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Biology 2 > bio 2 2nd exam (ENZYMES) > Flashcards

bio 2 2nd exam (ENZYMES) Flashcards

1
Q

Hydrolase

A

Hydrolase: General term for enzymes that catalyze a hydrolytic cleavage reaction

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2
Q

Nuclease

A

Nuclease: Break down nucleic acids by hydrolyzing bonds between nucleotides.

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3
Q

Protease

A

Protease: Break down proteins by hydrolyzing peptide bonds between amino acids

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4
Q

Synthase

A

Synthase: General name used for enzymes that synthesize molecules in anabolic reactions by condensing two molecules together

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5
Q

Isomerase

A

Isomerase: Catalyze the rearrangement of bonds within a single molecule

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6
Q

Polymerase

A

Polymerase: Catalyze polymerization reactions such as the synthesis of dna & rna

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7
Q

types of enzymes Kinase

A

Kinase Catalyze the addition of phosphate to molecules. Protein kinases are an important group of kinases that attach phosphate groups to proteins.

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8
Q

types of enzymes Phosphatase

A

Phosphatase Catalyze the hydrolytic removal of a phosphate group from a molecule

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9
Q

type of enzymes Oxido-reductase

A

Oxido-reductase General name for enzymes that catalyze reactions in which one molecule is oxidized while the

other is reduced. Enzymes of this type are often called oxidases, reductases, and dehydrogenases

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10
Q

type of enyme ATPase

A

ATPase Hydrolyze ATP. Many proteins with a wide range of roles have an energy-harnessing ATPase activity as part of their function, for example, motor proteins such as myosin and membrane transport proteins such as the sodium–potassium pump.

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11
Q

Metabolism

A

Step by step process by which cells take nutrients from their environment and convert them into sufficient components to double their mass and then become 2 cells (through mitosis)

All the biochemical reactions that take place in the cell are called its metabolism

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12
Q

Anabolism

A

nreactions that require energy to synthesize complex molecules from simpler ones

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13
Q

Catabolic rxns involve…

A

nCatabolic rxns involve oxidation and reduction rxns

reactions that release energy by breaking complex molecules into simpler ones.

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14
Q

Oxidation

A

Oxidation: the loss or removal of electrons

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15
Q

Reduction

A

Reduction: the gain of electrons

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16
Q

Function of Metabolism. Synthesis

A
  1. Synthesis (double in mass) and division
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17
Q

Function of Metabolism (cont.)

Reproduction

A
  1. Reproduction

Making more cellular materials

Requires the production of starting materials

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18
Q

Metabolic task (5)

A

1.Bringing nutrients into the cell

  1. Catabolism- convert nutrients into group of orgo compounds sereve as a starting point, ((12 precursor metabolites, ATP (Reducing power ie: NADH))
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19
Q

Metabolic task (5) (cont.)

biosynthesis

A

3. biosynthesis

Making small molecules the cell needs

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20
Q

Metabolic task (5)

polymerization

A

4. polymerization-To form macromolecules

5th is assembly

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21
Q

metabolic pathway

A

•metabolic pathway begins with a specific molecule and ends with a product. •Each step is catalyzed by a specific enzyme

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22
Q

Catabolic pathways

A

•Catabolic pathways release energy by breaking down complex molecules into simpler compounds

23
Q

Anabolic pathways

A

•Anabolic pathways consume energy to build complex molecules from simpler ones

24
Q

Bioenergetics

A

•Bioenergetics is the study of how organisms manage their energy resources

25
Q

Energy

A

•Energy is the capacity to cause change

26
Q

Kinetic Energy

A

•Kinetic Energy is energy associated with motion

27
Q

Heat (thermal energy)

A

•Heat (thermal energy) is kinetic energy associated with random movement of atoms or molecules

28
Q

Potential energy

A

•Potential energy is energy that matter possesses because of its location or structure

29
Q

Chemical energy

A

•Chemical energy is potential energy available for release in a chemical reaction

30
Q

exergonic reaction- types of rxns

A

exergonic reaction proceeds with a net release of free energy and is spontaneous- (–A process is spontaneous and can perform work only when it is moving toward equilibrium) (ENERGY RELEASED) Decrease in Gibbs free energy. Increase in stability. Spontaneous. Movement towards equilibrium. Coupled to ATP production. CATABOLISM!

31
Q

endergonic reaction (2nd type of rxn)

A

•An endergonic reaction absorbs free energy from its surroundings and is nonspontaneous. (ENERGY REQUIRED) Increase in Gibbs free energy. Decrease in stability. Not Spontaneous. Movement away from equilibrium. Coupled to ATP utilization. Anabolism

32
Q

ATP coupling. (3)

A

•CHEMICAL •TRANSPORT •MECHANICAL. •Most energy coupling in cells is mediated by ATP

33
Q

energy coupling

A

•To do work, cells manage energy resources by energy coupling, the use of an exergonic process to drive an endergonic one. coupled rxns are exergonic

34
Q

Enzymes Speed Up Reactions

A

–Provide Specificity: only the desired reaction occurs Permit reactions under mild conditions (only those reactions that need to happen, happen) Natures catalysts.

35
Q

Activation Energy Barrier

A

Enzymes decrease activation energy. •The initial energy needed to start a chemical reaction is called the free energy of activation, or activation energy (EA)

36
Q

substrate

A

•The reactant that an enzyme acts on is called the enzyme’s substrate

37
Q

enzyme substrare complex

A

•The enzyme binds to its substrate, forming an enzyme substrare complex

38
Q

Active site

A

•The Active site is the region on the enzyme where the substrate binds

39
Q

Induced fit

A

•Induced fit of a substrate brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction

40
Q

active site can lower activation energy by (enzymes, catalyst)

A
  • cov bon to substrate
  • provide favorable micro-enviornment
  • straining substrate bond
  • orientating substrate correctly
41
Q

enzyme shape

A
  • SHAPE! specificity is controled by stucture. unique fit of substrate with eneymes controls the selectivity for substrate and the product yeild
  • enzyme shape=tighter enduced fit
  • bring chem groups in position to catalyze the reaction
42
Q

enzyme specificity

A
  • succine dehydrogenase always catalyze an odxidation-reduction rxn and its substrate is succinic acid
  • alcohol dehydrogenase always catalyzes a # of different alcohols
43
Q

proximitiy and strain effects (Mechanisms)

A
  • substrate fit catalytic site with proper origention to catalytic groups.
  • enzyme conformation changes to give a strained E-S complex.
  • facilitates attaining the transition state
44
Q

electro-static effects (mechanisms)

A

–Substrate binding site excludes H2O & lowers the dielectric constant strengthening electrostatic interaction between E and S.

45
Q

•Acid-base catalysis

A

–Enzyme side chains act as proton donors and acceptors.

46
Q

Covalent Catalysis

A

–Powerful nucleophilic side chain forms an unstable covalent bond to the substrate.

47
Q

Local Conditions on Enzyme Activity

A
  • General environmental factors, suchas temperature and pH
  • Chemicals that specifically influence the enzyme
  • Chemicals Bind to the active site, ultimately shutting enzyme down
48
Q

Cofactors

A
  • Cofactors are nonprotein enzyme helpers
  • Cofactors may be inorganic or organic
  • organic cofactor = coenzyme
  • coenzymes include vitamins
49
Q

Enzyme Inhibitors

  • Competitive inhibitors
  • Noncompetitive inhibitors
A
  • Competitive inhibitors bind to the active site of an enzyme, competing with the substrate (enzyme typically not released)
  • Noncompetitive inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective (change shape=change function)
50
Q

Allosteric regulation (can be good or bad)

A

•Allosteric regulation occurs when a regulatory molecule binds to a protein at one site and affects the proteins function at another site

51
Q

Allosteric Activation and

Inhibition

A
  • Each enzyme has active and inactive forms
  • The binding of an activator stabilizes the active form of the enzyme
  • The binding of an inhibitor stabilizes the inactive form of enzyme
52
Q

cooperativity (allosteric regulation)

A

•In cooperativity, binding by a substrate to one active site stabilizes favorable conformational changes to all other subunits

53
Q
A

Biology 2 (4 decks)

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