Enzymes Lecture Flashcards

1
Q

What is an abzyme?

A

An antibody with catalytic activity

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2
Q

What is isoenzyme

A

Two or more enzymes with a different amino acid structure that catalyse the same reaction

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3
Q

Allosteric enzyme activator/inhibitor

A

A molecule that alters the activity of an enzyme by inducing conformational change. Often more than one active site

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4
Q

Chymotrypsin

A

Catalysts hydrolysis of peptide bonds

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5
Q

Carbonic anhydrase

A

Catalyses hydration of CO2 from tissues to the blood system to alveolar air

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6
Q

Papain

A

Generalist enzyme used in meat tenderising industry

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7
Q

Trypsin

A

Peptide bond cleavage, only on the carboxyl side of lysine and arginine residues

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8
Q

Thrombin

A

Blood clotting, catalyses breaking of arginine/glycine bonds

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9
Q

Oxidoreductases

A

Oxidation-reduction reactions

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10
Q

Transferase

A

Transfer of functional groups

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11
Q

Hydrolases

A

Hydrolysis reactions

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12
Q

Lyases

A

Group elimination to form bonds

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13
Q

Isomerases

A

Isomerization reaction

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14
Q

Ligases

A

Bond formation coupled with ATP hydrolysis

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15
Q

Lysosomal enzymes

A

Damage bacterial cell walls by catalysis hydrolysis of residues in peptidoglycan

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16
Q

Post translational modification: phosphorylating

A

Kinases

17
Q

Post-translational modification: removing phosphate

A

Phosphatases

18
Q

What is a coenzyme

A

A non-protein compound that is necessary for the functioning of an enzyme

19
Q

Two examples of inorganic co-factors

A

Mg2+ DNA polymerase

Zn2+ metalloproteases

20
Q

Examples of organic co-factors

A

NAD+
Biotin
Heme
Vitamins

21
Q

What is phosphorylation of proteins?

A

Key to cell signalling, mediated by kinases, brings about change in conformation of active site.