Kinetics

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Mixed Non Competitive

Back 1

Front 2

Uncompetitive Competition

Back 2

Front 3

Non Competitive

Back 3

Front 4

Competitive

Back 4

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y-axis

Back 5

1/Vo

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x-axis

Back 6

1/[S]

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KM

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1/2 Vmax, x-value

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pseudo first order kinetics

Back 8

within the box of KM

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Vmax

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max velocity, max amount of speed the enzyme can work out.

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Zero order kinetics

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Vmax, rate is independent of concentration of the reactant (substrate)

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When does M-M apply?

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-unimolecular reaction or bimolecular when the [one] does not change

- irreversible rxn (rare) or [P] = 0 initial cond.

-concentration of substrate is vastly different than E total also [E]T

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First Order Kinetics Equation

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Vo= k[s]1 , Vo proportional to [S]o

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Zero Order Kinetics Equation

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V= k [s]0

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Intracellular Conditions

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Constant:

Temp, PH, Concentration, Pressure

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Metabolic Pathways

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The feedback inhibitor (the end enzyme) inhibits the first possible enzyme in the pathway.

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allosteric site

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an inhibitor attaches to the allosteric site and thus closes the active site of the protein

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Catalytic Power

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rate w/enz

/

rate w/o enz

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Regulation

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ability to be turned on and off

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specificity

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for both rxn and reactant/ prods

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Branched Pathways

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two different pathways

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anabolic

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use small metabolites and enzymes source build macromolecules

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catabolic

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going to breaking down macromolecules

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specificity

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only fit into specific substrate of a specific protein

also only specific for a specific reaction (catalytic side chains on enz arranged in space)

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ligases

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reactions in which new bonds are formed between carbon and another atom; energy is required

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isomerases

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reactions in which a compound is converted to its isomer

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lyases

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reactions in which groups are removed without hydrolysis or addition of groups to a double bond

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hydrolases

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hydrolysis reactions

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transferases

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transfer reactions of groups, such as methyl, amino, and acetyl

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oxidoreductases

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oxidation-reduction reactions

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Random Single Displacement

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Ordered Single Displacement

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Double Displacement or Ping Pong

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x-intercept Displacement

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-1/Ks

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x-intercept of Ping-Pong

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-1/Kam (1+ Kbm/[B]

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holoenzyme

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catalytically active complex of protein and prosthetic group

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apoenzyme

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protein without the prostheticgroup; it is catalytically inactive.

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prosthetic groups

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a coenzyme is firmly associated with its enzyme, perhaps evenby covalent bonds, and it is difficult to separate the two

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A ----> I ----> J ----> P Which enzyme will be the inhibitor and which enzyme will be inhibited?

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P will inhibit A

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unimolecular reactions

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the molecularity equals 1, first order reactions

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bimolecularreactions

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its molecularity is 2, where two molecules must react to yield products, 2nd order reactions, rarely found

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second-order

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first-order with respectto A and first-order with respect to B

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second-order rate law

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v = k[A][B] or v = [A]^2

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first-order rate law

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v = k[A]

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transition state

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the probability is very high that theparticular rearrangement accompanying the A---->P transition will occur

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Back 45

raising the temperature brings the activation energy up to the needed delta G double dagger so the reaction can be performed

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Back 46

Catalystswork by lowering the energy of activation rather than by raising the average energyof the reactants. Catalysts accomplish this remarkable feat by combiningtransiently with the reactants in a way that promotes their entry into the reactive,transition-state condition.

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Rates are doubled when temperature is increased at increments of ______ degrees C.

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10

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Vmax

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At high [S], v becomesvirtually independent of [S] and approaches a maximal limit.

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saturation effect

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When v shows no increase even though [S] is increased, the system is saturated withsubstrate.

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active site

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that place on the enzyme where S binds

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steady-state assumption

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That is, ES is formed asrapidly from E + S as it disappears by its two possible fates: dissociation to regenerate E + S and reaction to form E + P. That is, the change in concentration of ES with time, t, is 0.

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equation for back reaction

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v = k-2[E][P]

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initial velocity

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is only observed in the reactionimmediately after E and S are mixed in the absence of P (back reaction)