# What are the units of k1 and K 1?

## What are the units of k1 and K 1?

Note that k1 and k-1 have different units, 1/(Ms) and 1/s respectively. The turnover rate v is defined as the increase (or decrease) in product over time, which is directly proportional to the concentration of enzyme-substrate complex [ES].

### What is k1 and k2 in enzyme kinetics?

and rewriting KM as KS + k2/k1 which is the sum of a dissociative and a kinetic element. The higher KS, the higher KM, and the lower the affinity for substrate. KM is also part of the second order enzyme specificity constant, k2/KM . k2/KM defines the probability of free E interacting with free S.

#### What are the units of k1?

The forward rate constant (k1) has units of M-1sec-1. The reverse rate constant (k-1) has units of sec-1.

How is k2 the turnover number of an enzyme calculated?

Question: To obtain k2, the turnover number of an enzyme, one must Question 1 options: divide Vmax by kcat. divide v by Vmax. divide Vmax by 2. divide Vmax by the total enzyme concentration.

How does the Michaelis-Menten equation relate to enzyme reactions?

The Michaelis–Menten equation describes how this slope varies with the concentration of substrate. Enzyme assays are laboratory procedures that measure the rate of enzyme reactions.

## When was the equation of enzyme kinetics described?

Rearranging Equation 3.2.10, Tthe Lineweaver–Burk plot (or double reciprocal plot) is a graphical representation of the Lineweaver–Burk equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934 (Figure 3.2.2 ).

### How to estimate enzyme rate constants using Enz?

A Lambda approximation method (described in the Lambda approximation method for enzyme rate constants section) and the measured Km values for each substrate can be used to estimate these rate constants. Enz […] denotes the kMech-defined function that provides additional capabilities to Cellerator.

#### When do we know how much enzyme is added to a reaction?

This equation is a simple relationship that says we know how much enzyme we added to our reaction mixture at time zero, so at any time, we know that the amount of free enzyme plus the amount of enzyme bound in the enzyme-substrate complex should equal the initial amount added.