Haloacetol phosphates. Potential active-site reagents for aldolase, triose phosphate isomerase, and glycerophosphate dehydrogenase. I. Preparation and properties

Biochemistry ◽  
1970 ◽  
Vol 9 (8) ◽  
pp. 1776-1782 ◽  
Author(s):  
Fred C. Hartman
Keyword(s):  
Active Site ◽  
Triose Phosphate Isomerase ◽  
Triose Phosphate ◽  
Glycerophosphate Dehydrogenase

Uniquely Labelled Active Site Sequence in Chicken Muscle Triose Phosphate Isomerase

Nature ◽  
1970 ◽  
Vol 227 (5254) ◽  
pp. 180-181 ◽  
Author(s):  
A. F. W. COULSON ◽  
J. R. KNOWLES ◽  
J. D. PRIDDLE ◽  
R. E. OFFORD
Keyword(s):  
Active Site ◽  
Triose Phosphate Isomerase ◽  
Triose Phosphate ◽  
Chicken Muscle ◽  
Active Site Sequence

scholarly journals Dihydroxyacetone phosphate. Its structure and reactivity with α-glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase and some possible metabolic implications

1971 ◽  
Vol 122 (3) ◽  
pp. 285-297 ◽  
Author(s):  
S. J. Reynolds ◽  
D. W. Yates ◽  
C. I. Pogson
Keyword(s):  
Aqueous Solution ◽  
Rate Constants ◽  
Reactive Species ◽  
Triose Phosphate Isomerase ◽  
Dihydroxyacetone Phosphate ◽  
Temperature Dependent ◽  
Keto Form ◽  
Triose Phosphate ◽  
Glycerophosphate Dehydrogenase ◽  
Neutral Aqueous Solution

1. Dihydroxyacetone phosphate exists in neutral aqueous solution at 20°C as a mixture of keto, gem-diol and enolic forms in the ratio 55:44:1. 2. The three forms are freely interconvertible and rate constants for these reactions have been determined. 3. Keto-dihydroxyacetone phosphate is the primary reactive species in the reactions catalysed by α-glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase. 4. The proportion of keto form to gem-diol forms of dihydroxyacetone phosphate is temperature-dependent. At 37°C, 83% is keto-dihydroxyacetone phosphate. 5. The enzymological and metabolic consequences of these results are discussed.

scholarly journals Molecular dynamics simulations of the interactions between triose phosphate isomerase and sulfonamides

2020 ◽  
Vol 2 ◽  
pp. e13
Author(s):  
Neville Y. Forlemu ◽  
Joseph Sloop
Keyword(s):  
Active Site ◽  
Malaria Incidence ◽  
Antimalarial Drugs ◽  
Glycolytic Enzyme ◽  
Triose Phosphate Isomerase ◽  
Van Der Waals Interactions ◽  
Dimer Interface ◽  
Triose Phosphate ◽  
Solvation Energies ◽  
Active Site Region

Malaria is a disease with debilitating health and negative economic impacts in regions at high risk of infection. Parasitic resistance and side effects of current antimalarial drugs are major setbacks to the successful campaigns that have reduced malaria incidence by 40% in the last decade. The parasite’s dependence on glycolysis for energy requirements makes pathway enzymes suitable targets for drug development. Specifically, triose phosphate isomerase (TPI) from Plasmodium falciparum (pTPI) and human (hTPI) cells show striking structural features that can be used in development of new antimalarial agents. In this study MD simulations were used to characterize binding sites on hTPI and pTPI interactions with sulfonamides. The molecular mechanics Poisson–Boltzmann surface area (MM–PBSA) method was used to estimate the interaction energies of four sulfonamide-TPI docked complexes. A unique combination of key residues at the dimer interface of pTPI is responsible for the observed selective affinity to pTPI compared to hTPI. The representative sulfonamide; 4-amino-N-(3,5-dimethylphenyl)-3-fluorbenzenesulfonamide (sulfaE) shows a strong affinity with pTPI (dimer interface, −42.91 kJ/mol and active site region, −71.62 kJ/mol), hTPI (dimer interface, −41.32 kJ/mol and active site region, −84.40 kJ/mol). Strong and favorable Van der Waals interactions and increases in non-polar solvation energies explain the difference in affinity between pTPI with sulfaE compared to hTPI at the dimer interface. This is an indication that the dimer interface of TPI glycolytic enzyme is vital for development of sulfonamide based antimalarial drugs.

Reaction energetics of a mutant triose phosphate isomerase in which the active-site glutamate has been changed to aspartate

Biochemistry ◽  
1986 ◽  
Vol 25 (22) ◽  
pp. 7142-7154 ◽  
Author(s):  
Ronald T. Raines ◽  
Eliza L. Sutton ◽  
Donald R. Straus ◽  
Walter Gilbert ◽  
Jeremy R. Knowles
Keyword(s):  
Active Site ◽  
Triose Phosphate Isomerase ◽  
Triose Phosphate
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