enzyme kenetics and inhibition

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  • Created by: anna888
  • Created on: 06-02-23 15:46
describe 1st order enzyme rate
rate dependent on [s]
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describe zero order enzyme rate
no relationship between v and [s]
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describe second order enzyme rate
v and [s] relationship not proportional, but depedant on multiple substrates
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what does v and vmax represent
v= the enzymatic rate. vmax= the rate of the reaction at which the enzyme is fully saturated with the substrate
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what does k1 and k2 represent
k1=binding k2= catalysis
5 of 20
what is v0, what is [p] at this point
inital velocity. [p]=0
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what do k-1 and k-2 represent
k-1= dissosiation of ES complex. k-2 is zero as products cant be turned back to ES complex
7 of 20
what is Km
ratio of rate constants. shows affinity of e for s. low Km shows high affinity for ES, greater affinity so greater reaction. uses [s] at 1/2 Vmax
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what is constant at Vmax, explain
Kcat. at Vmax and high [s], only [e] can increase rate. reperesents max number of s converted to p per second by the active site
9 of 20
use of lineweaver equation
converts m m equation to y=mx+c form so can plot linear graph
10 of 20
issuses with mm equation (4)
assumes free diffusion and random collisons. cytoplasm is gel like preventing free movement . hetrogenous enzyme reaction mean molecular mobility of e and s are restricted. homogenous enzymes recation mean e and s movement are limited
11 of 20
describe the three multisubstrate recations
1. random- independant binding of substrates to independant binding sites. 2. ordered- one substrate binds before next binds. 3. ping pong- one substrate binds and produced product inducing a intermidate enzyme, which allows next substrate to bind
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what are the reversible inhibitors
competivie, non competive , uncompetive
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describe competitive inhibition
binds to active site, similar shape to s, reversible by increasing [s]. vmax unchanged. Km decreases as now has affinity for inhibitor
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describe non competitive inhbibition
binds to allosteric site. diff shape to s. distorts e shape so s cant bind. v max decreases as reduces number of e for reaction. km stays same
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describe uncompetivie inhbition
seperate site. only binds to formed es complex. km decreases, vmax decreases
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describe irreversible enzyme inhibition
binds covelantly to enzyme
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what is the michaelis-menten equation
V0=Vmax[S]/Km + [S]
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km michelais menten equation
km=k-1+k2/k1
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line weaver burke equation
1/v0= (km/vmax) 1/[s] + 1/ vmax
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Other cards in this set

Card 2

Front

describe zero order enzyme rate

Back

no relationship between v and [s]

Card 3

Front

describe second order enzyme rate

Back

Preview of the front of card 3

Card 4

Front

what does v and vmax represent

Back

Preview of the front of card 4

Card 5

Front

what does k1 and k2 represent

Back

Preview of the front of card 5
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