[NMR paper] 19 F-NMR shows that active site aromatic residues in CYP121 of Mycobacterial tuberculosisplay a dual role in substrate interaction and protein structure
19 F-NMR shows that active site aromatic residues in CYP121 of Mycobacterial tuberculosisplay a dual role in substrate interaction and protein structure
CYP121 is an essential cytochrome P450 enzyme (CYP) from Mycobacterium tuberculosis.CYP121 mediates an atypical phenol-coupling reaction that converts cyclodityrosine (cYY) into mycocylosin. Our lab has previously employed a ^(19) F nuclear magnetic resonance (NMR) label, 3-bromo-1,1,1-trifluoroacetone (BTFA), to study dynamics of the FG-loop, a region connecting the F and G-helices. In other CYPs, the FG-loop region has been implicated in active site access and substrate recognition. The ^(19)...
[ASAP] Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues
Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b00297/20190509/images/medium/bi-2019-00297r_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b00297
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Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01325/20160115/images/medium/bi-2015-01325p_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01325
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Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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[NMR paper] Involvement of various amino- and carboxyl-terminal residues in the active site of th
Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins.
Related Articles Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with...
19 F-NMR shows that active site aromatic residues in CYP121 of Mycobacterial tuberculosisplay a dual role in substrate interaction and protein structure
Linear Mode
