@article{gao_bauer_shockley_pysz_kelly_2003, title={Growth of hyperthermophilic Archaeon Pyrococcus futiosus on chitin involves two family 18 chitinases}, volume={69}, ISSN={["1098-5336"]}, DOI={10.1128/AEM.69.6.3119-3128.2003}, abstractNote={ABSTRACT}, number={6}, journal={APPLIED AND ENVIRONMENTAL MICROBIOLOGY}, author={Gao, J and Bauer, MW and Shockley, KR and Pysz, MA and Kelly, RM}, year={2003}, month={Jun}, pages={3119–3128} }
 @article{chang_parker_bauer_kelly_2001, title={alpha-Glucosidase from Pyrococcus furiosus}, volume={330}, journal={Hyperthermophilic enzymes. Part A}, publisher={San Diego, Calif.: Academic Press}, author={Chang, S. T. and Parker, K. N. and Bauer, M. W. and Kelly, R. M.}, year={2001}, pages={260–269} }
 @article{cady_bauer_callen_snead_mathur_short_kelly_2001, title={beta-Endoglucanase from Pyrococcus furiosus}, volume={330}, journal={Hyperthermophilic enzymes. Part A}, publisher={San Diego, Calif.: Academic Press}, author={Cady, S. G. and Bauer, M. W. and Callen, W. and Snead, M. A. and Mathur, E. J. and Short, J. M. and Kelly, R. M.}, year={2001}, pages={346–354} }
 @article{bauer_driskill_callen_snead_mathur_kelly_1999, title={An endoglucanase, eglA, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes beta-1,4 bonds in mixed-linkage(1 -> 3),(1 -> 4)-beta-D-glucans and cellulose}, volume={181}, number={1}, journal={Journal of Bacteriology}, author={Bauer, M. W. and Driskill, L. E. and Callen, W. and Snead, M. A. and Mathur, E. J. and Kelly, R. M.}, year={1999}, pages={284–290} }
 @article{driskill_kusy_bauer_kelly_1999, title={Relationship between glycosyl hydrolase inventory and growth physiology of the hyperthermophile Pyrococcus furiosus on carbohydrate-based media}, volume={65}, number={3}, journal={Applied and Environmental Microbiology}, author={Driskill, L. E. and Kusy, K. and Bauer, M. W. and Kelly, R. M.}, year={1999}, pages={893–897} }
 @article{driskill_bauer_kelly_1999, title={Synergistic interactions among beta-laminarinase, beta-1,4-glucanase, and beta-glucosidase from the hyperthermophilicarchaeon Pyrococcus furiosus during hydrolysis of beta-1,4-,beta-1,3-, and mixed-linked polysaccharides}, volume={66}, DOI={10.1002/(SICI)1097-0290(1999)66:1<51::AID-BIT5>3.3.CO;2-B}, abstractNote={The synergistic interaction among three β-specific glycosidases from the hyperthermophilic archaeon Pyrococcus furiosus, namely two endoglucanases (EglA and LamA) and an exo-acting β-glucosidase (Bgl), on barley-glucan and laminarin, was examined. In addition to following glucose release and the generation of reducing sugar ends, the distribution and amounts of oligomeric products from β-1,3- and β-1,4-linked substrates were determined as a function of extent of hydrolysis at 98°C. Positive interactions were noted between endo/exo glucanase combinations, leading to enhanced and rapid degradation of the larger complex carbohydrates to oligosaccharides. The EglA/LamA endo-acting combination was also synergistic in degrading barley-glucan. However, hydrolysis was most efficient when a blend of all three hydrolases was used, possibly due to the relief of product inhibition by the exoglyosidase. Furthermore, by monitoring the distribution of oligosaccharides present during hydrolysis, patterns of enzymatic attack could be followed in addition to determining the specific contributions of each hydrolase to the overall process. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 66: 51–60, 1999.}, number={1}, journal={Biotechnology and Bioengineering}, author={Driskill, L. E. and Bauer, M. W. and Kelly, Robert}, year={1999}, pages={51–60} }
 @misc{bauer_driskill_kelly_1998, title={Glycosyl hydrolases from hyperthermophilic microorganisms}, volume={9}, ISSN={["0958-1669"]}, DOI={10.1016/S0958-1669(98)80106-7}, abstractNote={Glycosyl hydrolases from hyperthermophiles are, thus far, the most widely studied enzyme class from these organisms. Not only are there many biotechnological opportunities for these enzymes, but the rapidly increasing amount of information about their genetic, biochemical and biophysical characteristics (recently genomic sequencing data for both P. furiosus and P. horikoshi have been published on the Internet) make them ideal candidates for the study of biocatalysis and protein thermostability at extremely high temperatures.}, number={2}, journal={CURRENT OPINION IN BIOTECHNOLOGY}, author={Bauer, MW and Driskill, LE and Kelly, RM}, year={1998}, month={Apr}, pages={141–145} }
 @article{bauer_kelly_1998, title={The family 1 beta-glucosidases from Pyrococcus furiosus and Agrobacterium faecalis share a common catalytic mechanism}, volume={37}, ISSN={["0006-2960"]}, DOI={10.1021/bi9814944}, abstractNote={Comparisons of catalytic mechanisms have not previously been performed for homologous enzymes from hyperthermophilic and mesophilic sources. Here, the beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus was recombinantly produced in Escherichia coli and shown to have biophyscial and biochemical properties identical to those of the wild-type enzyme. Moreover, the recombinant enzyme was subjected to a detailed kinetic investigation at 95 degreesC to compare its catalytic mechanism to that determined at 37 degreesC for the beta-glucosidase (abg) from the mesophilic bacterium, Agrobacterium faecalis [Kempton, J., and Withers, S. G. (1992) Biochemistry 31, 9961]. These enzymes have amino acid sequences that are 33% identical and have been classified as family 1 glycosyl hydrolases on the basis of amino acid sequence similarities. Both enzymes have similar broad specificities for both sugar and aglycone moieties and exhibit nearly identical pH dependences for their kinetic parameters with several different substrates. Bronsted plots were constructed for bgl at several temperatures using a series of aryl glucoside substrates. These plots were concave downward at all temperatures, indicating that bgl utilized a two-step mechanism similar to that of abg and that the rate-limiting step in this mechanism did not change with temperature for any given aryl glucoside. The Bronsted coefficient for bgl at 95 degreesC (beta1g = -0.7) was identical to that for abg at 37 degreesC and implies that these enzymes utilize nearly identical transition states, at least in regard to charge accumulation on the departing glycosidic oxygen. In addition, a high correlation coefficient (rho = 0.97) for the linear free energy relationship between these two enzymes and similar inhibition constants for these two enzymes with several ground state and transition state analogue inhibitors further indicate that these enzymes stabilize similar transition states. The mechanistic similarities between these two enzymes are noteworthy in light of the large difference in their temperature optima. This suggests that, in the presumed evolution that occurred between the hyperthermophilic archaeal enzyme and the mesophilic bacterial enzyme, structural modifications must have been selected which maintained the integrity of the active site structure and, therefore, the specificity of transition state interactions, while adapting the overall protein structure to permit function at the appropriate temperature.}, number={49}, journal={BIOCHEMISTRY}, author={Bauer, MW and Kelly, RM}, year={1998}, month={Dec}, pages={17170–17178} }
 @article{halio_bauer_mukund_adams_kelly_1997, title={Purification and characterization of two functional forms of intracellular protease PFPI from the hyperthermophilic Archaeon Pyrococcus furiosus}, volume={63}, number={1}, journal={Applied and Environmental Microbiology}, author={Halio, S. B. and Bauer, M. W. and Mukund, S. and Adams, M. W. W. and Kelly, R. M.}, year={1997}, pages={289–295} }