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V and K are constants that are > 0, explain why the units of K and V are μm and μm/s respectively?

V and K are constants that are > 0, explain why the units of K and V are μm and μm/s respectively?

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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V and K are constants that are > 0, explain why the units of K and V are μm and μm/s respectively?

 

Enzymes are catalysts that facilitate the biochemical reactions that occur within all living organ- isms. One of the fundamental laws of enzyme kinetics was proposed by Leonor Michaelis and Maud Menten in 1913. The law has been supported by laboratory experiments and explained through mathematical modeling. Today Michaelis-Menten kinetics are used in many biological models. An enzyme molecule is designed to "fit" another molecule called a substrate. The substrate (S) and enzyme (E) form an intermediate complex (ES), which then dissociates to form the final end- product of the reaction (P) and the original enzyme (which can be re-used; see figure). An important question concerns the rate at which product molecules are formed. Under certain assumptions, Michelis-Menten kinetics relates the rate of production of P to the amount of S present. S ES Enzyme-substrate complex Enzyme + substrate Enzyme + product 1. We let R be the rate of production of the final product P and we let s be the concentration of the substrate S initially present. Concentrations are measured in units such as micro-moles (uM), while R is measured in uM/s. (Time is usually measured in seconds.) The Michaelis- Menten law says that Vs R(s) K+ s
Transcribed Image Text:Enzymes are catalysts that facilitate the biochemical reactions that occur within all living organ- isms. One of the fundamental laws of enzyme kinetics was proposed by Leonor Michaelis and Maud Menten in 1913. The law has been supported by laboratory experiments and explained through mathematical modeling. Today Michaelis-Menten kinetics are used in many biological models. An enzyme molecule is designed to "fit" another molecule called a substrate. The substrate (S) and enzyme (E) form an intermediate complex (ES), which then dissociates to form the final end- product of the reaction (P) and the original enzyme (which can be re-used; see figure). An important question concerns the rate at which product molecules are formed. Under certain assumptions, Michelis-Menten kinetics relates the rate of production of P to the amount of S present. S ES Enzyme-substrate complex Enzyme + substrate Enzyme + product 1. We let R be the rate of production of the final product P and we let s be the concentration of the substrate S initially present. Concentrations are measured in units such as micro-moles (uM), while R is measured in uM/s. (Time is usually measured in seconds.) The Michaelis- Menten law says that Vs R(s) K+ s
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