W6 Enzyme Action Flashcards
what is the enzyme transtion state theory
enzymes reduce activation barrier for smaller transition state energy
what complex is formed when substrates bind to enzyme
ternary complex
what are ping pong enzyme reactions
when 1 or more products bind before all substrate bind
what are 4 methods of catalysis
by approximation
covalent
acid base
metal ion
what is covalent catalysis
- temp binding of subtrate by nucleophlic attack
- intermediate lowers activation energy
- regenerate enzymes break covalent bond
what are 3 examples of residues used for covalent catalysis
Lys
Asp
Cys
what is acid base catalysis
- nucleophilic or electrophilci attack by acid or base
- donate/accept of protons stabilize the transition state
which 2 acid/bases are used for catalysis
cystine
histidine
what are the 3 most common metal ion catalyst
Fe2+
Zn2+
Cu2+
how does phosphorylation regulate enzymes
adds 2 -ve charges and form 3+ H bonds for high energy transfer
what do zymogens do
cleavage for activation of enzyme
what is Ubiquitination of an enzyme
addition of ubiquitin to polypeptide
marks proteins for degradation
what is an eample of ubiquitin
p27
what do apoenzyme + cofactor make
holoenzyme
what are 2 common co subtrates
ATP
NAD
what are the 4 things that control amount of enzyme
transcription
translation
processing
stability
what are 3 regulatory enzymes
heokinase
phosphofructokinase
pryuvate kinase
what is activated for more Ca2+
CAMKs
what do Ca2+ do for enzymes
increase affinity by binding to subtrate
why is Compartmentalisation good for enzymes
allow simultaneous metabolic reactions and complexes
what are uncompetitive inhibitors
bind to the ES complex instead of active sites
what happens to Km when more comp inhibitors are added
increase Km
what does more comp inhibitors mean for V max
nothing
what does more non-comp do to V max
reduced