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Allosteric properties of rabbit triosephosphate isomerase
Life Sciences, 1971Abstract Rabbit triosephosphate isomerase, except for the occurence of substrate inhibition, obeys the simple Michaelis-Menton equation with glyceraldehyde-3-phosphate as substrate. But with dihydroxycetone phosphate as substrate, it exhibits sigmoidal kinetics. Its isomerase activity can be inhibited by various phosphates and metabolites.
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Triosephosphate isomerase: a highly evolved biocatalyst
Cellular and Molecular Life Sciences, 2010Triosephosphate isomerase (TIM) is a perfectly evolved enzyme which very fast interconverts dihydroxyacetone phosphate and D: -glyceraldehyde-3-phosphate. Its catalytic site is at the dimer interface, but the four catalytic residues, Asn11, Lys13, His95 and Glu167, are from the same subunit. Glu167 is the catalytic base. An important feature of the TIM
Rik K. Wierenga +2 more
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Triosephosphate Isomerase Deficiency: A Patient With Val231Met Mutation
Pediatric Neurology, 2011Triosephosphate isomerase deficiency constitutes a rare autosomal recessive disorder, characterized by hemolytic anemia, neurodegeneration, and recurrent bacterial infections. It is the most severe glycolytic enzyme defect associated with progressive neurologic dysfunction.
Aydinok Y. +4 more
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Biochemistry, 2011
Protein-protein interactions are crucial for many biological functions. The redox interactome encompasses numerous weak transient interactions in which thioredoxin plays a central role. Proteomic studies have shown that thioredoxin binds to numerous proteins belonging to various cellular processes, including energy metabolism.
Hameed, Shahul MS, Sarma, Siddhartha P
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Protein-protein interactions are crucial for many biological functions. The redox interactome encompasses numerous weak transient interactions in which thioredoxin plays a central role. Proteomic studies have shown that thioredoxin binds to numerous proteins belonging to various cellular processes, including energy metabolism.
Hameed, Shahul MS, Sarma, Siddhartha P
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The Mechanistic Pathway of a Mutant Triosephosphate Isomerasea
Annals of the New York Academy of Sciences, 1986The glycolytic enzyme triosephosphate isomerase catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraJdehyde 3-phosphate, following the pathway iHustrated in SCHEME 1.1,2 From a variety of kinetic,3 stereochemical,4 and chemical modification studies,s.6 it is known that an enzymic base abstracts the I-pro-R proton of ...
Jeremy R. Knowles, Ronald T. Raines
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Triosephosphate isomerase as a therapeutic target against trichomoniasis.
Molecular and biochemical parasitology (Print), 2021C. Benítez-Cardoza +4 more
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Computational Modeling of the Catalytic Reaction in Triosephosphate Isomerase
Journal of Molecular Biology, 2004We present a comprehensive analysis of the catalytic cycle of the enzyme triosephosphate isomerase (TIM), including both the reactive chemistry and the catalytic loop and side-chain motions. Combining accurate mixed quantum mechanics/molecular mechanics (QM/MM) and protein structure prediction methods, we have modeled both the structural and chemical ...
Victor Guallar +3 more
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Dimerization Affects Collective Dynamics of Triosephosphate Isomerase
Biochemistry, 2008Molecular dynamics simulations (30-60 ns runs) are performed on free/apo triosephosphate isomerase (TIM) to determine any correlation between collective motions and loop 6 dynamics. Native TIM is reported to be active only as a homodimer even though cooperativity has not been observed between the two identical subunits.
Pemra Doruker, Sertan Cansu
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Triosephosphate Isomerase: A Theoretical Comparison of Alternative Pathways
Journal of the American Chemical Society, 2001Three mechanisms proposed for the triosephosphate isomerase (TIM) catalyzed reactions were studied with the QM/MM approach using B3LYP/6-31+G(d,p) as the QM method. The two pathways that involve an enediol species were found to give similar values for the barriers and the calculated rates are in satisfactory agreement with experiment.
Qiang Cui, Martin Karplus
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Triosephosphate isomerase deficiency: 2 new cases
Scandinavian Journal of Haematology, 19852 new cases of triosephosphate isomerase (TPI) deficiency associated with severe haemolytic anaemia in 2 unrelated Italian families are described. Only 1 case was extensively investigated. TPI deficiency was detectable in erythrocytes, leucocytes, platelets and plasma. The mutant enzyme showed normal Km for GAP and increased Km for DHAP, with an higher
C Borgna-Pignatti +6 more
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