chapter 8 pt 1 Flashcards

1
Q

catabolism

A

break bonds of large molecules
-release energy

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2
Q

anabolism

A

forms large macromolecules
-needs energy

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3
Q

what do enzymes do to chemical reaction

A

increase rate by lowering energy of activation
-not permanetly altering the reaction
-it is a physical site for substrate molecules to bind

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4
Q

simple enzyme

A

only proteins

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5
Q

conjugated enzymes

A

holoenzymes
-have protein and non protein molecules
-apoensyme and cofactors (can have one or both)

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6
Q

apoenzyme

A

part of the conjugate enzyeme that is protein
-secondary (h bond), tertiary (side group) and some quaternary structures
-site for substrate binding (active site) or catalytic site
-when the substrate moves into the active site a temporary enzyme substrate union occurs

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7
Q

cofactors

A

non protein part of the conjugates enzyme
-can be metallic (iron, copper, magnesium)
-can be coenzymes (an organic molecule like a vitamin)
-heme of hemoglobin

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8
Q

induces fit

A

the temporary union of the substrate moving into the active site
-this is not the lock and key model
-the key (substrate) never fits the lock right it has to be forced into the apoenzyme

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9
Q

synthesis

A

condensation reactions
-anabolic reaction that forms covalent bonds
-requires atp and releases one water molecule for each bond formed

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10
Q

hydrolysis reaction

A

Catabolic reaction
Input water to break bonds
-released energy can be harvested and used elsewhere

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11
Q

enzymes are sensitive to what?

A

their environment
-temp, ph and osmotic pressure of their organisms habitat
-ex: extremophile pol for pcr

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12
Q

labile

A

chemically unstable enzymes from changes in organisms habitat

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13
Q

denaturation

A

weak bonds that maintain the shape of the apoenzyme are broken due to changes in the organisms environment

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14
Q

constitutive enzymes

A

always present and produced in equal amounts/ rates regardless of the amount of substrate

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15
Q

regulated enzymes

A

not always present their production has to be turned on / induced and then repressed/ turned off in response to changes in the substrate concentration

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16
Q

how do we control enzyme activity

A

enzyme represion and enzyme induction

17
Q

enzyme repression

A

inhibits at the genetic level by controlling the synthesis of enzymes

18
Q

enzyme induction

A

enzymes are only made when suitable substrates are present

19
Q

direct enzyme control

A

competitive inhibition and noncompetitive inhibition

20
Q

competitive inhibition

A

substances that resemble the normal substrate and compete with the substrate for the active site

21
Q

noncompetitive inhibition

A

enzymes are regulated by the binding of molecules other than the substrate away from the active site
-allosteric inhibition
-molecule changes the shape so the original cant bind anymore

22
Q

steps of metabolic pathways are all….

A

all catalyzed by a different enzyme

23
Q

metabolic pathway

A

sum of the steps from start to finished product

24
Q

mutlienzyme system shaptes

A

linear, cyclic, branched (divergent and convergent)

25
energy
ability to do work and cause change
26
energy forms
thermal, radiant, electrical, mechanical, atomic and chemical
27
endergonic reaction
consume energy -anabolic -cold beaker
28
exergonic
release energy -catabolic -hot beaker
29
released energy
stored temporarily in high phosphate molecules -energy of these molecules is used in endergonic cell reactions
30
redox rxn
-happen in pairs -electron donor and an acceptor which makes up the redox rxn -released energy can be captures to phosphorulate ADP or smth else
31
electron and proton carriers
most are coenzymes -accept and release electrons and hydrogen to facilitate the transfer of redox energy
32
atp parts
-adenine (nitrogenous base) -ribose (5 carbon sugar) -3 phosphate groups
33
atp purpose
remove terminal phosphate and release energy -replenished in a constant cycle -used to make RNA
34
ATP formation mechanisms
-substrate level phosphorylation -oxidatice phosphorylation -photophosphorylation
35
substrate level phosphorylation
transfer phosphate group from a phosphorylated compound (substrate) to ADP
36