Lecture 3 Flashcards

1
Q

Pepsin works at ?

A

PH 2 Stomach

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2
Q

Amylase works at ?

A

PH 7 Mouth

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3
Q

Arginase “

A

PH 10 kidneys

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4
Q

As temperature increases what happens to the flexibility in the protein back bone

A

increases

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5
Q

Optimum temperature is dependent on?

A

hydroponic and hydrophilic interactions

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6
Q

K=

A

turnover number

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7
Q

e+s> es

k for forward and reverse reaction

A

k1 k-1

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8
Q

Es>E+ P

K for forward and reverse reaction

A

k2

not reversible

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9
Q

competitive Inhibitor?

A

has a similar shape to substate and occupies the active site

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10
Q

Inhibitor effect is reduced by

A

substrate concentration

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11
Q

Can enzyme controlled reaction reach the same Vmax with and without the inhibitor present?

A

yes if substate concentration is great enough

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12
Q

Km of the inhibited enzyme controlled reaction?

A

greater than without the inhibitor

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13
Q

In linnear regression km?

A

is closer to zero

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14
Q

Non-competitive inhibitor?

A

a small molecule which binds to a remote site on an enzyme and effects Kcat

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15
Q

Where do non competitive inhibitors bind?

A

allosteric sites

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16
Q

effect on active site (when in the presence of a non-competitive inhibitor)

A

conformational change of the enzyme active site, cannot bind to a substrate

17
Q

Effect non-competitive inhibitor has on km

A

no effect

18
Q

Y intersect on the liner regression on Micheal-mentons graph when enzyme is in the presence of a non-competitive inhibitor ?

A

greater

19
Q

Positive regulator ?

A

activator

20
Q

negative regulator

A

repressor

21
Q

Uncompetitive inhibitor?

A

A substrate which binds to the enzyme substrate complex and stops the formation of any further products

22
Q

uncompetitive inhibitors effect what which Is measured on a Micheal menton’s graph

A

Both Km and Vmax

23
Q

Allosteric inhibition?

A

In which a product from an enzyme cascade inhibits the first enzyme

24
Q

Curve to represent allosteric kinetics ?

A

sigmoidal curve not Micheal menton

25
Q

Cleavage activation is an example of?

A

Covalent regulation

26
Q

Cell signalling an example of?

A

Covalent regulation

27
Q

Adenylation is ?

A

addition of AMP to an enzyme

28
Q

Trysin enzyme Is made in?

why?

A

an inactive form: Tripsogen which when activated by the absence of an inhibitor, becomes trypsin

This mechanism is to stop trypsin damaging cells until outside cells where it is activated

29
Q

Oxidoreducases ?

A

oxidation reduction reaction

30
Q

Transferases?

A

transfer chemical groups

31
Q

Hydrolase’s ?

A

Induce hydrolytic cleavage

32
Q

Lyases

A

Cleave c-n c-o c=0 by eliminating molecules. Leaving double bonds, rings or conversely addition of groups to double bonds

33
Q

Isomerases

A

catalyse geometric/strctural changes within molecule

34
Q

Ligases

A

joining together of two groups coupled with hydrolysis of diphosphate bond