The Mechanism of the Triosephosphate Isomerase Reaction
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چکیده
منابع مشابه
The mechanism of the triosephosphate isomerase reaction.
The interconversion of dihydroxyacetone phosphate and glyceraldehyde 3-phosphate catalyzed by the enzyme triosephosphate isomerase was first demonstrated by Meyerhof and Kiessling (1). Since then studies with the enzyme have disclosed little about the mechanism of this reaction. Such an interconversion may be envisioned as occurring by formation of an enediol as, based on chemical analogy (2)) ...
متن کاملRevisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residue.
An analysis of 503 available triosephosphate isomerase sequences revealed nine fully conserved residues. Of these, four residues-K12, H95, E97 and E165-are capable of proton transfer and are all arrayed around the dihydroxyacetone phosphate substrate in the three-dimensional structure. Specific roles have been assigned to the residues K12, H95 and E165, but the nature of the involvement of E97 ...
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To explore the origin of the large-scale motion of triosephosphate isomerase's flexible loop (residues 166 to 176) at the active site, several simulation protocols are employed both for the free enzyme in vacuo and for the free enzyme with some solvent modeling: high-temperature Langevin dynamics simulations, sampling by a "dynamics driver" approach, and potential-energy surface calculations. O...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1959
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)98120-2