Dr. Martin St. Maurice’s Publications 2013 Lin, Y., and St. Maurice, M. 2013. The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family. Biochemistry. 52: 690-700. 2012 Waldrop, G.L., Holden, H.M., and St. Maurice, M. 2012. The enzymes of biotin dependent CO2 metabolism: What structures reveal about their reaction mechanisms. Protein Science 21(11):1597-1619. Adina-Zada, A., Sereeruk, C., Jitrapakdee, S., Zeczycki, T.N., St. Maurice, M., Cleland, W.W., Wallace, J.C., and Attwood, P.V. 2012. Roles of Arg427 and Arg472 in the binding and allosteric effects of acetyl CoA in pyruvate carboxylase. Biochemistry 51(41): 1597-1619. 2011 Adina-Zada, A., Hazra, R., Sereeruk, C., Jitrapakdee, S., Zeczycki, T.N., St. Maurice, M., Cleland, W.W., Wallace, J.C., and Attwood, P.V. 2011. Probing the allosteric activation of pyruvate carboxylase using 2′,3′-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate as a fluorescent mimic of the allosteric activator acetyl CoA. Arch. Biochem. Biophys. 117-126. Zeczycki, T.N., Menefee, A.L., Jitrapakdee, S., Wallace, J.C., Attwood, P.V., St. Maurice, M. and Cleland, W.W. 2011. Activation and inhibition of pyruvate carboxylase from Rhizobium etli. Biochemistry. 9694-9707. Lietzan, A.D., Menefee, A.L., Zeczycki, T.N., Kumar, S., Attwood, P.V., Wallace, J.C., Cleland, W.W. and St. Maurice, M. 2011. Interaction between the biotin carrier domain and the biotin carboxylase domain in the structure of Rhizobium etli pyruvate carboxylase. Biochemistry. 9708-9723. Zeczycki, T.N., Menefee, A.L., Adina-Zada, A., Surinya, K.H., Wallace, J.C., Attwood, P.V., St. Maurice, M., and Cleland, W.W. 2011. Novel insights into the biotin carboxylase reaction of pyruvate carboxylase from Rhizobium etli. Biochemistry. 9724-9737. 2010 Duangpan, S., Jitrapakdee, S., Adina-Zada, A., Byrne, L., Zeczycki, T.N., St. Maurice, M., Cleland, W.W., Wallace, J.C. and Attwood, P.V. 2010. Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis. Biochemistry. 49: 3296-3304. Zeczycki, T.N., St. Maurice, M., and Attwood, P.V. 2010. Inhibitors of pyruvate carboxylase, Open Enz. Inhibit. J. 3: 8-26. At Marquette University 2009 Mera, P.E., St. Maurice, M., Rayment, I., and Escalante-Semerena, J.C. “Residue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of Lactobacillus reuteri is critical to the formation of the four-coordinate Co(II) corrinoid substrate and to the activity of the enzyme” Biochemistry 48, 3138-3145. Zeczycki, T.N., St. Maurice, M., Jitrapakdee, S., Wallace, J.C., Attwood, P.V., and Cleland, W.W. 2009. “Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli” Biochemistry 48, 4305–4313 2008 Jitrapakdee, S., M. St. Maurice, I. Rayment, W.W. Cleland, J.C. Wallace, and P.V. Attwood,. 2008. Structure, mechanism and regulation of pyruvate carboxylase. Biochem. J., 413:369-387. St. Maurice, M., P. Mera, K. Park, T.C. Brunold, J.C. Escalante-Semerena, and I. Rayment. 2008. Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate. Biochemistry, 47:5755-5766. 2007 Mera, P.E., M. St. Maurice, I. Rayment, and J.C. Escalante-Semerena. 2007. Structural and functional analyses of the human-type corrinoid adenosyltransferase (PduO) from Lactobacillus reuteri” Biochemistry, 46:13829-13836. St. Maurice, M., L. Reinhardt, K.H. Surinya, P.V. Attwood, J.C. Wallace, W.W. Cleland, and I. Rayment. 2007. Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme. Science, 317:1076-1079. St. Maurice, M., N. Cremades, M.A. Croxen, G. Sisson, J. Sancho and P.S. Hoffman. 2007. Flavodoxin: Quinone Reductase (FqrB): A redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni. J. Bacteriol., 189:4764-4773. St. Maurice, M., P.E. Mera, M.P. Taranto, F. Sesma, J.C. Escalante-Semerena, and I. Rayment. 2007. Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri. J. Biol. Chem., 282:2596-2605. 2005 Siddiqi, F., J.R. Bourque, H. Jiang, M. Gardner, M. St. Maurice, C. Blouin, and S.L. Bearne. 2005. Perturbing the hydrophobic pocket of mandelate racemase to probe phenyl motion during catalysis. Biochemistry, 44:9013-9021. 2004 Brosseau, C.L., M. St. Maurice, S.L. Bearne, and S.G.Roscoe. 2004. Electrochemical quartz crystal nanobalance (EQCN) studies of the adsorption behaviour of an enzyme, mandelate racemase, and its substrate, mandelic acid, on Pt. Electrochim. Acta, 50:1289-1297. St. Maurice, M. and S.L. Bearne. 2004. Hydrophobic nature of the active site of mandelate racemase. Biochemistry, 43:2524-2532. 2003 St. Maurice, M., S.L. Bearne, W. Lu, and S.D. Taylor. 2003. Inhibition of mandelate racemase by -fluorobenzylphosphonates. Bioorg. Med. Chem. Lett., 13:2041-2044. 2002 St. Maurice, M. and S.L. Bearne. 2002. Kinetics and thermodynamics of mandelate racemase catalysis. Biochemistry, 41:4048-4058. 2002 St. Maurice, M. and S.L. Bearne. 2000. Reaction intermediate analogues for mandelate racemase: interaction between Asn 197 and the -hydroxyl of the substrate promotes catalysis. Biochemistry, 39:13324-13335. 1999 Bearne, S.L., M. St. Maurice, and M.D. Vaughan. 1999. An assay for mandelate racemase using high performance liquid chromatography. Anal. Biochem., 269:332-336. .