Biochemistry: Enzymes and Biological Catalysts Flashcards

1
Q

what do enzymes effect and not affect

A
  • speed of the reaction

- equilibrium

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2
Q

in what conditions do enzymes work

A
  • body temp
  • near neutral pH
  • in aq solutions
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3
Q

how are enzymes specific

A

recognise a limited range of substrates

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4
Q

how are enzymes potent

A

convert many substrates to products quickly

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5
Q

what is the activation energy and why is it present

A
  • energy required for enzymes to work

- stops reactions occurring in normal conditions

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6
Q

transition state

A

reaction intermediate substance that contains the most free energy

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7
Q

what do enzymes bind to and what do they do

A
  • transition state

- lower activation energy

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8
Q

describe glycogen storage disease

A

enzyme deficiency resulting in failure of glycogen to enter its phosphorylated state

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9
Q

what are co-factors

A

metal ions

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10
Q

what are co-enzymes

A

organic molecules

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11
Q

what do co-factors form in the enzymes

A

a metallo protein - metal co-ordination centre

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12
Q

how do co-enzymes associate with enzymes and what happens when they bind

A
  • transiently

- change or restructure themselves

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13
Q

prosthetic group

A

tightly bound co-enzymes

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14
Q

apoenzyme

A

enzyme without a co-factor

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15
Q

holoenzyme

A

enzyme with a co-factor

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16
Q

what type of reaction are co-enzymes involved in and what do they do

A
  • redox reactions

- stabilise transition states

17
Q

what are many co-enzymes derived from

18
Q

what do symptoms of vitamin deficiencies reflect and what are the classes of deficiencies

A
  • the loss of enzyme activity

- functional or dietary

19
Q

describe substrate binding to enzyme

A
  • substrate binds to an active site

- this contains the amino acids essential for catalysis and specific interactions

20
Q

what is the lock and key model

A

the substrate and active site are complementary shapes

21
Q

what is the induced fit model

A

substrate binding induces a conformational change leading to complementary fit

22
Q

what other factors can influence enzyme activity

A

temperature and pH

23
Q

describe the active site of pancreatic serine proteases

A

contain reactive serine residues that catalyse the hydrolysis of peptides at specific sites

24
Q

isoenzyme

A

isoforms of enzymes, enzymes that catalyse the same reaction but have different properties and structure

25
why can isoenzymes catalyse the same reaction but have a different make-up
- synthesised at different stages of development | - present in different tissues/cellular locations
26
what is the clinical use for isoezymes
diagnostic tests
27
how is lactate dehydrogenase used as a diagnostic test
it requires hypoxia sensitive transcription factors so a decreased presence in blood indicates tissue hypoxia
28
how is creatine kinase used as a diagnostic test
- dimeric protein that binds to muscle sarcomeres - M form (muscles) and B form (brain) - heart produces both - M form in blood suggests MI, B form in blood suggests stroke
29
how does phosphorylation regulate enzyme activity
phosphorylation is a reversible covalent modification that converts enzymes to and in/active form
30
what carries out phosphorylation reactions
protein kinases
31
describe a phosphorylation reaction
fast, reversible | side groups form phosphate esters
32
how do irreversible covalent modification regulate enzyme activity
results in an active form of enzyme irreversibly
33
zymogen
inactive precursor of an enzyme
34
what do zymogens do
irreversible transform into active enzymes via covalent bond cleavage
35
give examples of zymogens
- tripsinogen to trypsin via enteropeptidase - chymotrypsinogen to chymotrypsin via trypsin - pancreatic enzymes, blood clotting factors, clot-dissolving enzymes