Thermodynamics of the hydrolysis reactions of α-d-galactose 1-phosphate, sn-glycerol 3-phosphate, 4-nitrophenyl phosphate, phosphocreatine, and 3-phospho-d-glycerate

Goldberg, Robert N.; Lang, Brian E.; Lo, Catherine T.; Ross, David; Tewari, Yadu D.

doi:10.1016/j.jct.2008.12.017

The Journal of Chemical Thermodynamics

2009

DOI: 10.1016/j.jct.2008.12.017

|View full text |Cite

Thermodynamics of the hydrolysis reactions of α-d-galactose 1-phosphate, sn-glycerol 3-phosphate, 4-nitrophenyl phosphate, phosphocreatine, and 3-phospho-d-glycerate

Robert N. Goldberg

Brian E. Lang

Catherine T. Lo

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2014

2020

Publication Types

Select...

Article3

Relationship

Self Cite0

Independent3

Authors

Journals

Cited by 3 publications

(2 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The value for the endothermic heat generated by the dilution was obtained by injecting 10 µL of p-NPP (20 mM) into the reaction cell containing only buffer: ΔH = 3089 ± 52 µcal/µmol (i.e. 12.9 ± 0.22 kJ/mol), in good agreement with the corresponding ΔH value determined by enzymatic assays (13.2 ± 0.18 kJ/mol) [1]. In this study, we focused on measuring initial catalytic rates in order to minimize the effect of the reaction product and competitive inhibitor phosphate [2][3][4][5][6].Different concentrations of p-NPP were prepared and 8 µL of 0.24 µM rkbPAP were injected into the substrate solutions.…”

supporting

confidence: 70%

Structural elements that modulate the substrate specificity of plant purple acid phosphatases: Avenues for improved phosphorus acquisition in crops

et al. 2020

View full text Add to dashboard Cite

Experimental details for the ITC assay. The enthalpy change (ΔH) associated with the reaction of rkbPAP with p-NPP was determined by injecting 10 µL of p-NPP (20 mM) into the reaction cell (200 µL) containing 0.95 µM of rkbPAP, and by allowing the reaction to proceed to completion.The reaction is exothermic as indicated by the negative value of the heat pulse (dQ/dT); the value of ΔH can be calculated by integrating the area under the curve in Fig. S2a (minus the endothermic heat associated with the dilution) divided by the amount of p-NPP hydrolyzed in the cell. The value for the endothermic heat generated by the dilution was obtained by injecting 10 µL of p-NPP (20 mM) into the reaction cell containing only buffer: ΔH = 3089 ± 52 µcal/µmol (i.e. 12.9 ± 0.22 kJ/mol), in good agreement with the corresponding ΔH value determined by enzymatic assays (13.2 ± 0.18 kJ/mol) [1]. In this study, we focused on measuring initial catalytic rates in order to minimize the effect of the reaction product and competitive inhibitor phosphate [2][3][4][5][6].Different concentrations of p-NPP were prepared and 8 µL of 0.24 µM rkbPAP were injected into the substrate solutions. Fig. S2b shows a typical calorimetric trace of a reaction. The initial rates determined in µcal/s, when divided by ΔH (µcal/µmol), are transformed into µmol/s, representing the amount of p-NPP hydrolyzed per second in the cell. These rates were subsequently plotted against the p-NPP concentration and fitted to the Michaelis-Menten equation (Eq. 1; Fig. S2c), resulting in a kcat value (i.e. Vmax/[PAP]) of ~190 s -1 and a Michaelis constant Km of ~4 mM.

show abstract

supporting

confidence: 70%

Structural elements that modulate the substrate specificity of plant purple acid phosphatases: Avenues for improved phosphorus acquisition in crops

et al. 2020

View full text Add to dashboard Cite

show abstract

“…If 1 μmol of both organic substrate and phosphate are dissolved in 1 L of water, the point where half of both have condensed to form the organophosphate requires vaporization of that 1 L to several μL of water. Temperatures are solved for using van't Hoff's equation with enthalpies from Goldberg et al31…”

mentioning

confidence: 99%

Thermodynamics of Prebiotic Phosphorylation

Pasek

2019

Chem. Rev.

View full text Add to dashboard Cite

The formation of organophosphate molecules by prebiotic processes relies on nonenzymatic synthesis. Given the centrality of phosphorylated biomolecules in metabolic, structural, and replicative processes, it is highly likely that such nonenzymatic synthesis had to occur early in Earth's history. This Review collects and uses thermodynamic data to constrain processes that may have produced organophosphates and evaluates both the plausibility of reactants and the likelihood that environments conducive to phosphorylation were present. The energy required to phosphorylate organics is ∼15 kJ/mol, requiring either very low water activities or reactive inorganic phosphorus compounds. Thermodynamics permits evaluating phosphorylation environments for both plausibility and novelty and shows that several routes would have been available to form these potentially key reagents. Building from phosphate monoesters to diesters may have enabled the synthesis of nucleic acids, perhaps opening a way into the RNA world. CONTENTS 1. Introduction 4690 2. Phosphate and the Importance of Being Ionized 4691 3. Phosphate in Phosphorylation 4691 4. Thermodynamics of Phosphate and Phosphorus Sources 4692 5. Mineralogy and Phosphorylation 4695 6. Phosphorylation by Phosphate 4695 6.1. Thermodynamics of Phosphate Mineral Dissolution 4695 6.2. Thermodynamics of Environments 4696 6.3. Phosphorylation in Anhydrous Solvents 4696 6.4. Condensing Agents 4697 7. Phosphorylation by Energetic P Compounds 4697 7.1. Phosphorylation by P 4 O 10 and Trimetaphosphate 4697 7.2. Phosphorylation by Amidophosphate 4698 7.3. Phosphorylation by Schreibersite 4699 7.4. Reduced P Compounds 4699 8. Thermodynamics of Phosphorylation 4700 9. Thermodynamics of Polymerization 4701 10. Applications of Thermodynamics to Prebiotic Chemistry 4702 Author Information 4703 Corresponding Author 4703 ORCID 4703 Notes 4703 Biography 4703 Acknowledgments 4703 References 4703

show abstract

Phosphate Monoester Hydrolysis by Trinuclear Alkaline Phosphatase; DFT Study of Transition States and Reaction Mechanism

Chen

Liao

2014

ChemPhysChem

View full text Add to dashboard Cite

Alkaline phosphatase (AP) is a trinuclear metalloenzyme that catalyzes the hydrolysis of a broad range of phosphate monoesters to form inorganic phosphate and alcohol (or phenol). In this paper, by using density functional theory with a model based on a crystal structure, the AP-catalyzed hydrolysis of phosphate monoesters is investigated by calculating two substrates, that is, methyl and p-nitrophenyl phosphates, which represent alkyl and aryl phosphates, respectively. The calculations confirm that the AP reaction employs a "ping-pong" mechanism involving two chemical displacement steps, that is, the displacement of the substrate leaving group by a Ser102 alkoxide and the hydrolysis of the phosphoseryl intermediate by a Zn2-bound hydroxide. Both displacement steps proceed via a concerted associative pathway no matter which substrate is used. Other mechanistic aspects are also studied. Comparison of our calculations with linear free energy relationships experiments shows good agreement.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Thermodynamics of the hydrolysis reactions of α-d-galactose 1-phosphate, sn-glycerol 3-phosphate, 4-nitrophenyl phosphate, phosphocreatine, and 3-phospho-d-glycerate

Cited by 3 publications

References 46 publications

Structural elements that modulate the substrate specificity of plant purple acid phosphatases: Avenues for improved phosphorus acquisition in crops

Structural elements that modulate the substrate specificity of plant purple acid phosphatases: Avenues for improved phosphorus acquisition in crops

Thermodynamics of Prebiotic Phosphorylation

Phosphate Monoester Hydrolysis by Trinuclear Alkaline Phosphatase; DFT Study of Transition States and Reaction Mechanism

Contact Info

Product

Resources

About