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Agricultural Research Service United States Department of Agriculture
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Jay D Braker
Bioenergy Research Unit
Biological Science Lab Technician

Phone: (309) 681-6074
Fax: (309) 681-6427
Room 2133
1815 N UNIVERSITY STREET
PEORIA, IL, 61604-3999


Publications (Clicking on the reprint icon Reprint Icon will take you to the publication reprint.)
Activation of a GH43 ß-xylosidase by divalent metal cations: slow binding of divalent metal and high substrate specificity - (Peer Reviewed Journal) - (27-Feb-13)
Highly active ß-xylosidases of glycoside hydrolase family 43 - (Peer Reviewed Journal) - (25-Sep-12)
Plant cell walls to ethanol. - (Peer Reviewed Journal)
Jordan, D.B., Bowman, M.J., Braker, J.D., Dien, B.S., Hector, R.E., Lee, C.C., Mertens, J.A., Wagschal, K.C. 2012. Plant cell walls to ethanol. Biochemical Journal. 442:247-252.
Opposing influences by subsite -1 and subsite +1 residues on relative xylopyranosidase/arabinofuranosidase activities of bifunctional beta-D-xylosidase/alpha-L-arabinofuranosidase - (Peer Reviewed Journal)
Jordan, D.B., Braker, J.D. 2011. Opposing influences by subsite -1 and subsite +1 residues on relative xylopyranosidase/arabinofuranosidase activities of bifunctional beta-D-xylosidase/alpha-L-arabinofuranosidase. Biochimica et Biophysica Acta. 1814:1648-1657.
Kinetic mechanism of an aldehyde reductase of Saccharomyces cerevisiae that relieves toxicity of furfural and 5-hydroxymethylfurfural - (Peer Reviewed Journal)
Jordan, D.B., Braker, J.D., Bowman, M.J., Vermillion, K., Moon, J., Liu, Z. 2011. Kinetic mechanism of an aldehyde reductase of Saccharomyces cerevisiae that relieves toxicity of furfural and 5-hydroxymethylfurfural. Biochimica et Biophysica Acta. 1814:1686-1694.
Catalytic properties of ß-D-xylosidase XylBH43 from Bacillus halodurans C-125 and mutant XylBH43-W147G - (Peer Reviewed Journal)
Wagschal, K.C., Jordan, D.B., Braker, J.D. 2011. Expression, characterization, and site-directed mutagenesis of ß-D-xylosidase XylBH43 from Bacillus halodurans C-125. Process Biochemistry. doi:10.1016/j.procbio.2011.07.009.
Engineering lower inhibitor affinities in beta-D-xylosidase of Selenomonas ruminantium by site-directed mutagenesis of Trp145 - (Peer Reviewed Journal)
Jordan, D.B., Wagschal, K.C., Zhanmin, F., Yuan, L., Braker, J.D., Heng, C. 2011. Engineering lower inhibitor affinities in beta-D-xylosidase of Selenomonas ruminantium by site-directed mutagenesis of Trp145. Journal of Industrial Microbiology and Biotechnology. 38:1821-1835.
Stereochemistry of Furfural Reduction by a Saccharomyces cerevisiae Aldehyde Reductase That Contributes to In Situ Furfural Detoxification - (Peer Reviewed Journal)
Bowman, M.J., Jordan, D.B., Vermillion, K., Braker, J.D., Moon, J., Liu, Z. 2010. Stereochemistry of Furfural Reduction by a Saccharomyces cerevisiae Aldehyde Reductase That Contributes to In Situ Furfural Detoxification. Applied and Environmental Microbiology. 76(15):4926-4932.
Catalytic properties of two Rhizopus oryzae 99-880 glucoamylase enzymes without starch binding domains expressed in Pichia pastoris - (Peer Reviewed Journal)
Mertens, J.A., Braker, J.D., Jordan, D.B. 2010. Catalytic properties of two Rhizopus oryzae 99-880 glucoamylase enzymes without starch binding domains expressed in Pichia pastoris. Applied Biochemistry and Biotechnology. 162(8):2197-2213.
Engineering lower inhibitor affinities in beta-D-xylosidase by site-directed mutagenesis of Trp 145 - (Abstract Only)
Jordan, D.B., Wagschal, K.C., Fan, Z., Yuan, L., Braker, J.D., Heng, C. 2010. Engineering lower inhibitor affinities in beta-D-xylosidase by site-directed mutagenesis of Trp 145. Meeting Abstract. 84.
Beta-D-xylosidase from Selenomonas ruminantium: Role of Glutamate 186 in Catalysis Revealed by Site-Directed Mutagenesis, Alternate Substrates, and Active-site Inhibitor - (Peer Reviewed Journal)
Jordan, D.B., Braker, J.D. 2010. Beta-D-xylosidase from Selenomonas ruminantium: Role of Glutamate 186 in Catalysis Revealed by Site-directed Mutagenesis, Alternate Substrates, and Active-site Inhibitor. Applied Biochemistry and Biotechnology. 161(1-8):395-410.
Engineering Lower Inhibitor Affinities in Beta-D-Xylosidase - (Peer Reviewed Journal)
Fan, Z., Yuan, L., Jordan, D.B., Wagschal, K.C., Heng, C., Braker, J.D. 2010. Engineering lower inhibitor affinities in beta-D-xylosidase. Applied Microbiology and Biotechnology. 86(4):1099-1113.
Beta-D-xylosidase from Selenomonas ruminantium: Role of Glutamate 186 in Catalysis Revealed by Site-directed Mutagenesis, Alternate Substrates, and Inhibitor - (Abstract Only) - (31-Jul-09)
Beta-D-xylosidase from Selenomonas ruminantium: role of glutamate 186 in catalysis revealed by site-directed mutagenesis, alternate substrates, and inhibitors - (Abstract Only) - (06-May-09)
Beta-D-xylosidase from Selenomonas ruminantium: thermodynamics of enzyme-catalyzed and noncatalyzed reactions - (Peer Reviewed Journal)
Jordan, D.B., Braker, J.D. 2009. Beta-D-xylosidase from Selenomonas ruminantium: Thermodynamics of Enzyme-catalyzed and Noncatalyzed Reactions. Applied Biochemistry and Biotechnology. 155(1-3):330-346.
Aminoalcohols as Probes of the Two-subsite Active Site of Beta-D-xylosidase from Selenomonas ruminantium - (Peer Reviewed Journal)
Jordan, D.B., Mertens, J.A., Braker, J.D. 2009. Aminoalcohols as Probes of the Two-subsite Active Site of Beta-D-xylosidase from Selenomonas ruminantium. Biochimica et Biophysica Acta. 1794(1):144-158.
Beta-D-xylosidase from Selenomonas ruminantium: thermodynamics of enzyme-catalyzed and noncatalyzed reactions - (Abstract Only) - (18-Jul-08)
Beta-D-xylosidase from Selenomonas ruminantium: thermodynamics of enzyme-catalyzed and noncatalyzed reactions - (Abstract Only) - (07-May-08)
Beta-D-xylosidase from Selenomonas ruminantium: catalyzed reactions with natural substrates - (Abstract Only) - (07-May-08)
INHIBITION OF THE TWO-SUBSITE BETA-D-XYLOSIDASE FROM SELENOMONAS RUMINANTIUM BY SUGARS: COMPETITIVE, NONCOMPETITIVE, DOUBLE BINDING, AND SLOW BINDING MODES - (Peer Reviewed Journal)
Jordan, D.B., Braker, J.D. 2007. Inhibition of the two-subsite beta-d-xylosidase from Selenomonas ruminantium by sugars: competitive, noncompetitive, double binding, and slow binding modes. Archives of Biochemistry and Biophysics. 465(1):231-246.

   
 
Last Modified: 05/22/2013
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