Enzymes Flashcards

1
Q

What are enzymes?

A

Protein catalysts that speed up reactions

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2
Q

What are the benefits of enzymes in reactions?

A
  • more specific reactions (less side products)
  • milder reaction conditions
  • higher reaction rates (efficient)
  • better regulated biological pathways
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3
Q

What is a lock and key fit?

A

How enzymes bind to specific substrates to function (like a lock and a key)

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4
Q

What are cofactors?

A

Factors that help enzymes function

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5
Q

What is another name for organic cofactors?

A

Coenzymes

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6
Q

When things (like cofactors) bind to the inactive site they interact with whichever _____ binds to the ____ site

A

substrate/active

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7
Q

When a cofactor is bound to a protein is is called a _____, when it is with a cofactor the protein gets the prefix ____- and when it is without it gets the prefix ____-

A

prosthetic group/holo/apo

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8
Q

What are the six classifications of enzymes?

A

Oxidoreductases, transferases, hydrolases, lysases, isomerases, and ligases

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9
Q

What are oxidoreductases?

A

Enzymes that catalyze electron transfer

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10
Q

What are transferases?

A

Enzymes that catalyze the transfer of a group of atoms

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11
Q

What are hydrolases?

A

Enzymes that catalyze hydrolysis

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12
Q

What are lyases?

A

Enzymes that catalyze elimination reactions, usually resulting in a double bond or ring

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13
Q

What are isomerases?

A

Enzymes that catalyze the formation of isomers

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14
Q

What are ligases?

A

Enzymes that catalyze bond formation via condensation reactions, usually coupled with a hydrolysis reaction

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15
Q

How do enzymes speed up reactions?

A

By lowering activation energy

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16
Q

How do enzymes lower activation energy?

A

By organizing reactive groups into close proximity and proper orientation

17
Q

Catalytic mechanisms: ____-____ (gives and takes protons), _____ (changes reaction pathways), and ____ ___ (used REDOX cofactors and pKa shifters)

A

acid/base/covalent/metal ion

18
Q

What is the mechanism of chymotrypsin?

A

Chymotrypsin is a protease, it cleaved the carbonyl side of certain peptide bonds by acid-base catalysis and covalent catalysis
This happens in two main steps: acylation (when -OH binds to the substrate) and deacylation (using a water molecule)