Enzymes - Davies Flashcards

1
Q

Cofactors

A

small inorganic attachments to enzymes

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2
Q

Coenzymes

A

Organic Molecules that attach to enzymes.

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3
Q

Metalloprotease

A

Require metal ion to cleave proteins (uses Zn)

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4
Q

Kinase

A

Uses Mg to work and is calcium concentration depended. it wil lphosphorylate

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5
Q

Oxidoreductase

A

oxidate and reduction reaction

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6
Q

Transferase

A

transfer functional group

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7
Q

Hydrolase

A

catalyze bond cleavage with water

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8
Q

lyases

A

c-c bond cleavage

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9
Q

isomerase

A

move a group or a double bond

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10
Q

ligases

A

catalyze joining of a c-c bond

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11
Q

apoenzyme

A

enzyme without cofactor

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12
Q

haloenzyme

A

functional enzyme with cofactor

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13
Q

Trypsin

A

Serine protease, cleaves at arginine and lysine (basic)

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14
Q

Chymotrypsin (just what it cleaves)

A

serine protease cleaves at Phe, met, trp

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15
Q

Thrombin

A

serine protease cleaving at arg-gly bonds

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16
Q

ΔE*

A

Activation Energy without enzyme

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17
Q

ΔGo

A

Free energy change

18
Q

ΔEo+

A

Activation Energy of the catalyzed reaction

19
Q

Properties of an Active Site (4)

A

Crevice Creates microenvironment
3D fold
Held by weak non-covalent interactions
small part of enzyme

20
Q

Proximity Affect

A

Brings substrates closer together

21
Q

Lock and Key

A

Enzyme Substrate Complement one another

22
Q

Induced Fit

A

Enzyme Changes shape as substrate binds give energy to reach state

23
Q

V in kinetics

A

Rate or change in [] of reactants or products over time

24
Q

K1 in Kinetics

A

Rate Constant of forward reaction

25
Q

K2 in kinetics

A

Rate constant of the reverse reaction

26
Q

Michaelis Menton Shape

A

is a hyperbolic curve

27
Q

Allosteric Enzyme Curve Shape

A

sigmoidal curve

28
Q

At low Concentration of S what is the rate compared

A

The rate is proportional to the concentration of S and is first order

29
Q

at high S concentration rate is compared how

A

At high S concentration rate is independed and zero order

30
Q

What are the three michaelis Menton Assumptions

A

1 - formation and breakdwon are constant and so at steady state
2- product formation is irreversible
3 - K2

31
Q

Km is what

A

the michaelis menton constant. It combines all rate constants for formation and dissappearance. It is the concentration of substrate when it is half maximum

32
Q

What is the Km formula

A

Km = (k2+K3)/K1

33
Q

What does a high Km or low Km mean

A

High Km means loose binding low km means tight binding

34
Q

Vformation =

A

K1[s][E]

35
Q

V breakdown =

A

(K2+K3)[ES]

36
Q

Kcat is

A

the rate constant for the formation of P

37
Q

Lineweaver Burke Plot Readings

A

X Axis - 1/[s]
Y Axis - 1/V
X intercept = -1/km
Y Intercept 1/V

38
Q

Sequential Displacement

A

Substrate binds before product is released

39
Q

Ping Pong double displacement

A

one or more products are released before all substrates are

40
Q

Reversible Types of Inhibition and explanation

A

Competitive - Binds enzyme in active site and has a similar structure to substrate
non-competitive - binds to a site not the active site to change conformation of enzyme

41
Q

Kinetics of Competitive Inhibitor

A

Km will be larger because affinity decreases
the Vmax does not change
Therefore a graph would have increasing slope on a lineweaver burke plot