reduces necessary free energy (delta
G) need to overcome the activation
energy
do NOT alter final
equilibrium b/w reactants
and products
proteins
Dependent on many weak bonds e.g. hydrogen bonds, electrostatic
salt links and hydrophobic interactions
Makes enzymes sensitive to changes
in their environment
Inactive enzyme
Denatured enzyme state
e.g. by eating the protein, giving rise to a disorganised or tangled structure in which
the enzyme no longer has any catalytic activity
temperature
Between 20C, 30C and 40C for enzymes
found in the body, you will usually speed up
the reaction
Up to 50C and beyond, denaturing of the protein will occur,
similarly going to far below 20C will also reduce reaction
velocity
Enzyme catalysis
Enzymes contain an active site
substrate binds to the enzyme at the
active site producing an
enzyme-substrate complex
enzyme is then disregarded at the final product
is revealed
Stickase metaphor
illustrates that enzymes should be complementary to the
substrates transition phase rather than the substrate itself to
bring about the activation of the reaction > product
Substrate specificity
catalyse only one type of reaction
and will act only on a few related
molecules ('Group...')
few are so specific that they will
act only on a certain enzyme even
to the point will it will only act on
one stereoisomer
presence of a groove or cleft of defined shape
called the active site into which only the
substrate of the correct shape and charge can
fit
Relevance?
multiple enzymes within the same cellular
compartment can co-exist without interfering with e/o
allows for multiple metabolic pathways w/i cells
Systematic classification scheme of 6
main classes
Annotations:
Six classes are divided into subgroups according to their substrate or source i.e. the type of reaction they catalyse
Each enzyme IDed by individual 4 digit number
I.U.B. Commission on Enzymes - established the systematic classification on enzymes
Catalase 4 digit classification code - E.C. 1.11.1.6.