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anatomy > BIOCHEM - Enzyme 2 > Flashcards

BIOCHEM - Enzyme 2 Flashcards

1
Q

classes of enzymes:

A

Hydrolase
Isomerase
Ligase or Polymerase
Lyase
Oxidoreductase
Transferase

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2
Q

TRC: Hydrolysis (Catabolic)

A

Hydrolase

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3
Q

example of Hydrolase

A

Lipase - breaks down lipid molecules

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4
Q

TRC: rearrangement of atoms within a molecule (neither catabolic or anabolic)

A

Isomerase

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5
Q

example of Isomerase

A

Phosphoglucoisomerase - converts glucose 6 phosphate into fructose 6-phosphate during glycolysis

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6
Q

TRC: joining 2 or more molecule together (anabolic)

A

Ligase or polymerase

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7
Q

example of Ligase or polymerase:

A

Acetyl-CoA synthase - combines acetate and coenzyme A to form acetyl-CoA for the Krebs cycle

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8
Q

TRC: splitting a chemical into smaller part without using water (catabolic)

A

Lyase

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9
Q

example of Lyase:

A

Fructose 1, 6-bisphosphate aldolase - splits fructose 1,6-bisphosphate into G3P and DHAP

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10
Q

TRC: transfer of electrons or hydrogen atoms from one molecule to another

A

Oxidoreductase

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11
Q

example of oxidoreductase:

A

Lactic acid dehydrogenase - oxidizes lactic acid to form pyruvic acid during fermentation

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12
Q

TRC: Moving a functional group from one molecule to another (may be anabolic)

A

Transferase

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13
Q

example of transferase

A

Hexokinase - transfer phosphate from ATP to glucose in the first step of glycolysis

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14
Q

As the name implies, they catalyze redox reaction – transfer of electrons.

One molecule would lose an electron and another molecule would eventually gain an electron

A

Oxidoreductase

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15
Q

In organic chemistry, these are also
dehydrogenation reaction

A

Oxidoreductase

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16
Q

there is a subclass of oxidoreductase that is called ____________

malic dehydrogenase,
pyruvate dehydrogenase,
succinate dehydrogenase and
alcohol dehydrogenase

A

dehydrogenases

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17
Q

When we are talking about oxidoreductase, the usual coenzymes are

A

NAD
FAD or
NADP

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18
Q

Whenever we see an enzyme that bears the name dehydrogenase, try to look for the coenzyme right away.

There should be ______________ in that particular reaction.

A

NAD, FAD or NADP

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19
Q

These enzymes catalyze the transfer of functional groups such as methyl,
acetate and phosphate among other things.

A

Transferases

20
Q

There is a special class of transferases that are called ____________.

They transfer phosphate usually coming from ATP.

A

kinases

21
Q

One example of transferases is __________.

One of the very first reactions that ______
undergoes when it enters the cell is that it will be phosphorylated at C6.

Phosphate will be attached C6

A

glucose

22
Q

Phosphate was transferred from ATP to glucose. From ATP it became ADP.

The enzyme is called ___________.

A

hexokinase

23
Q

They catalyze hydrolytic reactions, adding water across C-C bonds.

These enzymes break bonds by adding water molecule

A

Hydrolyases

24
Q

Very similar to the enzyme hydrolases

They also break C-C bonds, C-O bonds, C-N bonds and other bonds.

Sometime they generate a ring or a
double bond.

They break bonds but do not incorporate
any water molecules.

A

Lyases

25
Q

This reaction is catalyzed by __________

The bond between the 2 Cs has been cleaved, making the carboxyl group in the form of CO2.

There is no water molecule involved making _________ a form of lyase

A

pyruvate decarboxylase

26
Q

cleave C-C, C-O, C-N, etc

generate C=C bond or ring

A

Lyase - Pyruvate decarboxylase

27
Q

Also called mutases.

They catalyze interconversion between isomers.

A

Isomerases

28
Q

are molecules that have the same structure but different configuration.

Example: fumarate and maleate

A

Isomers

29
Q

In naming the product, they both can be ___________.

One of them can be the product and the other the substrate or vice versa

A

interconverted

30
Q

(mutases) catalyze isomerization

ex: Maleate isomerase

A

Isomerases

31
Q

They catalyze condensation between 2 substrate with splitting of ATP

They form bonds between 2 molecules and there has to be source of energy, and the usual source of energy is ATP

A

Ligases

32
Q

example of ligases

A

pyruvate carboxylase

33
Q

__________ is formed by condensation of
bicarbonate and pyruvate.

A bond here has been formed and the source of energy is the splitting of ATP to ADP in Pi (inorganic phosphate)

A

oxaloacetate

34
Q

“to tie together”

A

ligate

35
Q

opposite of lyase

A

ligases

36
Q

HOW ARE ENZYMES
CONTROLLED/REGULATED?

A
  1. Anchoring enzymes in membranes
  2. Inactive precursors
  3. Allosteric regulation
  4. Covalent modification
  5. Regulation of enzyme synthesis
37
Q

The cell membrane is composed of 2 layers of phospholipid and inserted into them are integral proteins. Some of these integral
proteins are actually ________________.

A

enzymes

38
Q

When enzymes are inserted into
membranes, it allows them to interact efficiently with their substrate.

They are locked into that particular area; having nowhere else to go therefore they can act efficiently with their _________.

A

substrate

39
Q

Proteolytic enzymes are stored as ____________,

  • Once they have been secreted, they are usually cleaved to yield the active enzyme
A

zymogens

40
Q

example of Inactive precursors.

This is stored in the pancreas. Just before it is secreted, it is cleaved between arginine 15 (Arg 15) and isoleucine 16 (Ile 16) to yield active chymotrypsin.

A

Chymotrypsinogen

41
Q

In this example, we can see a pathway. The initial substrate A becomes B then becomes C and so on.

The final product is E. Each step is catalyzed by a respective enzyme like A becomes B catalyzed by enzyme a.

A

Allosteric regulation

42
Q

If there is excessive amount of the final product E, it can provide feedback inhibition to the initial enzyme a to slow down the reaction.

A

Feedback inhibition

43
Q

regulation are inhibitory in nature.

Sometimes they can activate an enzyme. This time, it is no longer called an allosteric inhibitor but a ______________.

A

positive modulator

44
Q

One of the functional groups in the enzyme will be attached to another functional group. In this case, phosphate was attached to serine, rendering the enzyme active.

This form of covalent modification is what is known as _____________.
The source of phosphate is usually ATP.

A

phosphorylation

45
Q

The most sophisticated way of controlling enzymes.

  • Genes are DNA which encode for proteins. Proteins are made through a process of transcription and translation of a particular
    gene.

So gene encodes proteins and enzymes are PROTEINS

A

Regulation of enzyme synthesis

46
Q
A

anatomy (15 decks)

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