for these isomers converging at the ring-cleavage substrate protocatechuate. (nih.gov)
Pathway4
  • The biosynthesis of catechin begins with ma 4-hydroxycinnamoyl CoA starter unit which undergoes chain extension by the addition of three malonyl-CoAs through a PKSIII pathway. (wikipedia.org)
  • 4-Hydroxycinnamoyl CoA is biosynthesized from L-phenylalanine through the Shikimate pathway. (wikipedia.org)
  • The biosynthesis of catechin is shown below Leucocyanidin reductase (LCR) uses 2,3-trans-3,4-cis-leucocyanidin to produce (+)-catechin and is the first enzyme in the proanthocyanidin (PA) specific pathway. (wikipedia.org)
  • Whereas flurorescent pseudomonads use the beta-ketoadipate pathway, the nonfluorescent strains and micrococci examined use of meta-cleavage (4,5-) route. (nih.gov)