Michaelis–Menten kinetics

<p>In <a href="/facts/Biochemistry/fa2pWEBp">biochemistry</a>, Michaelis–Menten kinetics, named after <a href="/facts/Leonor_Michaelis/aCxJnRoU">Leonor Michaelis</a> and <a href="/facts/Maud_Menten/zJkyCefF">Maud Menten</a>, is the simplest case of <a href="/facts/Enzyme_kinetics/LJ0lWoMc">enzyme kinetics</a>, applied to enzyme-catalysed reactions involving the transformation of one substrate into one product. It takes the form of a <a href="/facts/Differential_equation/9MGbE3Ca">differential equation</a> describing the <a href="/facts/Reaction_rate/Prwvxq0y">reaction rate</a> 
  
    
      
        v
      
    
    {\displaystyle v}
  
 (rate of formation of <a href="/facts/Product_(biology)/8uCoDUdv">product</a> P, with concentration 
  
    
      
        p
      
    
    {\displaystyle p}
  
) as a function of 
  
    
      
        a
      
    
    {\displaystyle a}
  
, the <a href="/facts/Concentration/wqBmz5od">concentration</a> of the <a href="/facts/Enzyme_substrate_(biology)/6MnaV19h">substrate</a>  A (using the symbols recommended by the <a href="/facts/IUBMB/6Tbm9SPF">IUBMB</a>). Its formula is given by the Michaelis–Menten equation:
</p>

v
        =
        
          
            
              
                d
              
              p
            
            
              
                d
              
              t
            
          
        
        =
        
          
            
              V
              a
            
            
              
                K
                
                  
                    m
                  
                
              
              +
              a
            
          
        
      
    
    {\displaystyle v={\frac {\mathrm {d} p}{\mathrm {d} t}}={\frac {Va}{K_{\mathrm {m} }+a}}}

<p>
  
    
      
        V
      
    
    {\displaystyle V}
  
, which is often written as 
  
    
      
        
          V
          
            max
          
        
      
    
    {\displaystyle V_{\max }}
  
, represents the limiting rate approached by the system at saturating substrate concentration for a given enzyme concentration. The Michaelis constant 
  
    
      
        
          K
          
            
              m
            
          
        
      
    
    {\displaystyle K_{\mathrm {m} }}
  
 has units of concentration, and for a given reaction is equal to the concentration of substrate at which the reaction rate is half of 
  
    
      
        V
      
    
    {\displaystyle V}
  
. Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions. Only a small proportion of enzyme-catalysed reactions have just one substrate, but the equation still often applies if only one substrate concentration is varied.
</p>

Michaelis–Menten kinetics open-in-new

Michaelis–Menten kinetics