Jul 24, 2009 · Km and Vmax are related to enzyme kinetics in a biological system. Km is the substrate concentration that is required for the reaction to occur at 1/2 Vmax. In other words, it …

Jun 15, 2008 · If Vmax is dependent on enzyme concentration and Km is the substrate concentration = 1/2Vmax. If you increase the enzyme concentration, Vmax increases, then Km …

Aug 27, 2018 · Hi everyone, I was having trouble understanding the Kaplan explanation for why Vmax is unchanged in competitive inhibition, but it decreases with non-competitive inhibition. I …

Jan 4, 2012 · Although, generally, noncompetitive inhibition does change Vmax, allosteric regulation is a special circumstance. An allosteric enzyme inhibitor is a case of noncompetitive …

Dec 2, 2014 · Vmax is a maximum reaction velocity and happens when all of the enzyme's active sites are saturated with substrate. Therefore, adding more enzyme will proportionally change …

May 7, 2009 · Since km is used as a measure of an enzyme's affinity for a given substrate, it must either be independent of enzyme concentration, or have a set (standard) concentration value. …

Jul 19, 2016 · Km represents two things, the ease at which the enzyme grabs substrates and the concentration at which the reaction is at Vmax/2. Vmax stays the same when you add a …

Oct 9, 2012 · Km is the concentration of substrate at 1/2 Vmax and is an intrinsic property of the enzyme. Therefore with irreversible binding you decrease the Vmax because there are less …

Feb 26, 2007 · So I just need some confirmation. In competitive inhibition, Vmax does not change but Km does. Km most likely shifts to the right? which means a decrease in substrate affinity? …

Oct 5, 2011 · In noncompetitive inhibition, Km is unchanged but Vmax decreases. This means Km / Vmax increases (because the denominator is getting smaller), so the slope increases. …