Jan 5, 2015 · Vmax=kcat * ([E total]) If the units for Vmax are M/s i.e. s-1 and you divide Vmax by the concentration of total enzyme which has units in M, the Ms will cancel out, leaving you with …

Mar 16, 2019 · This is a correct interpretation of kcat. You can think of kcat as the speed limit of the enzyme. This shows how fast the enzyme can act under optimal conditions (i.e. saturating …

Apr 19, 2021 · The resulting rate (kcat[E]tot) is only achieved when every molecule of enzyme essentially always is in the act of converting substrate to product. That is, every time a product …

Aug 19, 2009 · kcat/km = .008 s-1*M-1 I'm assuming that I just need to convert the 71.7 uM into M (.0000717M) and then divide to get the value 7670 s-1*M-1 However, and older, much …

May 15, 2015 · The enzyme catalysis reaction following MM kinetics can be depicted as: $$\Large\ce{E + S<=>[k_f][k_r]ES->[k_{cat}]E + P }$$

Apr 26, 2008 · What is the turnover number (Kcat) of carbonic anhydrase expressed in units of per min and per sec)? Mr of CO 2 is 44. So here are my calculations: Kcat = Vmax/[E]t, where …

Specific activity is defined as the number of 'Units' per mg of protein. One enzyme unit is defined as the amount of enzyme that catalyzes the formation of 1 μmol of product per min under …

May 7, 2021 · Calculating Vmax (or Kcat) given specific activity of an enzyme over length of time incubated with an activator 4 Is it possible to use Vmax as Kcat in a Michaelis-Menten reaction?

Apr 29, 2019 · From what I understand about the Michaelis Menten Model Km defines the amount of substrate required to reach half-saturation. 1/2 Vmax corresponds to Km on the x axis …

Mar 25, 2004 · "kcat/Km" of the two enzyme is indeed different... Let me describe a bit more detial... what I have done was comparing two modified enzymes, one of it (just call it enzyme …