2017年5月1日 · $\begingroup$ I wouldn't say "can bind with more substrate" I would say "binds substrate more strongly" - the answers to your other two questions are yes - affinity is a function of the structure of the enzyme (as well as the shape/structure of the ligand), and yes a difference in affinities in two species indicates there is a difference in amino acids that affects the binding …

Since the Michaelis-Menton constant Km is the concentration of substrate at 0.5Vmax, it is an inverse measure of its substrate affinity, because a lower Km indicates that less substrate is needed to reach a certain reaction speed. Hence, a low …

2015年10月28日 · The purification step for his tags involves an affinity column of immobilized nickel, which binds to imidazole on histidine. After pushing the associated binding, wash and elution buffers through the column containing the sample, you should in theory have your purified protein product.

2016年6月27日 · Enzyme inhibitors (even competitive ones ones) don't change the intrinsic binding affinity of the free enzyme to substrate. Instead, they draw off some of the enzyme from the productive pathway. Because they change the concentration of particular enzyme species, they change the observed rate equation.

For which I think the only conditions are that the enzyme reaction follows. and the enzyme does not bind more than one substrate molecule (isn't allosterically binding) 'sigmoidal' kinetics; Where the enzyme is an allosteric enzyme and binding of more substrate to the enzyme increases the enzyme's affinity for the substrate.

2020年7月8日 · Could it be that, as the concentration of substrate goes up, the probability of a substrate interacting with an unbound enzyme goes down. In my scenario, the first substrate has a 1000/1000 chance to find a free enzyme, the second substrate has a 999/1000 chance of finding a free enzyme, etc.

$\begingroup$ @Chris, an allosteric regulator changes the conformation of the active site, but with saturation of substrate I know the enzyme suppose to work as there is no regulation at all - changes the affinity to substrate (Km) and not the ability of the enzyme to work (Vmax). in that perspective it's dynamics behave like a competitive inhibitor.

2018年11月29日 · Unless they have an extremely high affinity there will be an equilibrium between bound and unbound inhibitor, and the inhibitor can be competed out by substrate — i.e. the binding is reversible. You can read about this in more detail, but still at an introductory level, in the Wikipedia article on Enzyme Inhibitors or this section in the ...

2019年6月3日 · The correct answer is "The affinity of the enzyme for the substrate is greater than with one substrate bound." My confusion lies in the fact that the question never specified whether this cooperative enzyme had a positive or negative Hill coefficient. When approaching future questions like this, should I assume a positive Hill coefficient?

2016年11月29日 · The role of enzyme flexibility in catalysis is a highly disputed topic currently. The dynamics of proteins are an important concept for the understanding of the full reaction pathway, but there are some people who think that an important contribution of the protein is funneling vibrational energy into the appropriate bond motions for catalyssi.