ENZYMES Flashcards

1
Q

what are enzymes?

A

biological catalyst, usually a protein, synthesized by living organisms that speed up rate of reaction w/o being used up or permanently altered at the end of the reaction

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2
Q

what is a catalyst?

A

substance that speeds up the rate of reaction by lowering the amount of energy needed for the reaction to occur
- reactant binds to a catalyst and change into products which then dissociate from the catalyst

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3
Q

what is the importance of enzymes?

A

w/o it, biochemical reactions in cells will either not occur at all or occur at a rate that is too slow for life to be sustained

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4
Q

what are the 7 characteristics of enzymes?

A
  • substrate specifity
  • regulated enzyme activity
  • speeds up reaction
  • temperature
  • pH
  • salt concentration
  • cofactor
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5
Q

what is substrate specifity?

A

enzymes are highly specific for the reactants or substrates that they act on and the products that they form
- properties and spatial arrangement of the amino acid residues forming the active site of an enzymes will determine which molecules can bind and serve as substrates for that enzyme

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6
Q

what is regulated enzyme activity?

A

enzyme is regulated and the can be enhance or suppressed by the very same molecules whose reaction they catalyse

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7
Q

what is speeding up of the reaction?

A

speeds up the rate of reaction w/o being used up/permanently altered

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8
Q

what affects enzymes?

A

temp, pH, salt conc.

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9
Q

what is cofactor?

A

some enzymes require other organic compound molecules, coenzymes to be bound to them before they can catalyse any reactions

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10
Q

what is the structure of enzymes?

A

usually proteins w complex 3D shapes or conformation in which each enzymes have a groove/pocket called an active site to which reactant bind to
- structure of an enzyme determines its specifity, hence determining its functions which determines the type of reaction that the enzyme catalyse

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11
Q

what is binding and active site?

A

binding site : bind and orient substrates

catalytic site : reduce chemical activation energy

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12
Q

what are the two model of enzymes actions?

A

1 ) Lock and key model
- two shapes are considered as rigid and fixed and perfectly complement each other when brought tgt in the right alignment
2 ) Induced fit model
- binding of substrate to the active site induces a conformational change in the enzyme to fit the shape of an enzymes

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13
Q

what bonds hold the substrates and enzymes together?

A

hydrogen bonds and reversible covalent bonds, van der waals, hydrophobic and electrostatic interactions

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14
Q

what are the 6 classes of enzymes?

A

OXIDOREDUCTASES : catalyse redox reactions
TRANSFERASE : catalyse group transfer reactions which requires the presence of co-enzymes
HYDROLASES : catalyse hydrolysis ; water serving as the receptor of the group transfer
LYASES : catalyse lysis of a substance, generating a double bond
ISOMERASES : catalyse structural change within a single molecule
LIGASES : catalyse ligation ; joining of two substrates which require the input of the c.p.e of ATP

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15
Q

what are enzyme assays?

A

measure the rate of conversion of substrate to product, under conditions of cofactos, pH and temp at which the enzyme is optimally active
- rate of appearance of product/rate of disappearance of substrates is measured in the change in absorbance using a spectrophotometer or by linking enzymes to another enzymes-catalysed reaction that does involve a change in absorbance

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16
Q

what is enzyme kinetics?

A

study of rates of enzyme-catalysed reactions

17
Q

how does substrate concentration\ affect enzyme activity?

A
  • at low [S] , 2x [S] will lead to 2x Vo

at high [S] , enzyme becomes saturated and there is no further increase in Vo

18
Q

how does enzyme concentration affect enzyme activity?

A

when enzyme concentration is saturating, a 2x of the enzyme conc. will lead to a 2x of Vo

19
Q

how does temperature affect enzyme activity?

A

higher temperature, higher thermal energy of the substrate molecules hence, increasing the proportion of molecules with sufficient energy to overcome the activation energy barrier, hence increasing the rate of reaction
- each enzyme has its own optimal temp in which it works best at

20
Q

how does pH affect enzyme activity?

A

each enzymes has an optimum pH at which the rate of the reaction that it catalyses is a max/fastest speed

  • small deviations in pH from the optimum lead to a decrease in enzyme activity due to changes in the ionisation of groups at the active site of the enzyme
  • larger deviation in pH will lead to the denaturation of the enzyme protein due to interference with many weak non-covalent bonds
21
Q

how does salt concentration affect enzyme activity?

A

too high of a salt conc. will interfere with the 3D structure of the enzyme thereby destroying the enzyme activity

22
Q

how does cofactors affect enzyme activity?

A

some enzymes require the presence of cofactors to help weaken the bonds of the substrate, allowing it to react with the enzymes
- Holoenzymes : catalytically active form of the enzyme with its cofactor
apoenzyme : protein portion of an enzymes that has no activity

23
Q

what are isoenzymes?

A

diff. forms of an enzyme which catalyse the same reaction but exhibit different physical or kinetic properties

24
Q

what are cofactors?

A

can be essential ions, coenzymes and coenzyme classification

25
Q

what are essential ions?

A

1 ) metal activated enzymes
- have an absolute requirement for the added metal ion or are simulated by the addition of metal ions
2 ) Metalloenzymes
- contain firmly bound metal ions at their active site ; usually transition metals

26
Q

what are coenzymes?

A

1 ) cosubstrates
- cosubstrate is altered in the course of the reaction and dissociates from the active site and its orginal structure will be regenerated in a subsequent reaction catalysed by another enzyme ; cosubstrate is recycled repeatedly
2 ) Prosthetic group
- remains bound to the enzyme during the course of the reaction

27
Q

what are coenzymes classification?

A

1 ) Metabolite coenzymes
- synthesized from common metabolites which includes a no. of ATP
2 ) Vitamin-derived coenzymes
- vitamins required for the synthesis of coenzymes must be obtained as nutrients usually in small amounts
- mammals and other animals rely on other organism to supply these nutrients such as plants and microorganisms