Atrazine is a chlorinated herbicide of the triazine class. It is used to prevent pre-emergence broadleaf weeds in crops such as maize (corn), soybean and sugarcane and on turf, such as golf courses and residential lawns. Atrazine's primary manufacturer is Syngenta and it is one of the most widely used herbicides in the United States, Canadian, and Australian agriculture. Its use was banned in the European Union in 2004, when the EU found groundwater levels exceeding the limits set by regulators, and Syngenta could not show that this could be prevented nor that these levels were safe.
Diphtheria toxin is an exotoxin secreted mainly by Corynebacterium diphtheriae but also by Corynebacterium ulcerans and Corynebacterium pseudotuberculosis, the pathogenic bacterium that causes diphtheria. The toxin gene is encoded by a prophage called corynephage β. The toxin causes the disease in humans by gaining entry into the cell cytoplasm and inhibiting protein synthesis.
Purine metabolism refers to the metabolic pathways to synthesize and break down purines that are present in many organisms.
D-amino-acid dehydrogenase is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids.
The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing amino acids to α-keto acids, ammonia, and thiols:
In enzymology, a 4-chlorobenzoyl-CoA dehalogenase (EC 3.8.1.7) is an enzyme that catalyzes the chemical reaction
In enzymology, an adenosylcobyric acid synthase (glutamine-hydrolysing) (EC 6.3.5.10) is an enzyme that catalyzes the chemical reaction
ADP-ribose diphosphatase (EC 3.6.1.13) is an enzyme that catalyzes a hydrolysis reaction in which water nucleophilically attacks ADP-ribose to produce AMP and D-ribose 5-phosphate. Enzyme hydrolysis occurs by the breakage of a phosphoanhydride bond and is dependent on Mg2+ ions that are held in complex by the enzyme.
Aryldialkylphosphatase is a metalloenzyme that hydrolyzes the triester linkage found in organophosphate insecticides:
The enzyme tannase (EC 3.1.1.20) catalyzes the following reaction:
In enzymology, an adenosine-phosphate deaminase (EC 3.5.4.17) is an enzyme that catalyzes the chemical reaction
In enzymology, a cyanuric acid amidohydrolase (EC 3.5.2.15) is an enzyme that catalyzes the chemical reaction
In enzymology, a hydroxydechloroatrazine ethylaminohydrolase (EC 3.5.99.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-isopropylammelide isopropylaminohydrolase (EC 3.5.99.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a riboflavin kinase is an enzyme that catalyzes the chemical reaction
The Purine Nucleotide Cycle is a metabolic pathway in protein metabolism requiring the amino acids aspartate and glutamate. The cycle is used to regulate the levels of adenine nucleotides, in which ammonia and fumarate are generated. AMP coverts into IMP and the byproduct ammonia. IMP converts to S-AMP (adenylosuccinate), which then coverts to AMP and the byproduct fumarate. The fumarate goes on to produce ATP (energy) via oxidative phosphorylation as it enters the Krebs cycle and then the electron transport chain. Lowenstein first described this pathway and outlined its importance in processes including amino acid catabolism and regulation of flux through glycolysis and the Krebs cycle.
Enzyme promiscuity is the ability of an enzyme to catalyse a fortuitous side reaction in addition to its main reaction. Although enzymes are remarkably specific catalysts, they can often perform side reactions in addition to their main, native catalytic activity. These promiscuous activities are usually slow relative to the main activity and are under neutral selection. Despite ordinarily being physiologically irrelevant, under new selective pressures these activities may confer a fitness benefit therefore prompting the evolution of the formerly promiscuous activity to become the new main activity. An example of this is the atrazine chlorohydrolase from Pseudomonas sp. ADP that evolved from melamine deaminase, which has very small promiscuous activity toward atrazine, a man-made chemical.
The enzyme cocaine esterase (EC 3.1.1.84, CocE, hCE2, hCE-2, human carboxylesterase 2; systematic name cocaine benzoylhydrolase) catalyses the reaction
Pesticide degradation is the process by which a pesticide is transformed into a benign substance that is environmentally compatible with the site to which it was applied. Globally, an estimated 1 to 2.5 million tons of active pesticide ingredients are used each year, mainly in agriculture. Forty percent are herbicides, followed by insecticides and fungicides. Since their initial development in the 1940s, multiple chemical pesticides with different uses and modes of action have been employed. Pesticides are applied over large areas in agriculture and urban settings. Pesticide use, therefore, represents an important source of diffuse chemical environmental inputs.
Paenarthrobacter aurescens is a bacterium species from the genus Paenarthrobacter . Paenarthrobacter aurescens produces nitrilase and L-N-carbamoylase. Paenarthrobacter aurescens has a low GC-content and has the ability to utilize anethole.
