701-64-4Relevant articles and documents
Biologically reversible phosphate-protective groups
Farquhar,Srivastva,Kuttesch,Saunders
, p. 324 - 325 (1983)
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Model studies indicate that copper phenanthroline induces direct strand breaks via β-elimination of the 2'-deoxyribonolactone intermediate observed in enediyne mediated DNA damage [2]
Chen,Greenberg
, p. 3815 - 3816 (1998)
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Organophosphorous phenyl phosphates: Synthesis, dye/protein interactions and antimicrobial evaluation
Ameta, Rakesh Kumar,Duan, Yongtao,Koshti, Rohit R.,Muddassir, Mohd.,Patel, Amee S.,Trivedi, Nidhi S.,Vyas, Akshay
, (2021/01/09)
A series of Phenyl Phosphates (PPs) has been synthesized and characterized with FTIR spectroscopy. PPs, the product of the reaction of phenol and phosphoryl chloride followed by hydrolysis having larger number of hydrophilic hydroxyl groups, used for the dye interaction and antimicrobial activities. Interaction of PPs with 1,2-diphenyldiazene and 4-(phenyldiazene)phenol were studied through UV/ Vis method where observed hypochromic effect has revealed the dye adsorption property of PPs. Similarly PPs have shown the interaction with bovine serum and human serum albumins where the weaker interaction observed with later. Antimicrobial in vitro evaluation has been assessed on the basis of zone of inhibition with six bacterial (gram +ve and –ve) strains. Since PPs were found very active so minimal inhibitory concentration (MIC) analysis was done where all PPs have shown MIC less than 5 μg/mL. Due to high number of hydroxyl groups PPs have shown good interactions with biomolecules and cell wall of bacteria therefore this impression has predicted their future in medicinal field.
Transition States and Control of Substrate Preference in the Promiscuous Phosphatase PP1
Chu, Yuan,Williams, Nicholas H.,Hengge, Alvan C.
, p. 3923 - 3933 (2017/08/07)
Catalytically promiscuous enzymes are an attractive frontier for biochemistry, because enzyme promiscuities not only plausibly explain enzyme evolution through the mechanism of gene duplication but also could provide an efficient route to changing the catalytic function of proteins by mimicking this evolutionary process. PP1γ is an effectively promiscuous phosphatase for the hydrolysis of both monoanionic and dianionic phosphate ester-based substrates. In addition to its native phosphate monoester substrate, PP1γ catalyzes the hydrolysis of aryl methylphosphonates, fluorophosphate esters, phosphorothioate esters, and phosphodiesters, with second-order rate accelerations that fall within the narrow range of 1011-1013. In contrast to the different transition states in the uncatalyzed hydrolysis reactions of these substrates, PP1γ catalyzes their hydrolysis through similar transition states. PP1γ does not catalyze the hydrolysis of a sulfate ester, which is unexpected. The PP1γ active site is tolerant of variations in the geometry of bound ligands, which permit the effective catalysis even of substrates whose steric requirements may result in perturbations to the positioning of the transferring group, both in the initial enzyme-substrate complex and in the transition state. The conservative mutation of arginine 221 to lysine results in a mutant that is a more effective catalyst toward monoanionic substrates. The surprising conversion of substrate preference lends support to the notion that mutations following gene duplication can result in an altered enzyme with different catalytic capabilities and preferences and may provide a pathway for the evolution of new enzymes.