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Biosynthesis of isoprenoids: characterization of a functionally active recombinant 2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) from Mycobacterium tuberculosis H37Rv.
- W. Shi, Jian-Fei Feng, Honghai Wang
- Biology, ChemistryJournal of biochemistry and molecular biology
- 30 November 2007
This study is expected to help better understand the features of IspD and provide useful information for the development of novel antibiotics to treat M. tuberculosis.
Rhodopsin Mutants Discriminate Sites Important for the Activation of Rhodopsin Kinase and G(*)
- W. Shi, S. Osawa, C. D. Dickerson, E. Weiss
- Biology, ChemistryThe Journal of Biological Chemistry
- 3 February 1995
This work has identified mutants that fall into three distinct categories: those that show altered phosphorylation but normal Gt activation, such as T62A/V63A/Q64A and R147A/F148A/G149A in Loops I and II, respectively; mutants that have reduced ability to activate Gt but are phosphorylated normally, including T242A/T243A and V250 a/T251A/R252A in Loop III.
Purine nucleoside phosphorylase from Mycobacterium tuberculosis. Analysis of inhibition by a transition-state analogue and dissection by parts.
The M. tuberculosis deoD gene encodes a presumptive purine nucleoside phosphorylase (PNP) that is trimeric, similar to mammalian PNP's but unlike the hexameric Escherichia coli enzyme.
A transition-state analogue reduces protein dynamics in hypoxanthine-guanine phosphoribosyltransferase.
- F. Wang, W. Shi, E. Nieves, R. Angeletti, V. Schramm, C. Grubmeyer
- 10 July 2001
Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is the key enzyme in purine base salvage in humans and in purine auxotrophs, including Plasmodium falciparum, the leading cause of malaria.…
Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal.
- W. Shi, C. Sports, D. Raman, S. Shirakawa, S. Osawa, E. Weiss
- Biology, ChemistryBiochemistry
- 7 April 1998
Surprisingly, several of the mutants could be phosphorylated by rhodopsin kinase and could bind arrestin in the absence of 11-cis-retinal but were not able to activate Gt, the rod cell G protein, transducin.
Sizing of bovine heart and kidney pyruvate dehydrogenase complex and dihydrolipoyl transacetylase core by quasielastic light scattering.
Quasielastic light scattering measurements on several preparations of bovine heart and kidney pyruvate dehydrogenase complex yielded hydrodynamic radii ranging from 25.7 to 30 nm, which indicate that the larger number of pyruVate dehydration components in the heart complex than the kidney complex associate without radial expansion of the heartcomplex.
Effects of carboxyl-terminal truncation on the stability and G protein-coupling activity of bovine rhodopsin.
Data suggest that the proximal region of the carboxyl terminus is critical for the proper folding and stability of the rhodopsin molecule and that amino acids Cys316 to Ala348 are not necessary for the activation of Gt.
Electron paramagnetic resonance and electron nuclear double resonance spectroscopic identification and characterization of the tyrosyl radicals in prostaglandin H synthase 1.
It is concluded that a tyrosyl residue other than the catalytically essential Y385 species is most likely responsible for the indomethacin-inhibited, narrow-singlet spectrum and this inhibitor may function by redirecting radical formation to a catalysttically inactive side chain.
Aspartate-407 in Rhodobacter sphaeroides cytochrome c oxidase is not required for proton pumping or manganese binding.
Results suggest that Asp407 does not play a critical role in proton translocation or in Mn/Mg binding, as evidenced by visible, EPR, and resonance Raman spectroscopy.
Tyrosyl radicals in enzyme catalysis: some properties and a focus on photosynthetic water oxidation.
General properties of the radical enzymes are summarized from which it is concluded that their essential role in catalysis is to initiate substrate metabolism by hydrogen-atom abstraction.