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42 Cards in this Set

  • Front
  • Back
organic compounds-----fermentation products

organic compounds - glucose 6-C, electron and H+ flow is interal via redox rxns

fermentation (ethanol, lactate) products contain much of orig E of glucose
---C in glucose in products too
---electrons/H+s not gone, still in products
aerobic respiration
organic compounds---CO2

org compounds (glucose)
---elec/H+ flow is external via redox rxns to O via ETS

product is CO2 and E in glucose stored in reduced molecules (NADH and FADH2)
anaerobic respiration
organic compounds---CO2

org compounds-
(glucose, cellulose)
--electron/H+ flow is external via redox rxns

product is CO2 and the E is reduced mol's NH4, H2S, CH4

swamp, flames

bacteria live w/o much O

look @ q's
axioms of enzymology
1. enzymes are proteins
2. enzymes are macrmols
3. enzymes made from a.acids joined by peptide bonds
4. amino acids are of the l-config
5. props -->ed by sequence of a.acids
6. orderly structures (crystallized, or still retain activity)
7. catalytic action carried out at active site
8. enzymes form an enzyme substrate complex w/ their substrates
9. rxn rate of enzyme catalyzed rxn depends on [substrate]
10. rates of conversion of the enzyme substrate complex [ES] to product is very FAST (turnover number high)
axioms of enzymology: 1. enzymes are proteins
enzymes are proteins, (a few RNA mol's that act similar to enzymes have been found)
axioms of enzymology: the active site
where enzyme acts w/ substrate

a geometrically discrete region of the enzyme

ex: hemoglobin w/ oxygen

catalytic action carried out within an active site
axioms of enzymology: turnover number
how much substrate -->ed to product per enzyme per active site per unit of time

rates of conversion of the enzyme substrate complex [ES] to product is very FAST (turnover number high)
___ and ___ affect active site
pH & temp

at higher temps, rate decreases quickly

pH: pepsin works well low pH
temp: trypsin high pH
substrate level phosphorylation
ATP made on spot @ active site

substrate gives Pi to ATP from ADP

enough E released to ADP --> ATP
an ___ exists between substrate --> product
energy barrier
energy barrier is a ___ that ___ must overcome in order to be raised to a higher E level
energy barrier is a ENERGETIC HILL that the SUBSTRATE must overcome in order to be raised to a higher E level
activation E
'fleeting molecular moment'

enzymes decrease E of activation to start the rxn
--proteins, regulate metabolism



--large macromol's w/ small active sites

don't change equilib of rxn

speed up rxns by moving substrates, adding charges to substrates, or by inducing strain on substrate
transition state
top of 'energetic hill' E barrier

reactant (A) raised to higher unstable E level and will --> forward P or decay bk to A

diff b/t ground state and transition state = free E of activatoin
rxn rates caused by
increasing temp, increasing # mol's
activation E can be lowered by
adding a catalyst

catalysts lowering activation energies
in living systems, the ___ is an enzyme
in living systems, the catalyst is an enzyme
michaeli menten kinetics equation
E+S <--> ES ---> E +P

E enzyme
S substrate
ES enzyme substrate complex
P products
M&M kinetics factors of the equation
depends on

phy factors:
pH, temp, pressure

chem factors: [S] and [E] which --> [ES] --> [P] and [E]
product is a ___
product is a rate
use ___ to compare enzymes
use MAX VELOCITY to compare enzymes

MAX amt of substrates per unit of volume

since [E] not limiting the rxn, as amt of [S] increases, so does velocity of the rxn
rate of enzymatic rxn if amt of [E] NOT limiting and substrate is increased
[S] v. V

levels off
influence of phy factors pH and temp on enzymes
as [S] increases, so does volume

enzyme starts converting -->

no limit --> keeps going up but not realistic b/c no space! not unlimtied supply of enzymes

there is a fixed amt
rate of enzymatic rxn if the amt of enzyme is limiting and substrate is increased
eventually will stop increasing -->

maximum velocity: max amt of substrate created
max velocity
use max velocity to compare enzymes

max amt of substrate created

enzyme limiting and substrate increased --> increased velocity
compare enzymatic rxns

since may [S] produce Vmax, proposed this

1 [substrate[ --> 1/2VMax

Km - [S] that -->es 1/2 max vel
compares how single enzyme may react to 2 diff substrates

[S] that --> Vmax/2

S1 and S2 diff substrates, produce same max veloc Vmax....takes much more of S2 to reach Vmax than S1

S1 gets faster, takes less to get to Vmax

no diff in how enzyme rxs

Km1 lower than Km2 --> enz higher affinity for sub1 than sub2

E+S1 --> >er ES complex than E+S2
1. if [ES] is large then Km is small

small Km=good affinity of enzyme

close to 0--> enz/sub high affinity

2. if [ES] small then Km large
large Km=less affinity of enz for substrate
almost impossible to measure [ES] so --> formula
v=Vmax [S]
Km + [S]

michaelis Menten Equation

way of relating velocity of rxn to [substrate]
michaelis menten kinetics and equation are true if following conditions met
1. enzymatic rxns go thru an ES complex
2. rate of conversion of [ES]--> [P] depends on rate of ES formed

3. [S] is greater --> no need to correct for S in ES complex

4. velocity proportional to [ES] complex

5. vmax is proportional to the amt of enzyme participating in the rxn
(a) if [S] < Km, v depends on [S]
(b) if [S] sig >er than Km, velocity is Vmax
(c) when [S]=Km, velcotiy is Vmax/2 (equilib)
(d) if [S] increased, other conditions constantm, velocity increase to Vmax and no more
(e) at Vmax, an increase in [S] will have no influence on velocity
active site
specific substrate binding are of enzyme

where enzyme's shape comes from
enzyme-substrate complex (ES)
once enzyme bound to active site
bind to enzymes and slow rate of rxn

--irreversible inhibition
--reversible inhibition
-~~~~ non/competitive ~~~~~~inhibitors
irreversible inhibition
inhibitors covalently bond to an enzyme and destroy its active site
reversible inhibition
inhibitgors bind to/alter the active site but its changeable

dpeends on [] of inhibitor and substrate
competitive inhibitors
type of reversibile inhibition

compete with substrate for the active site
noncompetitive inhibitors
irreversibile inhibiton

bind elsehwere but alter active site so that substrate can't bind/ rate of binding decreased
M&M discovered what?
[ES] complex
two things that occur @ transition site
1. can go bk down to A, becomes the same [S]

2. or can --> product

describes what?
compares how [S] rxs w/ the enzyme
Km small --

Km large---
Km small -- [ES]/affinity big

Km LARGE -- affinity SMALL/[ES] small
vmax value know as enzymes _____ value
constant, fixed value