Saturday, March 27, 2010

enzyme catalysts.

The way the molecule binds the enzyme catalysts to accelerate their reaction was not as simple as what you think, says chemist from England and Spain. Some enzymes do not need to tie in a way that will best stabilize the reaction transition state, but particularly in a way that minimizes the overall energy barrier for the reaction. Applying this idea to design a new molecular catalysts can help to improve their performance.

People - people often think the reaction with the enzyme catalytic transition state stabilization, said Jonathan Goodman of the University of Cambridge. Transition state can be thought of as the top "hill" that must be energetic climb to the reaction that followed - if the energy is lowered, then the reaction will move faster.

However, what Goodman - together - together with Luis Simón of the University of Salamanca - find when they dig up the protein databank (PDB) to find the way to acquire these enzymes, is that the hydrogen bonding groups at the enzyme active site is not structured to provide stabilization maximum in the transition state.

The addition reaction-type enzyme oxyanion hole in mengakatalisasi carbonyl group (C = O). Goodman explained that they expect to see the location of the active enzyme composed with hydrogen bonding donor at the carbonyl samaseperti extent, because it is known to provide good stabilization of the transition state.

Bond planar (left) of carbonyl compounds to stabilize the transition state is good, but plays its bonds (right) is very good unuk reduce the energy barrier. However, what they find by looking at the structure of the enzyme is that the hydrogen bond donors tend to play out of the field of carbonyl.

This pair found that the bond on the configuration of the molecule also lowered initial reactant - the foundation reaction - and with more than a lowered transition state. This means that the overall energy barrier - the size of the hill of the molecules that must pass - real big sanagt

The way the molecule binds the enzyme catalysts to accelerate their reaction was not as simple as what you think, says chemist from England and Spain. Some enzymes do not need to tie in a way that will best stabilize the reaction transition state, but particularly in a way that minimizes the overall energy barrier for the reaction. Applying this idea to design a new molecular catalysts can help to improve their performance.

People - people often think the reaction with the enzyme catalytic transition state stabilization, said Jonathan Goodman of the University of Cambridge. Transition state can be thought of as the top "hill" that must be energetic climb to the reaction that followed - if the energy is lowered, then the reaction will move faster.

However, what Goodman - together - together with Luis Simón of the University of Salamanca - find when they dig up the protein databank (PDB) to find the way to acquire these enzymes, is that the hydrogen bonding groups at the enzyme active site is not structured to provide stabilization maximum in the transition state.

The addition reaction-type enzyme oxyanion hole in mengakatalisasi carbonyl group (C = O). Goodman explained that they expect to see the location of the active enzyme composed with hydrogen bonding donor at the carbonyl samaseperti extent, because it is known to provide good stabilization of the transition state.

Bond planar (left) of carbonyl compounds to stabilize the transition state is good, but plays its bonds (right) is very good unuk reduce the energy barrier. However, what they find by looking at the structure of the enzyme is that the hydrogen bond donors tend to play out of the field of carbonyl.

This pair found that the bond on the configuration of the molecule also lowered initial reactant - the foundation reaction - and with more than a lowered transition state. This means that the overall energy barrier - the size of the hill of the molecules that must pass - real big sanagt

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