Enzymes Lecture Flashcards
What is an abzyme?
An antibody with catalytic activity
What is isoenzyme
Two or more enzymes with a different amino acid structure that catalyse the same reaction
Allosteric enzyme activator/inhibitor
A molecule that alters the activity of an enzyme by inducing conformational change. Often more than one active site
Chymotrypsin
Catalysts hydrolysis of peptide bonds
Carbonic anhydrase
Catalyses hydration of CO2 from tissues to the blood system to alveolar air
Papain
Generalist enzyme used in meat tenderising industry
Trypsin
Peptide bond cleavage, only on the carboxyl side of lysine and arginine residues
Thrombin
Blood clotting, catalyses breaking of arginine/glycine bonds
Oxidoreductases
Oxidation-reduction reactions
Transferase
Transfer of functional groups
Hydrolases
Hydrolysis reactions
Lyases
Group elimination to form bonds
Isomerases
Isomerization reaction
Ligases
Bond formation coupled with ATP hydrolysis
Lysosomal enzymes
Damage bacterial cell walls by catalysis hydrolysis of residues in peptidoglycan
Post translational modification: phosphorylating
Kinases
Post-translational modification: removing phosphate
Phosphatases
What is a coenzyme
A non-protein compound that is necessary for the functioning of an enzyme
Two examples of inorganic co-factors
Mg2+ DNA polymerase
Zn2+ metalloproteases
Examples of organic co-factors
NAD+
Biotin
Heme
Vitamins
What is phosphorylation of proteins?
Key to cell signalling, mediated by kinases, brings about change in conformation of active site.