Search Results - "Huber, Reuben E"

LacZ β‐galactosidase: Structure and function of an enzyme of historical and molecular biological importance by Juers, Douglas H., Matthews, Brian W., Huber, Reuben E.

“…This review provides an overview of the structure, function, and catalytic mechanism of lacZ β‐galactosidase. The protein played a central role in Jacob and…”
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Gata3 participates in a complex transcriptional feedback network to regulate sympathoadrenal differentiation by Moriguchi, Takashi, Takako, Nakano, Hamada, Michito, Maeda, Atsuko, Fujioka, Yuki, Kuroha, Takashi, Huber, Reuben E, Hasegawa, Susan L, Rao, Arvind, Yamamoto, Masayuki, Takahashi, Satoru, Lim, Kim-Chew, Engel, James Douglas

“…Gata3 mutant mice expire of noradrenergic deficiency by embryonic day (E) 11 and can be rescued pharmacologically or, as shown here, by restoring Gata3…”
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Elucidating factors important for monovalent cation selectivity in enzymes: E. coli β-galactosidase as a model by Wheatley, Robert W, Juers, Douglas H, Lev, Bogdan B, Huber, Reuben E, Noskov, Sergei Yu

“…Many enzymes require a specific monovalent cation (M(+)), that is either Na(+) or K(+), for optimal activity. While high selectivity M(+) sites in transport…”
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Structural Explanation for Allolactose (lac Operon Inducer) Synthesis by lacZ β-Galactosidase and the Evolutionary Relationship between Allolactose Synthesis and the lac Repressor by Wheatley, Robert W., Lo, Summie, Jancewicz, Larisa J., Dugdale, Megan L., Huber, Reuben E.

“…β-Galactosidase (lacZ) has bifunctional activity. It hydrolyzes lactose to galactose and glucose and catalyzes the intramolecular isomerization of lactose to…”
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An allolactose trapped at the lacZ β-galactosidase active site with its galactosyl moiety in a (4)H3 conformation provides insights into the formation, conformation, and stabilization of the transition state by Wheatley, Robert W, Huber, Reuben E

“…When lactose was incubated with G794A-β-galactosidase (a variant with a "closed" active site loop that binds transition state analogs well) an allolactose was…”
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β-Galactosidase (Escherichia coli) has a second catalytically important Mg2+ site by Sutendra, Gopinath, Wong, Sean, Fraser, Marie E., Huber, Reuben E.

“…It is shown here that Escherichia coli β-galactosidase has a second Mg2+ binding site that is important for activity. Binding of Mg2+ to the second site caused…”
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Ser-796 of β-galactosidase ( Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop by Jancewicz, Larisa J., Wheatley, Robert W., Sutendra, Gopinath, Lee, Michael, Fraser, Marie E., Huber, Reuben E.

“…[Display omitted] ► β-Galactosidase active site loop (residues 794–803) opens/closes during reaction. ► If loop is ‘open’ enzyme substrate complex stabilized…”
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Direct and indirect roles of His‐418 in metal binding and in the activity of β‐galactosidase (E. coli) by Juers, Douglas H., Rob, Beatrice, Dugdale, Megan L., Rahimzadeh, Nastaron, Giang, Clarence, Lee, Michelle, Matthews, Brian W., Huber, Reuben E.

“…The active site of ß‐galactosidase (E. coli) contains a Mg2+ ion ligated by Glu‐416, His‐418 and Glu‐461 plus three water molecules. A Na+ ion binds nearby. To…”
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Transglucosidic reactions of the Aspergillus niger Family 3 β-glucosidase: Qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH by Seidle, Heather F., Huber, Reuben E.

“…The hydrolytic and transglucosidic reactions of the Aspergillus niger Family 3 β-glucosidase were characterized. Michaelis–Menten plots of the rates of…”
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Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase (Escherichia coli) by Dugdale, Megan L, Dymianiw, Dayna L, Minhas, Bhawanjot K, D'Angelo, Igor, Huber, Reuben E

“…The Met-542 residue of β-galactosidase is important for the enzyme's activity because it acts as a guide for the movement of the benzyl side chain of Phe-601…”
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Substitution for Asn460 Cripples β-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability by Wheatley, Robert W., Kappelhoff, John C., Hahn, Jennifer N., Dugdale, Megan L., Dutkoski, Mark J., Tamman, Stephanie D., Fraser, Marie E., Huber, Reuben E.

“…► The activity of β-galactosidase decreases substantially upon substituting for Asn460. ► Binding of O3 hydroxyl of galactose of the substrate via water is…”
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Trp-49 of the family 3 β-glucosidase from Aspergillus niger is important for its transglucosidic activity: Creation of novel β-glucosidases with low transglucosidic efficiencies by Seidle, Heather F., Allison, Sandra J., George, Erica, Huber, Reuben E.

“…Family 3 β-glucosidases from Aspergillus niger with substitutions for Trp-49 result in the accumulation of very small amounts of transglucosidic adducts,…”
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Importance of Arg-599 of β-galactosidase (Escherichia coli) as an anchor for the open conformations of Phe-601 and the active-site loop by Dugdale, Megan L, Vance, Michael L, Wheatley, Robert W, Driedger, Michael R, Nibber, Anjan, Tran, Angela, Huber, Reuben E

“…Structural and kinetic data show that Arg-599 of β-galactosidase plays an important role in anchoring the "open" conformations of both Phe-601 and an…”
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Studies of Glu-416 variants of beta-galactosidase (E. coli) show that the active site Mg(2+) is not important for structure and indicate that the main role of Mg (2+) is to mediate optimization of active site chemistry by Lo, Summie, Dugdale, Megan L, Jeerh, Nisha, Ku, Tabitha, Roth, Nathan J, Huber, Reuben E

“…Variants of beta-galactosidase with Valine and with Glutamine replacing Glutamate-416 did not have a Mg(2+) bound at the active site even at high Mg(2+)…”
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Trp-262 is a key residue for the hydrolytic and transglucosidic reactivity of the Aspergillus niger family 3 β-glucosidase: Substitution results in enzymes with mainly transglucosidic activity by Seidle, Heather F., McKenzie, Kyle, Marten, Ira, Shoseyov, Oded, Huber, Reuben E.

“…Trp-262 of the Aspergillus niger family 3 β-glucosidase is shown in this report to be a key residue for determining the ratio of this enzyme’s hydrolytic and…”
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Structural Basis for the Altered Activity of Gly794 Variants of Escherichia coli β-Galactosidase by Juers, Douglas H, Hakda, Shamina, Matthews, Brian W, Huber, Reuben E

“…The open−closed conformational switch in the active site of Escherichia coli β-galactosidase was studied by X-ray crystallography and enzyme kinetics…”
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Physical and kinetic properties of the family 3 beta-glucosidase from Aspergillus niger which is important for cellulose breakdown by Seidle, Heather F, Marten, Ira, Shoseyov, Oded, Huber, Reuben E

“…A beta-glucosidase (BGS) purified from Aspergillus niger cellulase powder (obtained from Sigma, St. Louis, MO, USA) was characterized. Electrophoresis, size…”
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Trp-999 of β-Galactosidase (Escherichia coli) Is a Key Residue for Binding, Catalysis, and Synthesis of Allolactose, the Natural Lac Operon Inducer by Huber, Reuben E, Hakda, Shamina, Cheng, Calvino, Cupples, Claire G, Edwards, Robert A

“…Trp-999 is a key residue for the action of β-galactosidases (Escherichia coli). Several site specific substitutions (Phe, Gly, Tyr, Leu) for Trp-999 were made…”
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Practical Considerations When Using Temperature to Obtain Rate Constants and Activation Thermodynamics of Enzymes with Two Catalytic Steps: Native and N460T-β-Galactosidase (E. coli) as Examples by Kappelhoff, John C., Liu, Su Yi Judy, Dugdale, Megan L., Dymianiw, Dayna L., Linton, Larry R., Huber, Reuben E.

“…The values of the rate constants and the associated enthalpies and entropies of enzymes with two catalytic steps can be measured by determining the effects of…”
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Thermal denaturation of .beta.-galactosidase and of two site specific mutants by Edwards, Robert A, Jacobson, Ada L, Huber, Reuben E

“…The thermal denaturation of wild-type beta-galactosidase and two beta-galactosidases with substitutions at the active site was studied by kinetics,…”
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