"
Team:SCUT-China/Modeling/Simulation
From 2014.igem.org
(Difference between revisions)
Yanzw scut (Talk | contribs) |
Yanzw scut (Talk | contribs) |
||
| Line 7: | Line 7: | ||
.head{margin:-100px auto;font-family:Arial, Helvetica, sans-serif;font-size:50px;font-weight:bold;text-align:center;} | .head{margin:-100px auto;font-family:Arial, Helvetica, sans-serif;font-size:50px;font-weight:bold;text-align:center;} | ||
| - | #container{margin: | + | #container{margin:140px 20px;} |
.title{font-family:'Traditional Arabic', Helvetica, sans-serif;font-size:28px;font-weight:bold;color:#C6F;} | .title{font-family:'Traditional Arabic', Helvetica, sans-serif;font-size:28px;font-weight:bold;color:#C6F;} | ||
| Line 55: | Line 55: | ||
<p class="title">Reactions and Mechanism</p> | <p class="title">Reactions and Mechanism</p> | ||
| - | <p class="bold">1.Mechanism</p | + | <p class="bold">1.Mechanism</p> |
<p> | <p> | ||
The model for enzyme action, first suggested by Brown and Henri but later established more thoroughly Michaelis and Menten, suggests the binding of free enzyme to the substrate forming a enzyme-substrate(ES) complex. This complex undergoes a transformation, releasing product and free enzyme. The free enzyme is then available for another round of binding to new substrate.<br/><br/> | The model for enzyme action, first suggested by Brown and Henri but later established more thoroughly Michaelis and Menten, suggests the binding of free enzyme to the substrate forming a enzyme-substrate(ES) complex. This complex undergoes a transformation, releasing product and free enzyme. The free enzyme is then available for another round of binding to new substrate.<br/><br/> | ||
Revision as of 18:03, 17 October 2014
Simulation
Reactions and Mechanism
1.Mechanism
The model for enzyme action, first suggested by Brown and Henri but later established more thoroughly Michaelis and Menten, suggests the binding of free enzyme to the substrate forming a enzyme-substrate(ES) complex. This complex undergoes a transformation, releasing product and free enzyme. The free enzyme is then available for another round of binding to new substrate.
In the single substrate enzyme catalyzed reactions, the mechanism is often written as:
