Lecture 17 Flashcards

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1
Q

Exergonic reaction

A

proceeds with a net release of free energy is spontaneous

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2
Q

Endergonic reaction

A

Absorbs free energy from its surrounding and is non-spontaneous

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3
Q

free energy

A

a living systems free energy is energy that can do work when temperature and pressure are uniform as in a living cell

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4
Q

Activation energy

A

the initial energy needed to start a chemical reaction is called the free energy of activation or activation energy

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5
Q

how enzymes speed up reactions

A

in catalysis, enzymes of other catalysts speed up specific reactions by lowering the Ea barrier

enzymes do not affect the change in free energy; instead they hasten reactions that would occur eventually

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6
Q

substrate specificity of enzymes

A

the reactant that an enzyme acts on is called the enzyme substrate

the enzyme binds to its substrate, forming an enzyme-substrate complex

while bound the activity of the enzyme coverts substrate to product

the reaction catalysed by each enzyme where the substrate binds

induced fit of a substrate bring chemical groups of the active site into positions that enhance their ability to catalyse the reaction

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7
Q

How enzymes lower the Ea barrier

A

enzymes catalyse reactions by lowering the Ea barrier of a specific reaction pathways

enzymes do not affect the change in free energy: instead they hasten reactions that would occur eventually

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8
Q

Catalysis in the enzymes active site

A

in an enzymatic reaction, the substrate binds to the active site of the enzyme

enzymes are extremely fast acting and emerge from reactions in their original form

very small amounts of enzyme can have substantial metabolic effects because they are used repeatedly in catalytic cycles

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9
Q

The active site and catalytic cycle of an enzyme

A
  1. substrate enter active site
  2. substrates are held in active site by weak interactions forming enzyme substrate complex
  3. the active site lowers Ea
  4. substrates are converted to products
  5. products are released
  6. active site is available for new substrates
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10
Q

The active site can lower Ea barrier by

A

-orientating substrates correctly
-straining substrate bonds
-providing a favourable microenvironment
-covalent bonding to the substrate

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11
Q

Saturated enzyme

A

where active site is engaged

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12
Q

Effects of local conditions on enzyme activity

A

an enzymes activity can be affected by:
- general environmental factors such as temperature and pH
- Chemicals that specifically influence the enzyme

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13
Q

Effects of temperature and pH on enzyme

A

each enzyme can function over a fixed range of temperature and pH conditions

so each enzymes has an optimal pH and temperature at which it can function

optimal conditions favour the most active shape for the enzyme molecule

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14
Q

Cofactors

A

non protein enzyme helpers
- may be inorganic (such as a metal in ionic form) or organic
- an organic cofactor is called a coenzyme
- coenzymes include vitamins

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15
Q

Enzyme inhibitors

A

competitive inhibitors- binds to the active site of an enzyme, competing with the substrate

noncompetitive inhibitors- bind to another part of an enzyme =, causing the enzyme to change shape and making the active site less effective

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16
Q

regulation of enzyme activity helps control metabolism

A

chemical chaos would result if a cells metabolic pathways were not tightly regulated

a cell does this by switching on or off the genes that encode specific enzymes or by regulating the activity of enzymes

17
Q

Allosteric regulation of enzymes

A

may either inhibit or stimulate an enzymes activity

allosteric regulation occurs when a regulatory molecules binds to a protein at one site and affects the proteins function at another site

18
Q

Allosteric activation and inhibition

A

mostly allosterically regulated enzymes are made from polypeptide subunits, each with its own active site

the enzyme complex has active and inactive forms

the binding of an activator stabilised the active form of the enzyme

the binding of an inhibitor stabilises the inactive form of the enzyme

19
Q

Allosteric enzyme structure

A

four subunits each with an active site and regulatory site

20
Q

Activation and inactivation of allosteric enzymes

A

oscillation changes an allosteric enzyme from active to inactive or vice versa

activators stabilise both active and inactive forms of allosteric enzymes

21
Q

Cooperativity

A

is a form of allosteric regulation that can amplify enzyme activity
- one substrate molecule primes an enzyme to act on additional substrate molecules more readily

allosteric because binding by a substrate to one active site affects catalysis in a different active site

22
Q

Feedback inhibition

A

in feedback inhibition, the end product of a metabolic pathway shuts down the pathway

feedback inhibition prevents a cell from wasting chemical resources by synthesising more product than is needed

23
Q

Localisation of enzymes within the cell

A

structure within the cell help bring order to metabolic pathways

some enzymes act as structural components of membranes

in eukaryotic cells, some enzymes reside in specific organelles