Search Results - "Cristobal, Judith R."

Glycerol 3‑Phosphate Dehydrogenase Catalyzed Hydride Transfer: Enzyme Activation by Cofactor Pieces by Hegazy, Rania, Cristobal, Judith R., Richard, John P.

“…Glycerol 3-phosphate dehydrogenase catalyzes reversible hydride transfer from glycerol 3-phosphate (G3P) to NAD+ to form dihydroxyacetone phosphate; from the…”
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Glycerol 3‑Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction by Cristobal, Judith R., Hegazy, Rania, Richard, John P.

“…Kinetic parameters are reported for glycerol 3-phosphate dehydrogenase (GPDH)-catalyzed hydride transfer from the whole substrate glycerol 3-phosphate (G3P) or…”
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Glycerol-3-Phosphate Dehydrogenase: The K120 and K204 Side Chains Define an Oxyanion Hole at the Enzyme Active Site by Cristobal, Judith R., Richard, John P.

“…The cationic K120 and K204 side chains lie close to the C-2 carbonyl group of substrate dihydroxyacetone phosphate (DHAP) at the active site of…”
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Kinetics and mechanism for enzyme-catalyzed reactions of substrate pieces by Cristobal, Judith R, Richard, John P

“…The most important difference between enzyme and small molecule catalysts is that only enzymes utilize the large intrinsic binding energies of nonreacting…”
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Utilization of Cofactor Binding Energy for Enzyme Catalysis: Formate Dehydrogenase-Catalyzed Reactions of the Whole NAD Cofactor and Cofactor Pieces by Cristobal, Judith R., Nagorski, Richard W., Richard, John P.

“…The pressure to optimize enzymatic rate accelerations has driven the evolution of the induced-fit mechanism for enzyme catalysts where the binding interactions…”
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Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable Probe by Richard, John P., Cristobal, Judith R., Amyes, Tina L.

“…Conspectus Linear free energy relationships (LFERs) for substituent effects on reactions that proceed through similar transition states provide insight into…”
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Hydride Transfer Catalyzed by Glycerol Phosphate Dehydrogenase: Recruitment of an Acidic Amino Acid Side Chain to Rescue a Damaged Enzyme by He, Rui, Cristobal, Judith R, Gong, Naiji Jabin, Richard, John P

“…K120 of glycerol 3-phosphate dehydrogenase (GPDH) lies close to the carbonyl group of the bound dihydroxyacetone phosphate (DHAP) dianion. pH rate (pH 4.6–9.0)…”
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The Organization of Active Site Side Chains of Glycerol-3-phosphate Dehydrogenase Promotes Efficient Enzyme Catalysis and Rescue of Variant Enzymes by Cristobal, Judith R, Reyes, Archie C, Richard, John P

“…A comparison of the values of k cat/K m for reduction of dihydroxyacetone phosphate (DHAP) by NADH catalyzed by wild type and K120A/R269A variant…”
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Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic Reactions by Fernandez, Patrick L, Nagorski, Richard W, Cristobal, Judith R, Amyes, Tina L, Richard, John P

“…The activation barriers ΔG ⧧ for k cat/K m for the reactions of whole substrates catalyzed by 6-phosphogluconate dehydrogenase, glucose 6-phosphate…”
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Neurotoxic Effects of Mixtures of Perfluoroalkyl Substances (PFAS) at Environmental and Human Blood Concentrations by Ríos-Bonilla, Karla M., Aga, Diana S., Lee, Jungeun, König, Maria, Qin, Weiping, Cristobal, Judith R., Atilla-Gokcumen, Gunes Ekin, Escher, Beate I.

“…Per- and polyfluoroalkyl substances (PFAS) may cause various deleterious health effects. Epidemiological studies have demonstrated associations between PFAS…”
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Protein–Ribofuranosyl Interactions Activate Orotidine 5′‑Monophosphate Decarboxylase for Catalysis by Cristobal, Judith R, Brandão, Tiago A. S, Reyes, Archie C, Richard, John P

“…The role of a global, substrate-driven, enzyme conformational change in enabling the extraordinarily large rate acceleration for orotidine 5′-monophosphate…”
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Modeling the Role of a Flexible Loop and Active Site Side Chains in Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase by Mhashal, Anil R, Romero-Rivera, Adrian, Mydy, Lisa S, Cristobal, Judith R, Gulick, Andrew M, Richard, John P, Kamerlin, Shina C. L

“…Glycerol-3-phosphate dehydrogenase is a biomedically important enzyme that plays a crucial role in lipid biosynthesis. It is activated by a ligand-gated…”
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Human Glycerol 3‑Phosphate Dehydrogenase: X‑ray Crystal Structures That Guide the Interpretation of Mutagenesis Studies by Mydy, Lisa S, Cristobal, Judith R, Katigbak, Roberto D, Bauer, Paul, Reyes, Archie C, Kamerlin, Shina Caroline Lynn, Richard, John P, Gulick, Andrew M

“…Human liver glycerol 3-phosphate dehydrogenase (hlGPDH) catalyzes the reduction of dihydroxyacetone phosphate (DHAP) to form glycerol 3-phosphate, using the…”
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The Mechanism of Action of Glycerol-3-Phosphate Dehydrogenase and Orotidine 5'-Monophosphate Decarboxylase: Insights from Studies of Enzyme Variants by Cristobal, Judith R

“…The role of a global, substrate-driven enzyme conformational change, in enabling the large rate acceleration for orotidine 5'-monophosphate decarboxylase…”
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