Miller Laboratory

Enzyme function, structure, and evolution


Whittington, A. C., Larion, M., Bowler, J. M., Ramsey, K.M., Brüschweiler, R., Miller, B.G. (2015) Dual allosteric activation mechanisms in monomeric human glucokinaseProceedings of the National Academy of Sciences doi:10.1073/pnas.1506664112

Larion, M., Hansen, A. L., Zhang, F,. Bruschweiler-Li, L., Tugarinov, V., Miller, B. G., Brüschweiler, R. (2015) Kinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small DomainAngewandte Chemie 127, 8247-8250.

Larion, M., Miller, B., Brüschweiler, R. (2015) Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study, Intrinsically Disordered Proteins 3 (1), 1-4


Martinez, J. A., Larion M., Conejo M.S., Porter C.M., and Miller, B. G. (2014) Role of connecting loop I in catalysis and allosteric regulation of human glucokinaseProtein Science 23, 915-922.

Schulenburg C. and Miller, B. G. (2014) Enzyme Recruitment and Its Role in Metabolic ExpansionBiochemistry 53, 836–845.


Beck, T. and Miller, B. G. (2013) Structural basis for regulation of human glucokinase by glucokinase regulatory proteinBiochemistry 52.

Xiao, Q., Jackson, J. J., Basak, A., Bowler, J. M., Miller B. G. and Zakarian, A. (2013) Enantioselective synthesis of tatanans A-C and reinvestigation of their glucokinase activating propertiesNature Chem. 5, 410-416.

Bowler, J. M., Hervert, K. L., Kearley, M. L., and Miller B. G. (2013) Small-molecule allosteric activation of human glucokinase in the absence of glucose, ACS Med. Chem. Lett. 4, 580-584.


Larion, M., Salinas, R. K., Bruschweiler-Li, L., Miller, B. G., and Brüschweiler, R. (2012) Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinasePLoS Biol. 10, e1001452. 

Larion, M. and Miller, B. G. (2012) Homotropic allosteric regulation in monomeric mammalian glucokinaseArch. Biochem. Biophys. 519, 103-111.

Porter, C. M., and Miller B. G. (2012) Cooperativity in monomeric enzymes with single ligand-binding sitesBioorg. Chem. 43, 44-50.


Larion, M. and Miller, B. G. (2010) Global fit analysis of glucose binding curves reveals a minimal model for kinetic cooperativity in human glucokinase, Biochemistry 49, 8902-8911.

Desai, K. K., and Miller B. G. (2010) Recruitment of genes and enzymes conferring resistance to the nonnatural toxin bromoacetateProc. Natl. Acad. Sci. USA 107, 17968-17973.

Larion, M., Salinas, R.K., Bruschweiler-Li, L., Brüschweiler, R., and Miller B. G. (2010) Direct evidence for conformational heterogeneity in human pancreatic glucokinase from high-resolution NMRBiochemistry 49, 7969-7971.

Conejo, M. S., Thompson, S. M., and Miller B. G. (2010) Evolutionary bases of carbohydrate recognition and substrate discrimination in the ROK protein familyJ. Mol. Evol. 70, 545-556.

Desai, K. K., and Miller, B. G. (2010) L-Glyceraldehyde 3-phosphate reductase from Escherichia coli is a heme binding proteinBioorg. Chem. 38, 37-41.


Larion, M., and Miller, B. G. (2009) 23-residue C-terminal α-helix governs kinetic cooperativity in monomeric human glucokinaseBiochemistry 48, 6157-6165.

Desai, K. K.; Miller, B. G. (2009) Assessing and exploiting the persistence of substrate ambiguity in modern protein catalysts. In Protein Engineering Handbook; Bornscheuer, U. and Lutz, S. Eds. Wiley-VCH, 343-359.

Pal, P., and Miller, B. G. (2009) Activating mutations in the human glucokinase gene revealed by genetic selectionBiochemistry 48, 814-816.


Desai, K. K., and Miller, B. G. (2008) A metabolic bypass of the triosephosphate isomerase reactionBiochemistry 47, 7983-7985.

Van Vleet, J. L., Reinhardt, L. A., Miller, B. G., Sievers, A. and Cleland, W. W. (2008) Carbon isotope effect study on orotidine 5’-monophosphate decarboxylase: support for an anionic intermediateBiochemistry 47, 798-803.


Larion, M., Moore, L. B., Thompson, S. T., and Miller, B. G. (2007) Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificityBiochemistry 46, 13564-13772.

Callahan, B. P. and Miller, B. G. (2007) OMP decarboxylase – an enigma persists,Bioorg. Chem. 35, 465-469.

Miller, B. G. (2007) The mutability of enzyme active-site shape determinantsProt. Sci. 16, 1965-1968.

Dhar, P., Cao, Y., Kline, T., Pal, P., Swayne, C., Fischer, T., Miller, B., Sen, A. and Johansen, T. (2007) Autonomously moving local nanoprobes in heterogeneous magnetic fieldsJ. Phys. Chem. C. 111, 3607-3613.

Publications prior to 2007

Miller, B. G., and Raines, R. T. (2005) Reconstitution of a defunct glycolytic pathway via recruitment of ambiguous sugar kinases, Biochemistry 44, 10776-10783. 

Miller, B. G. (2004) Insight into the catalytic mechanism of orotidine 5´-phosphate decarboxylase from crystallography and mutagenesis, Topics in Curr. Chem. 238, 43-62.  

Miller, B. G., and Raines, R. T. (2004) Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases, Biochemistry 43, 6387-6392.  

Miller, B. G., and Wolfenden, R. (2002) Catalytic proficiency: the unusual case of OMP decarboxylase, Annu. Rev. Biochem. 71, 847-885.  

Miller, B. G., Snider, M. J., Wolfenden, R., and Short, S. A. (2001) Dissecting a charged network at the active site of orotidine 5´-phosphate decarboxylase, J. Biol. Chem. 276, 15174-15176.  

Miller, B. G., Butterfoss, G. L., Short, S. A., and Wolfenden, R. (2001) Role for enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5´-phosphate decarboxylase: a role for substrate destabilization? Biochemistry 40, 6227-6232.  

Miller, B. G., Snider, M. J., Short, S. A., and Wolfenden, R. (2000) Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5´-phosphate decarboxylase, Biochemistry 39, 8113-8118.  

Miller, B. G., Hassell, A. M., Milburn, M. V., and Short, S. A. (2000) Crystallization of native and selenomethionyl yeast orotidine 5´-phosphate decarboxylase, Acta Crystallogr. Sect. D: Biol. Crystallogr. 56, 474-474.

Miller, B. G., Hassell, A. M., Wolfenden, R., Milburn, M. V., and Short, S. A. (2000) Anatomy of a proficient enzyme: the structure of orotidine 5´-monophosphate decarboxylase in the presence and absence of a potential transition state analog, Proc. Natl. Acad. Sci. USA 97, 2011-2016. 

Miller, B. G., Smiley, J. A., Short, S. A., and Wolfenden, R. (1999) Activity of yeast orotidine 5´-phosphate decarboxylase in the absence of metals, J. Biol. Chem. 274, 23841-23843. 

Wolfenden, R., Snider, M., Ridgway, C., and Miller, B. (1999) The temperature dependence of enzyme rate enhancements, J. Am. Chem. Soc. 121, 7419-7420. 

Miller, B. G., Traut, T. W., and Wolfenden, R. (1998) Effects of substrate binding determinants in the transition state for orotidine 5´-monophosphate decarboxylase, Bioorg. Chem. 26, 283-288.

Miller, B. G., Traut, T. W., and Wolfenden, R. (1998) A role for zinc in OMP decarboxylase, an unusually proficient enzyme, J. Am. Chem. Soc. 120, 2666-2667.