127074-29-7Relevant articles and documents
Optimizing Pyrazolopyrimidine Inhibitors of Calcium Dependent Protein Kinase 1 for Treatment of Acute and Chronic Toxoplasmosis
Janetka, James W.,Hopper, Allen T.,Yang, Ziping,Barks, Jennifer,Dhason, Mary Savari,Wang, Qiuling,Sibley, L. David
supporting information, p. 6144 - 6163 (2020/07/10)
Calcium dependent protein kinase 1 (CDPK1) is an essential Ser/Thr kinase that controls invasion and egress by the protozoan parasite Toxoplasma gondii. The Gly gatekeeper of CDPK1 makes it exquisitely sensitive to inhibition by small molecule 1H-pyrazolo
Selective aliphatic carbon-hydrogen bond activation of protected alcohol substrates by cytochrome P450 enzymes
Bell, Stephen G.,Spence, Justin T. J.,Liu, Shenglan,George, Jonathan H.,Wong, Luet-Lok
, p. 2479 - 2488 (2014/04/03)
Protected cyclohexanol and cyclohex-2-enol substrates, containing benzyl ether and benzoate ester moieties, were designed to fit into the active site of the Tyr96Ala mutant of cytochrome P450cam. The protected cyclohexanol substrates were efficiently and selectively hydroxylated by the mutant enzyme at the trans C-H bond of C-4 on the cyclohexyl ring. The selectivity of oxidation of the benzoate ester protected cyclohexanol could be altered by making alternative amino acid substitutions in the P450cam active site. The addition of the double bond in the cyclohexyl ring of the benzoate ester protected cyclohex-2-enol has a debilitative effect on the activity of the Tyr96Ala mutant with this substrate. However, the Phe87Ala/Tyr96Phe double mutant, which introduces space at a different location in the active site than the Tyr96Ala mutant, was able to efficiently hydroxylate the C-H bonds of 1-cyclohex-2-enyl benzoate at the allylic C-4 position. Mutations at Phe87 improved the selectivity of the oxidation of 1-phenyl-1-cyclohexylethylene to trans-4-phenyl-ethenylcyclohexanol (92%) when compared to single mutants at Tyr96 of P450cam. the Partner Organisations 2014.
Biohydroxylation reactions catalyzed by enzymes and whole-cell systems
Flitsch, Sabine L.,Aitken, Suzanne J.,Chow, Cathy S.-Y.,Grogan, Gideon,Staines, Adam
, p. 81 - 90 (2007/10/03)
The biohydroxylation of a number of cyclic substrates (3-24) containing aromatic side chains was used to compare substrate specificity and selectivity of hydroxylation using microbial enzymes and whole-cell biocatalysts. In general, the regioselectivity of reaction was remarkably similar between the different catalysts in that little aromatic or benzylic, but significant aliphatic hydroxylation was observed. However, a more detailed investigation of isolated products showed complementary substrate specificity, functional group compatibility, and regioselectivity of hydroxylation. Substrate specificity and regioselectivity could be further modulated by small changes to the nature of the aromatic side chain, which appears to play an important role in substrate recognition.
