Enzyme Kinetics II Flashcards

1
Q

in the concentration vs time reaction, when the reactions is starting what is high

A

substrate & enzyme

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2
Q

in the concentration vs time reaction, when the reactions is starting what is low

A

ES low
product low

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3
Q

the state when the enzyme is just enzyme with the substrate, it is called

A

pre-steady

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4
Q

rate of formation of enzyme substrate complex is

A

directly proportional to the rate of the ES complex

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5
Q

For an enzyme catalyzed reaction, if the Vo is 10mM min-1 when the substrate concentration is 10mM, then what must Vmax be if we know that Km=30mM

A

40 mM min-1

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6
Q

what type of allostery is when it is the same ligand that is modifying the subunit to either positively or negatively

A

homotropic

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7
Q

what type of allostery is when it is the different ligand that is modifying the subunit to either positively or negatively

A

heterophic

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8
Q

when the binding of the inhibitor changes the site making it impossible for the substrate to bind is called

A

allosteric inhibition

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9
Q

when the binding of the ligand changing the active site allowing for the substance to bind to the substrate is called

A

allosteric activation

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10
Q

how are enzyme regulation

A

allostery
covalent modification
cleavage

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11
Q

inactive form of enzyme is called

A

proenzyme=zymogen

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12
Q

inactive form of chymotrypsin and trypsin

A

chymotrypsinogen and trypsinogen

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13
Q

when pro is added to like protein or non enzyme, what doe that mean

A

procollagen

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14
Q

what is the direction of converting inactive precursor to active enzyme by enzymatic cleavage

A

one-way street, unidirectional

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15
Q

benefit of making an inactive enzyme to active enzyme

A

because u have to wait to get the stimulus from the cell to do that so the enzyme doesn’t eat up other rthings

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16
Q

chymotrypsinogen chews to which amino acids

A

aromatic residue

17
Q

Trypsinogen chews at which amino acids residue

A

Lysine residue

18
Q

enzyme that add modification to the protein are called

A

writers

19
Q

enzyme that remove modification to the protein are called

A

erasers

20
Q

what do covalent structure affect

A

affect structure (therefore function)
changes charges
alter binding surface
blocks active sites

21
Q

what do covalent structure result in

A

enzyme on/off
change localization
change substrate preference
change binding partners
degradation

22
Q

—– enzyme adds phosphorylates and —– enzyme removes phosphorylation

A

kinases, phosphotases

23
Q

which is specific kinase or phosphotases

A

kinase

24
Q

glycogen phosphorylase exist in which form

A

active and less active

25
Q

methotrexate is used to

A

inhibit folic acid , reduces dntp

26
Q

round up used in our yards

A

has aromatic amino acid synthesis inhibitor

27
Q

molecules interfering with catalysis are called

A

enzyme inhibtors

28
Q

types os reversible inhibitors

A

competitive
uncompetitive
mixed
non competitive

29
Q

enzyme inhibitors can affect which values

A

Vmax & Km , Vmax apparent & K max apparent

30
Q

when an enzyme binds to its substrate and then an inhibitor looks exactly similar directly competing for the binding site, this is called

A

competitive inhibitor

31
Q

when an inhibitor binds to a completely different site on an enzyme that affects the way the enzyme function, this is called

A

uncompetitive inhibitor

32
Q

when an inhibitor changes the active site of the protein, this is called

A

noncompetitive inhibtor

33
Q

what changes in competitive inhibitor

A

no changes in Vmax, changes in Km

34
Q

in uncompetitive inhibitor, can the reaction move forward ?

A

no

35
Q

what change sin uncompetitive inhibitor

A

Vmax, Km

36
Q

when binding E and ES at the site is distinct from the substrate, this is called

A

mixed competitor

37
Q

which inhibitor binds like a substrate and is acted upon by enzyme at some point changes the structure of the enzyme

A

suicide inhibitor