An article Aminobacter sp. MSH1 Mineralizes the Groundwater Micropollutant 2,6-Dichlorobenzamide through a Unique Chlorobenzoate Catabolic Pathway WOS:000484644500018 published article about SP STRAIN HBP1; HYDROLYTIC DEHALOGENATION; DEGRADATION; BAM; DICHLOBENIL; GENES; ACID; 4-CHLOROBENZOATE; 3-CHLOROBENZOATE; 2,3-DIOXYGENASE in [Raes, Bart; Horemans, Benjamin; T’Syen, Jeroen; Springael, Dirk] Katholieke Univ Leuven, Div Soil & Water Management, B-3000 Leuven, Belgium; [Ghequire, Maarten G. K.; De Mot, Rene] Katholieke Univ Leuven, Ctr Microbial & Plant Genet, B-3000 Leuven, Belgium; [Rentsch, Daniel] Swiss Fed Labs Mat Sci & Technol, Lab Funct Polymers, Empa, CH-8600 Dubendorf, Switzerland; [Wattiez, Ruddy] Univ Mons, Dept Prote & Microbiol, B-7000 Mons, Belgium; [Kohler, Hans-Peter E.] Swiss Fed Inst Aquat Sci & Technol, Dept Environm Microbiol, Eawag, CH-8600 Dubendorf, Switzerland in 2019.0, Cited 52.0. The Name is 2,6-Dichlorobenzoic acid. Through research, I have a further understanding and discovery of 50-30-6. Computed Properties of C7H4Cl2O2
2,6-Dichlorobenzamide (BAM) is a major groundwater micropollutant posing problems for drinking water treatment plants (DWTPs) that depend on groundwater intake. Aminobacter sp. MSH1 uses BAM as the sole source of carbon, nitrogen, and energy and is considered a prime biocatalyst for groundwater bioremediation in DWTPs. Its use in bioremediation requires knowledge of its BAM-catabolic pathway, which is currently restricted to the amidase BbdA converting BAM into 2,6-dichlorobenzoic acid (2,6-DCBA) and the monooxygenase BbdD transforming 2,6-DCBA into 2,6-dichloro-3-hydroxybenzoic acid. Here, we show that the 2,6-DCBA catabolic pathway is unique and differs substantially from catabolism of other chlorobenzoates. BbdD catalyzes a second hydroxylation, forming 2,6-dichloro-3,5-dihydroxybenzoic acid. Subsequently, glutathione-dependent dehalogenases (BbdI and BbdE) catalyze the thiolytic removal of the first chlorine. The remaining chlorine is then removed hydrolytically by a dehalogenase of the alpha/beta hydrolase superfamily (BbdC). BbdC is the first enzyme in that superfamily associated with dehalogenation of chlorinated aromatics and appears to represent a new subtype within the alpha/beta hydrolase dehalogenases. The activity of BbdC yields a unique trihydroxylated aromatic intermediate for ring cleavage that is performed by an extradiol dioxygenase (BbdF) producing 2,4,6-trioxoheptanedioic acid, which is likely converted to Krebs cycle intermediates by BbdG.
Computed Properties of C7H4Cl2O2. Welcome to talk about 50-30-6, If you have any questions, you can contact Raes, B; Horemans, B; Rentsch, D; T’Syen, J; Ghequire, MGK; De Mot, R; Wattiez, R; Kohler, HPE; Springael, D or send Email.
Reference:
Chloride – Wikipedia,
,Chlorides – an overview | ScienceDirect Topics