# How does competitive inhibition affect Lineweaver-Burk plot?

## How does competitive inhibition affect Lineweaver-Burk plot?

Competitive inhibition: the added molecule competes with the enzyme’s normal substrate for access to the enzyme’s binding site. By physically occupying the active binding site, the molecule blocks the enzyme’s normal interaction with its substrate, thereby slowing the overall reaction velocity.

### How do you determine the type of inhibition from a Lineweaver-Burk plot?

As shown in Figure 13.14, when we display kinetic data using as a Lineweaver-Burk plot it is easy to determine which mechanism is in effect. For example, an increase in slope, a decrease in the x-intercept, and no change in the y-intercept indicates competitive inhibition.

#### What does a Lineweaver-Burk plot show?

The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, before the wide availability of powerful computers and non-linear regression software. The y-intercept of such a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents −1/Km.

**What is slope of Lineweaver-Burk plot?**

A Double-Reciprocal or Lineweaver-Burk Plot. A double-reciprocal plot of enzyme kinetics is generated by plotting 1/V0 as a function 1/[S]. The slope is the KM/Vmax, the intercept on the vertical axis is 1/Vmax, and the intercept on the horizontal axis (more…)

**Why is Lineweaver-Burk plot more accurate?**

For instance; Lineweaver-Burke plot, the most favoured plot by researchers, has two distinct advantages over the Michaelis-Menten plot, in that it gives a more accurate estimate of Vmax and more accurate information about inhibition. It increases the precision by linearizing the data.

## Why is Lineweaver Burk plot more accurate?

### Why is Michaelis-Menten better than Lineweaver-Burk plot?

#### What is the disadvantage of Lineweaver-Burk plot?

Figure 6-5a shows a Lineweaver—Burk plot. The disadvantage of this plot is that it depends on less precisely determined points obtained at low values of [S], whereas the more accurate points obtained at high values of [S] cluster and so are less valuable in establishing the linear plot.

**When to use Lineweaver-Burk plot for competitive inhibition?**

Competitive inhibition can be recognized by using a Lineweaver–Burk plot if V0 is measured at different substrate concentrations in the presence of a fixed concentration of inhibitor.

**How is the Lineweaver Burk plot used in enzyme kinetics?**

The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, before the wide availability of powerful computers and non-linear regression software. The y -intercept of such a graph is equivalent to the inverse of Vmax; the x -intercept of the graph represents −1/ Km.

## Who is the author of the Lineweaver-Burk plot?

The 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. This plot is a derivation of the Michaelis–Menten equation and is represented as:

### What is the y-intercept of the Lineweaver-Burk plot?

The y-intercept of the Lineweaver- Burk plot is the reciprocal of maximum velocity. K M: Michaelis-Menten constant or enzyme affinity. The lower the K M the higher the affinity. Graphically the x-intercept of the line is -1/K M. K cat: turnover number, or reactions per unit time. The lower the K cat the slower the reaction. K cat =V max / [Enzyme].