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Results 1 - 9 of 9
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20malfunction analysis of substrate binding by the mutant P316Q and the wild-type enzyme, docking study, overview 765761
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20metabolism the enzyme is involved in degradation of the herbicide 2,4-dichlorophenoxyacetic acid 742330
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20metabolism the enzyme is involved in the catabolism of 2,4-dichlorophenol, pathways, overview -, 764591
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20metabolism two dcm gene clusters essential for the degradation of diclofop-methyl in a microbial consortium of Rhodococcus sp. JT-3 and Brevundimonas sp. JT-9 764947
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20more molecular docking experiments of the enzyme TfdB-JLU's homology model with its natural substrate 2,4-dichlorophenol (with template PDB ID 5brt) reveals that the phenyl rings of 2,4-DCP form strong interactions with residues His47, Ile48, Trp222, Pro316, and Phe424. These residues are found to be important for substrate binding in the active site 765761
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20more synthesis of hybrid nanoflowers (hNFs) formed from cold-adapted 2,4-dichlorophenol hydroxylase (tfdBJLU) and Cu3(PO4)2 x 3H2O. Analysis of the influence of experimental factors, such as the pH of the solution mixture and the enzyme and Cu2+ concentrations, on the activity of the prepared tfdB-JLU-hNFs. 200 mM is the optimal Cu2+ concentration to get tfdB-JLU-hNFs with highest activity recovery, method optimization, overview. The tfdB-JLU-hNFs exhibit excellent durability with 58.34% residual activity after six successive cycles, and up to 90.58% residual activity after 20 days of storage. This multistage and hierarchical flower-like structure can effectively increase enzyme activity and stability with respect to those of the free enzyme. The satisfactory removal rate of 2,4-dichlorophenol catalyzed by tfdB-JLU-hNFs suggests that this immobilized enzyme exhibits great potential for application in bioremediation 765760
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20physiological function 2,4-dichlorophenol hydroxylase (2,4-DCP hydroxylase) is a key enzyme in the degradation of 2,4-dichlorophenoxyacetic acid through the hydroxylation step in many bacteria 765761
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20physiological function degradation of 2,4-dichlorophenol (2,4-DCP) by phenol adapted bacterium Bacillus licheniformis strain SL10 (MTCC 25059) at a relatively fast rate. The organism exhibits tolerance to 150 ppm of 2,4-DCP and shows a linear relationship between the growth and substrate concentration, the inhibitory concentration is 55.74 mg/l, kinetics, overview. The degradation efficiency of the organism is 74% under optimum conditions but increases to 97% when the growth medium contains nil sodium chloride. The organism follows a meta-cleavage pathway while degrading 2,4-DCP -, 764591
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.20physiological function the consortium L1 of Rhodococcus sp. JT-3 and Brevundimonas sp. JT-9 is able to degrade diclofop-methyl (DCM) through a synergistic metabolism, molecular mechanism of DCM degradation, overview. DCM is initially transformed by strain JT-3 to diclofop acid and then by strain JT-9 to 2-(4-hydroxyphenoxy) propionic acid as well as 2,4-dichlorophenol (DCP). DCP is the first intermediate during the degradation of herbicide 2,4-dichlorophenoxyacetic acid (2,4-D), wherein 2,4-D is converted into 3,5-dichlorocatechol by the 2,4-dichlorophenol hydroxylase 764947
Results 1 - 9 of 9