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Help with enzyme kenetic

How to work out Km with competitive inhibition?
Vmax is 200 and inhibition concentration is 3

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username4648086

Check out page 2 on this pdf
http://www-plb.ucdavis.edu/courses/bis/105/lectures/EnzKinetics2.pdf

OP

Original post by lyer_in_hellfyre

Check out page 2 on this pdf
http://www-plb.ucdavis.edu/courses/bis/105/lectures/EnzKinetics2.pdf

Kmapp is Vmax？

username4648086

Original post by Xcyx336

Kmapp is Vmax？

I thought the question was asking abt Kmapp?

(edited 4 years ago)

OP

can you see the graph

OP

Original post by lyer_in_hellfyre

I thought the question was asking abt Kmapp?

image-321ad165-c4c5-4c00-a957-035249de366f957382980357619930-compressed.jpg.jpeg

username4648086

72F6E697-A401-47D6-80A4-373927742320.jpg.jpeg

This is the equation for the graph V0/ :undefined:

:undefined:

OP

This answer should be 100 because it's asking in absence of inhibition which is half of Vmax

username4648086

Also this...
0A6F249C-DC2B-4ED4-BC93-67213B1ACF52.jpg.jpeg

0A6F249C-DC2B-4ED4-BC93-67213B1ACF52.jpg.jpeg

OP

Original post by lyer_in_hellfyre

72F6E697-A401-47D6-80A4-373927742320.jpg.jpeg

This is the equation for the graph V0/ :undefined:

:undefined:

so Kmapp is equal to inhibition concentration add substrate concentration at Km

username4648086

Original post by Xcyx336

This answer should be 100 because it's asking in absence of inhibition which is half of Vmax

Is the Vmax without inhibitor 200 tho?

OP

Original post by lyer_in_hellfyre

Is the Vmax without inhibitor 200 tho?

yes

username4648086

Original post by Xcyx336

yes

Well then, half v max is 100 as you said...what did you get Km as?

OP

Original post by lyer_in_hellfyre

Well then, half v max is 100 as you said...what did you get Km as?

Km is half of Vmax so is 100

OP

Original post by lyer_in_hellfyre

Well then, half v max is 100 as you said...what did you get Km as?

the only thing is I don't know how to get km in present of inhibition

username4648086

Original post by Xcyx336

Km is half of Vmax so is 100

Km is the substrate concentration at half v max . Half v max is 100
which means Km is 10 μM

(edited 4 years ago)

OP

Original post by lyer_in_hellfyre

Km is the substrate concentration at half v max . Half v max is 100

so now see the graph is 10 for no inhibition and 30 for inhibition

OP

Original post by lyer_in_hellfyre

Km is the substrate concentration at half v max . Half v max is 100
which means Km is 10 μM

image-1bbc1c27-a0ba-4bee-8ce4-2887808919f71028505900112863108-compressed.jpg.jpeg

username4648086

Original post by Xcyx336

so now see the graph is 10 for no inhibition and 30 for inhibition

Edit :
Yep 10 μM is Km and 30μM is Km'

(edited 4 years ago)

OP

Original post by lyer_in_hellfyre

Yep 10 μM is Km and 30μM is Ki

According to the graph, Km with inhibition should be 30 right?

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