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Creator:: Perkins, Arden, Nelson, Kimberly J., Parsonage, Derek, Poole, Leslie B., and Karplus, P. Andrew
Abstract:: Peroxiredoxins (Prxs) are a ubiquitous family of cysteine-dependent peroxidase enzymes that play dominant roles in regulating peroxide levels within cells. These enzymes, often present at high levels and capable of rapidly clearing peroxides, display a remarkable array of variations in their oligomeric states and susceptibility to regulation by hyperoxidative inactivation...
Resource Type:: Article
Full Text:: , 1 Kimberly J. Nelson, 2 Derek Parsonage,2 Leslie B. Poole 2* and P. Andrew Karplus1* 1

Creator:: Nelson, Kimberly J., Parsonage, Derek, Karplus, P. Andrew, and Poole, Leslie B.
Abstract:: Peroxiredoxins (Prxs) are very effective peroxide reducing enzymes, but also are susceptible to being oxidatively inactivated by their own substrates. The level of sensitivity to such hyperoxidation varies depending both on the enzyme involved and the type of peroxide substrate. For some Prxs, the hyperoxidation has physiological relevance, so it...
Resource Type:: Article
Full Text:: sensitivity towards inactivation by peroxide substrates Kimberly J. Nelson1, Derek Parsonage1, P

Creator:: Elkhal, Callia K., Kean, Kelsey M., Parsonage, Derek, Maenpuen, Somchart, Chaiyen, Pimchai, Claiborne, Al, and Karplus, P. Andrew
Abstract:: The formation of hydrogen peroxide (H₂O₂) by the FAD-dependent α-glycerophosphate oxidase (GlpO), is important for the pathogenesis of Streptococcus pneumoniae and Mycoplasma pneumoniae. The structurally known GlpO from Streptococcus sp. (SspGlpO) is similar to the pneumococcal protein (SpGlpO) and provides a guide for drug design against that target. However, M....
Resource Type:: Article
Full Text:: -glycerophosphate oxidase from Mycoplasma pneumoniae Callia K. Elkhal,1# Kelsey Kean,1# Derek Parsonage,2

Creator:: Maenpuen, Somchart, Watthaisong, Pratchaya, Supon, Pacharee, Sucharitakul, Jeerus, Parsonage, Derek, Karplus, P. Andrew, Claiborne, Al, and Chaiyen, Pimchai
Abstract:: L-α-glycerophosphate oxidase is an FAD-dependent enzyme that catalyzes the oxidation of L-α-glycerophosphate (Glp) by molecular oxygen to generate dihydroxyacetone phosphate (DHAP) and hydrogen peroxide (H₂O₂). The catalytic properties of the recombinant His₆-GlpO from Mycoplasma pneumoniae (His₆-MpGlpO) were investigated with transient and steady-state kinetics and ligand binding. The results indicate that...
Resource Type:: Article
Full Text:: , Pacharee Supon1, Jeerus Sucharitakul2, 4 Derek Parsonage3, P. Andrew Karplus4, Al Claiborne3and Pimchai

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