Brian G MillerSummaryAffiliation: University of Wisconsin Country: USA Publications
| Collaborators
|
Detail Information
Publications
Catalytic proficiency: the unusual case of OMP decarboxylaseBrian G Miller
Department of Biochemistry, University of Wisconsin, Madison, Wisconsin, 53706 1544, USA
Annu Rev Biochem 71:847-85. 2002..Very large connectivity effects are indicated by the results of experiments testing how transition state stabilization is affected by the truncation of binding determinants of the substrate and the active site...
Carbon isotope effect study on orotidine 5'-monophosphate decarboxylase: support for an anionic intermediateJeremy L Van Vleet
Institute for Enzyme Research and Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53726, USA
Biochemistry 47:798-803. 2008..The isotope effect for the decarboxylation of the slow substrate 2'-deoxy-OMP produced a intrinsic isotope effect of nearly 1.0461...
Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinasesBrian G Miller
Department of Biochemistry, University of Wisconsin Madison, Madison, Wisconsin 53706 1544, USA
Biochemistry 43:6387-92. 2004..Our findings suggest that modern genomes harbor a wealth of latent enzyme activities and that extant metabolic pathways are equivocal, in contrast to their usual depiction...
Reconstitution of a defunct glycolytic pathway via recruitment of ambiguous sugar kinasesBrian G Miller
Department of Biochemistry, University of Wisconsin, Madison 53706 1544, USA
Biochemistry 44:10776-83. 2005....
Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificityMioara Larion
Department of Chemistry and Biochemistry, The Florida State University, Tallahassee, Florida 32306 4390, USA
Biochemistry 46:13564-72. 2007..This finding is consistent with an evolutionary process that includes the formation of intermediates possessing relaxed substrate specificities during the initial steps of enzyme functional divergence...
The mutability of enzyme active-site shape determinantsBrian G Miller
Department of Chemistry and Biochemistry, The Florida State University, Tallahassee, Florida 32306 4390, USA
Protein Sci 16:1965-8. 2007..These findings establish non-hydrogen bonding shape determinants as highly appealing targets for widespread substitution during efforts to redesign the catalytic properties of natural enzymes...
OMP decarboxylase--An enigma persistsBrian P Callahan
Division of Infectious Disease, Wadsworth Center NYS DOH, Albany, NY 12202, USA
Bioorg Chem 35:465-9. 2007..In this perspective, we provide a summary of the reaction pathways under consideration for ODCase, highlight the supporting and refuting data, and suggest experiments designed to further test each of the candidate pathways...
A metabolic bypass of the triosephosphate isomerase reactionKevin K Desai
Department of Chemistry and Biochemistry, 217 Dittmer Laboratory of Chemistry, Florida State University, Tallahassee, Florida 32306 4390, USA
Biochemistry 47:7983-5. 2008..This transformation provides an alternate pathway to the formation of dihydroxyacetone phosphate...
