catalytic strategies Flashcards

1
Q

what is an acid-base catalysis

A

An enzyme that accepts H + from hydronium and transfers it to an amino group of the substrate.
the result is an increase in the rate of release of the product. T

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2
Q

what does carbonic anhydrase use?

A

acid-base catalysis
catalysis by approximation
metal ion catalysis

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3
Q

what does serine proteases use?

A

acid-base catalysis
catalysis by approximation
covalent catalysis

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4
Q

what does serine proteases contain?

A

a serine residue in their active site

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5
Q

what does the catalytic triad of serine proteases contains:

A

serine, histidine and aspartic acid residues

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6
Q

What metabolic type of reaction involves the addition of a functional group across a double bond or the removal of a functional group to form a double bond?

A

lyase

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7
Q

what are the features of equilibrium of this reaction?
CO2 + H2O ⇌ H2CO3

A
  • An increase in the concentration of CO 2 will result in a decrease of pH.
  • The H2CO3 dissociates to H+ and bicarbonate ion, HCO3–.
  • The majority of CO2 is transported to the lungs in the form of HCO3–.
  • This reaction is catalysed by carbonic anhydrase.
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8
Q

What is not an internationally accepted class of enzymes?

A

polymerase

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9
Q

What metabolic type of reaction involves the cleavage of bonds by the addition of water?

A

hydrolysis

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10
Q

What is the most predominant form for the transfer of carbon dioxide in the blood?

A

HCO3-

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11
Q

what enzyme does carbonic anhydrase contains in its active site.

A

Zn2+ ion

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12
Q

what does carbonic anhydrase do?

A

decreases the pKa of water

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