ENZYMATIC TRANSITION STATES AND TRANSITION STATE ANALOG DESIGN
نویسندگان
چکیده
منابع مشابه
Enzymatic transition states and transition state analog design.
All chemical transformations pass through an unstable structure called the transition state, which is poised between the chemical structures of the substrates and products. The transition states for chemical reactions are proposed to have lifetimes near 10(-13) sec, the time for a single bond vibration. No physical or spectroscopic method is available to directly observe the structure of the tr...
متن کاملEnzymatic transition states and transition state analogues.
Transition states are the balance point of catalysis. Bonds are partially made and/or broken at the transition state, and the energy of the extended system provides near-equal probability that the system forms products or reverts to reactants. Enzymatic catalytic sites provide dynamic electronic environments that increase the probability that the transition state will be formed. Alignment of re...
متن کاملEnzymatic transition state theory and transition state analogue design.
The incredible catalytic rate enhancements caused by enzymes led Linus Pauling (1) to suggest that enzymes bind tightly to substrates distorted toward the transition state, thereby concentrating them and enforcing catalysis. Wolfenden (2) explained that chemically stable analogues that resemble the transition state would be expected to bind more tightly than substrate by factors resembling the ...
متن کاملEnzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes.
Experimental analysis of enzymatic transition-state structures uses kinetic isotope effects (KIEs) to report on bonding and geometry differences between reactants and the transition state. Computational correlation of experimental values with chemical models permits three-dimensional geometric and electrostatic assignment of transition states formed at enzymatic catalytic sites. The combination...
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The primary and secondary 18O isotope effects for the alkaline (KOH) and enzymatic (phosphotriesterase) hydrolysis of two phosphotriesters, O,O-diethyl p-nitrophenyl phosphate (I) and O,O-diethyl O-(4-carbamoylphenyl) phosphate (II), are consistent with an associative mechanism with significant changes in bond order to both the phosphoryl and phenolic leaving group oxygens in the transition sta...
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ژورنال
عنوان ژورنال: Annual Review of Biochemistry
سال: 1998
ISSN: 0066-4154,1545-4509
DOI: 10.1146/annurev.biochem.67.1.693