Exam 1 | Chp. 2 & 3 Flashcards
Light, Spectrophotometry, Electrochemistry, Enzymes, Chromatography, Electrophoresis, & Immunoassays (46 cards)
Apoenzyme
protein core without cofactor
cofactor
non-protein that activates complex
holoenzyme
apoenzyme + cofactor(s)
Enzymes do not alter
chemical bonds
Enzymes allow
changes to occur with less energy expended
Chemical properties of an active site determine 2 things
- Specificity of an enzyme for its substrate
- The reaction it catalyzes
Absolute specificity
enz catalyzes only one rxn
Group specificity
enz only acts on molecules w/ specific functional groups
Linkage specificity
enz acts on particular types of chemical bonds regardless of mol structure
Stereochemical specificity
enz only acts on a particular isomer
3 types of cofactors
- Coenzymes
- Prosthetic Groups
- Metal ion activators
Coenzyme is a non-protein organic substance that
loosely attached to apoenzyme, related to vitamins
Prosthetic Group is a non-protein organic substance that
firmly attached to apoenzyme, ex is NAD, NADP
Metal Ion activators
may be an integral part or loosely bound to apoenzyme
Oxidoreductases catalyze
redox rxns
Transferases catalyze
transfer of functional group
Hydrolases catalyze
hydrolysis rxns
Lyases catalyze
removal of chemical groups
Isomerases catalyze
conversion of bonding patterns
Ligases catalyze
coupling of molecules with the hydrolysis of ATP bonds
Isoenzymes
different multimeric forms of an enzyme
Energy required for a substrate to be activated is provided by
the free energy of binding S to E
Enzyme substrate complex breaks down to give these two things
rxn products (P) and free enzyme (E)
A rxn can be forced to proceed in only one direction by
using a secondary rxn to remove product from availability