ENZYMES: structure Flashcards

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1
Q

what is the general shape/material of enzymes?

A

• Almost always soluble, globular proteins (although there are a small number of RNA enzymes)

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2
Q

can enzymes have one or more pp chains?

A

yes - most are oligomers, some are monomeric

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3
Q

deifne: monomeric enzyme

A

single pp chain with one binding site, eg. ribonuclease

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4
Q

define: oligomers

A

atleast two pp chains (same or different), with multiple binding sites

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5
Q

All enzymes have an__

A

active site?

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6
Q

how is the active site formed?

A

by the folding of pp chains to form a small region with a unique specific 3D shape. This region is small, made of about 3-12 amino acids

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7
Q

what happens when the active site is altered?

A

it may not be complementary to the substrate and its functionality will be permanently/temporarily lost/reduced.

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8
Q

describe the bonds between the enzyme and substrate.

A

stabilise the enzyme-substrate complex. can be hydrogen/ionic, or covalent

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9
Q

3 types of specifity?

A

absolute/substrate, bond, group specifitty

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10
Q

define: absolute/substrate specificity

A

an enzyme can act on one substrate only (lactase can only hydrolyse lactose to form galactose and glucose)

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11
Q

define: bond specificity

A

enzyme can act on only one kind of bond (peptidase can only act on peptide bonds between 2 amino acids)

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12
Q

define: group specificity

A

enzyme can only act on molecules with particular functional group(s) surrounding a bond (trypsin can only act on bonds adjacent to amino acids with basic side chains – lysine and arginine)

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