Metabolism Flashcards

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1
Q

Define metabolism

A

Metabolism is from Greek and means change. It is the process of how all living conjure energy and transform it to something tangible.
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All living things must have a mechanism to acquire energy from. If not it’s not dead. Generally speaking there are two classes and a lot of subclasses and inbetweens.
Autotrophs can be defined as the producers because they make their own food through raw materials and energy.
Heterotrophs are known as the consumers and are dependent on chains formed by other organisms.

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2
Q

What are trophic levels and how are they related to the food chain

A

In all food chain there are three trophic levels.
The first trophic level is always occupied by the producers, thereafter the second level is occupied by the herbivores, then on the third level we got the carnivores. It usually ends at level 4 or 5 containing the apex predators.

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3
Q

Metabolism got two central parts, katabolism and anabolism. Define them

A

Katabolism is change brought breaking down things, like food breaking down in our stomach.
Anabolism is change brought through building up things, like the same food which is broken down gets absorbed and used as energy.

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4
Q

What are an energy carrier?

A

An energy carrier is a material we can directly use as energy. Like ATP, NADH and FADH. NADH and FADH is key for respiration.

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5
Q

Define an enzyme

A

An enzyme is a protein that oversee and interfere with reactions and speed up the process. They are also called biological catalysts, a catalyst is something that affects the reaction speed without self getting changed and used up by the process.

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6
Q

Which are some ways that reaction speed be altered?

A
  1. Increase concentration of the reactants reacting. This way increases the possibility of them interacting and reacting.
  2. Increasing temperature. Increased temperature means increased movement in the reactants.
  3. Adding a catalyst.
  4. Pressure. More pressure means that the reactants are forced more closely together.
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7
Q

What is an exotherm reaction?

A

A exotherm reaction is a reaction where energy gets distributed to the environment.

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8
Q

What is a endothermic reaction?

A

A endothermic reaction is a reaction that takes energy from the environment.

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9
Q

The chemical reaction:

Reactant + reactant = product is the standard equation. how does it look when an enzyme is involved?

A
Enzyme + substrate (reactant) -> enzyme-substrate complex -> 
product + enzyme
F.ex.
Sucrose + water + sucrase (ase) ->
Enzyme-substrate complex ->
Glucose + fructose + sucrase
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10
Q

Why does enzymes bring down activation energy and what is it?

A

Activation energy is the required energy for a reaction to happen.

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11
Q

Why does enzymes decrease activation energy for chemical reactions?

A

Emilie Fischer said that substrate and enzyme fits like a key in a lock.
Meaning
The enzymes are specially made for specific substrates. This involves in shape, and substances. Like carrying oxygen you need a haemoglobin molecule. They have a specific seat for the specific molecule, there can be multiple seats, when it comes to interaction these active seats can bring two substrates closer together and meet, and then the enzyme can also enhance that connection.

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12
Q

Name three factors in the environment that has substantial influence over the activity of enzymes

A

Enzymes like species of the earth have a wide area of specialities. Some thrive in the cold and some in the warm. Some in the sour and some in the bases. If there’s more of them or more of it.

  1. pH-levels. Enzymes are very specific and therefore also is very sensitive to pH. The level where the enzyme is most suited to be and do it’s job is the enzymes pH-optimum.
  2. Temperature. Like pH-optimum there is also a temperature-optimum. If the degree is too warm or too cold for the enzyme/s then they will denature.
  3. The amount of substrate and enzyme. If either is added the faster the speed. Except if it’s too much of the substrate, dounk.
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13
Q

What are a denatured protein?

A

A denatured protein is a protein that has been exposed to energy at such a high level it’s original structure has been destroyed, usually resulting in loss of tertiary structure.
In a few cases it can obtain its former self, this is called denatured protein.

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14
Q

How do you name a protein?

A

All proteins gets -ase at the end.

Proteins gets named firstly after the substrate they have, then after the reaction they catalyst.

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15
Q

Define some main enzyme groups.

A
  1. Oxireductase. Oxidises or reduce organic substances. Some of these enzymes are de most important one in cell respiration.
  2. Transferases. Group of enzymes that transport one substance to another. A big part of the transferases is the kinases, these transport phosphate groups, like heksokinase which is important in glycolyses.
  3. hydrolases. Enzyme that catalyses the hydrolysis of chemical bonds in bio molecules. Making big molecules to smaller using water. Like the peptidases, lipases, and glykoxidases.
  4. Lyase. Catalyses the breakdown of covalent bonds. A key enzyme group here is the decarboxylacidases, these remove CO2 from carboxylacid groups, like pyrovatdehydrogenases in cell respiration.
  5. Isomeraser. These catalyst changes in a molecule that makes it into its isomer shape.
  6. Ligases. These catalyse production of covalent bonds. It takes energy in form of ATP. An important enzyme is DNA-ligase that glues the Okazaki fragments together.
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16
Q

What are cofactors and coenzymes?

A

Cofactors and coenzymes are substances that works together with enzymes.
An enzyme is in simple terms a protein that mediate a process, directly or indirectly. Cofactors and coenzymes are substances that help the enzymes do it’s job, better.

17
Q

What are some typical cofactors?

A

Typical cofactors are the metal ions.

Iron(Fe+2/Fe+3), magnesium (Mg2+), manganese (Mn2+), Copper (Cu2+) and sink (Zn2+).

18
Q

What are cofactors important in?

A

Redux reactions and oxidations reactions. This is because they are important in electron transfer.

19
Q

What are prosthetic groups in cofactors?

A

Prosthetic groups in cofactors are names given to cofactors that are tightly bound to the enzyme and remains that way under the entire reaction.
An example is the hem group in haemoglobin. Which is an iron ring that can attach itself to oxygens.

20
Q

What are coenzymes?

A

Coenzymes are organic substances that are necessary for one or more enzyme to function.
the coenzymes on the contrary to prosthetic groups loosely bound and also gets changed under the reaction.
It’s main job is to add or derive chemical groups or add to electron transport.
A lot of the coenzymes are made from vitamins, or is just whole vitamins.
After the reaction they will be remade and take part in the same reaction.
For example. Biotin which carry COO- coenzyme. Or coenzyme A, which transport pyruvate. Another coenzymes are NAD and FAD which transport electrons.

In human diet all the water soluble vitamins are forerunners for coenzymes.

21
Q

What two form of enzyme inhibitors do we have?

A

Competitive inhibitors.
And
Non-competitive inhibitors.

22
Q

What are competitive inhibitors?

A

Competitive inhibitors are substances that compete with the substances for the active seat/son the enzymes.
If an competitive inhibitor takes an active seats then the substance are unable to interact with the enzyme and the reaction won’t happen. This process is often reversible, meaning that the competitive inhibitor detaches itself from the active seat after some time.

23
Q

What are non-competitive inhibitors?

A

Non-competitive inhibitors are substances that attaches itself on other parts of the enzyme than the active seat, therefore meaning it doesn’t compete directly with the substances.
But, the non-competitive inhibitors does affect the active seat and it’s ability to attach the substrate. Meaning it doesn’t sit as well as it’s supposed to be.

24
Q

What are irreversible inhibitors?

A

Irreversible inhibitors are substances that will make the enzyme permanent unable to function. These types of substances are dangerous to the cell because of the importance of enzymes. They have a job for a reason and when they can’t complete that job something is bound to happen.

25
Q

Name an irreversible inhibitor

A

The nerve gasses. They are constant inhibitor for the enzyme acetylcolinesterases, these enzymes work in the nervous system and maintain normal functions.

26
Q

What are allosteric enzymes?

A

Allosteric enzymes are enzymes that the cell can change its shape to determine if it’s active or not.
You can say it’s state inhibits or not.
An allosteric enzyme have different seats along with the active seat. For example, it’s has two or more regulating units for it to modify.
1. The first regulating unit contains an inhibiting seat. When it’s inactive it’s filled with an allosteric inhibitor.
2. The second regulating unit contains an allosteric activating unit, when the enzyme is active the seat is taken by a allosteric activator

27
Q

Why are allosteric enzymes really practical?

A

Allosteric enzymes are really practical because if the enzyme doesn’t get used, the cell doesn’t have to break it down. Instead it can make it inactive through regulating units

28
Q

What is an allosteric activator and inhibitor?

A

An allosteric activator is a substance that activate the allosteric enzyme so it can take on the substrate.

An allosteric inhibitor is a substance that can inhibit the activity of the allosteric enzyme when it’s put on the inhibiting seat.

So. 
Inhibiting seat = allosteric inhibitor
Activating seat = allosteric activator 
Active seat = substrate 
The two allosteric seats each sits on a regulating unit.
29
Q

Since most of the important reactions are chain reactions, it’s important that the cell can stop or start it following the need of it. How does it do this?

A

The cell does this through a mechanism called feedback.
Feedback in simple terms means that the end product in a chain reaction affects the first or one of the first enzyme that gets this process started