New and highly active microbial phosphotriesterase sources
نویسندگان
چکیده
منابع مشابه
Perturbations to the active site of phosphotriesterase.
Phosphotriesterase catalyzes the hydrolysis of organophosphate nerve agents. Four amino acid residues, located within the active site pocket, were mutated in an effort to ascertain the roles that these groups play in the structure and function of this enzyme. Tryptophan-131 is located at the entrance to the binuclear metal center, and the indole ring is positioned to suggest that it could provi...
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There is an increased need for new drug leads to treat diseases in humans, animals and plants. A dramatic example is represented by the need for novel and more effective antibiotics to combat multidrug-resistant microbial pathogens. Natural products represent a major source of approved drugs and still play an important role in supplying chemical diversity, despite a decreased interest by large ...
متن کاملStructure and Reactivity of the Phosphotriesterase Active Site
The structure and reactivity of the native, mutant, and metal substituted phosphotriesterase (PTE) is determined by ab initio quantum chemistry calculations. The x-ray structure for the Zn-Zn enzyme is leveraged into a catalytically competent active site in which a wide range of theoretical structures can be optimized for metal substituted and mutant active sites. The structural behavior of the...
متن کاملThe latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase.
In essence, evolutionary processes occur gradually, while maintaining fitness throughout. Along this line, it has been proposed that the ability of a progenitor to promiscuously catalyze a low level of the evolving activity could facilitate the divergence of a new function by providing an immediate selective advantage. To directly establish a role for promiscuity in the divergence of natural en...
متن کاملEnhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues.
The factors that govern the substrate reactivity and stereoselectivity of phosphotriesterase (PTE) toward organophosphotriesters containing various combinations of methyl, ethyl, isopropyl, and phenyl substituents at the phosphorus center were determined by systematic alterations in the dimensions of the active site. The wild type PTE prefers the S(P)-enantiomers over the corresponding R(P)-ena...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 2016
ISSN: 1574-6968
DOI: 10.1093/femsle/fnw276