enzymes as Biological Catalysts Flashcards

1
Q

does an enzyme affect the equilibrium of a reaction?

A

no, just speeds up the rate at which the reaction reaches equilibrium

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2
Q

enzymes are mostly proteins, what is the exception?

A

some types of RNA - eg. ribozymes

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3
Q

how potent and specific are enzymes, generally?

A

each enzyme only has a limited no. of substrates, therefore some can distinguish stereoisomers
V. potent - can convert many substrate molecules into product per second

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4
Q

how do enzymes speed up reactions, generally?

A

decrease activation energy by providing alternative pathways, stabilise transition state

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5
Q

what is the transition state?

A

reaction intermediate species which has the greatest free energy (basically the point at which the reaction tips over the edge)

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6
Q

what causes glycogen storage disease?

A

enzyme deficiency that results in failure of glycogen to enter transition “phosphorylated” state meaning glycogen cant be broken down resulting in low glucose

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7
Q

what is the most common glycogen storage disease and how does it present?

A

Von Gierke’s Disease

hypoglycaemia, hepatomegaly, ulcers, infections, bowel problems

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8
Q

how is von gierke’s disease treated?

A

slow release glucose meal

feed little and often

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9
Q

what are the 2 types of cofactor?

A
metal ions (cofactors)
organic molecules (coenzymes)
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10
Q

what do cofactors (metal ions) do?

A

involved in redox reactions and stabilise transition states

form a metal co-ordination centre in the enzyme (metalloprotein

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11
Q

what do coenzymes (organic molecules) do?

A

many involved in redox reactions or group transfer processes (ATP, CoA)
most associate transiently with the enzyme, chaging charge or structure

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12
Q

what is a prosthetic group?

A

tightly bound coenzymes (eg. haem in haemoglobin)

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13
Q

give some examples of cofactors and coenzymes

A

cofactors - zinc, iron, copper

coenzymes - many derived from vitamins (i.e - vitamin deficiencies reflect loss of enzyme activity)

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14
Q

name a common coenzyme for redox reactions and describe its action

A

Nicotinamide adenine dinucleotide (NAD+)
may donate or receive electrons during enzyme catalysis
easily regenerated

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15
Q

give an example of an enzyme that works via induced fit

A

hexokinase

changes shape as glucose binds to active site

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16
Q

name the 3 pancreatic serine proteases and their reactive sites

A

chymotrypsin - hydrophobic pocket binds aromatic amino acids
trypsin - _ve Asp binds +ve Lys or Arg
elastase - active site partially blocked, only amino acids with small or no side chains can bind

17
Q

give an example of different isozymes of an enzyme

A

lactate dehydrogenase
H (heart) form = promotes aerobic environment
M (Muscle) form promotes anaerobic environment

18
Q

what is a clinical use of isozymes? give an example

A

relative amounts of an isozyme in a specific tissue are useful for diagnostic purposes
E.g - creatine kinase (CK)
- M type in skeletal muscle
- B form in Brain
Heart produces both types (MB)
appearance of brain type in blood = stroke or tumour
appearance of heart type = heart attack

19
Q

how are enzymes regulated by phosphorylation?

A

reversible covalent modification
Via protein kinases
can convert enzyme to active or inactive form

20
Q

what is a zymogen?

A

inactive precursor of an enzyme

21
Q

how are zymogens activated, give examples

A

irreversible cleavage of a covalent bond
E.g - trypsinogen and chymotrypsinogen formed in pancreas and cleaved by enteropeptidase in small intestine to give active chymotrypsin

22
Q

give some examples of enzymes that are regulated by partial proteolysis

A

digestive enzymes (trypsin etc)
Blood coagulation enzymes (VII, IX, X, XI, XIII, thrombin etc)
Blood clot dissolving enzymes (plasminogen etc)
Programmed development enzymes (chitin synthetase, cocoonase, collagenase)