Enzymes and Vitamins Flashcards
What is an Enzyme?
protein that acts as a catalyst for a biochemical reaction.
These are the two enzyme structures (describe their differences)
Simple (composed only of protein) and Conjugated Enzyme (has a
nonprotein part in addition to a
protein part)
Apoenzyme + Cofactor = ?
Holoenzyme
protein part of conjugated enzyme
apoenzyme
NON protein part of conjugated enzyme
cofactor
what is the function of a catalysts?
speeds up chemical reaction and does not undergo any changes at the end
suffix of an enzyme
-ase
an enzymes’ prefix is often noted by its _____
type of reaction that it catalyzes
a catalyze oxidation-reduction that adds or removes an oxygen or hydrogen
Oxidoreductases
subclass of Oxidoreductases and their functions
Oxidases - oxidation of a substrate
Reductases - reduction of a substrate
Dehydrogenases - removal of two H atoms from a substrate
it catalyze transfer of one group to another
transferases
subclass of transferases and their functions between substrates
transaminase - Transfer of amino group between substrates
kinase - Transfer of a phosphate group between substrates
catalyze the hydrolysis of substrate
breaking of bonds and addition of water
hydrolases
hydrolysis in ester linkages in LIPIDS
lipases
hydrolysis of AMIDE LINKAGES in proteins
proteases
hydrolysis of GLYCOSIDIC BONDS of carbohydrates
carbohydrases
hydrolysis of SUGAR-PHOSTPHATE ester bond in carbohydrates
nucleases
hydrolysis of PHOSTPHATE ester bond
phosphatases
“lein” word means?
to break
it catalyze the addion of hydrogen oxiden or carbon dioxide to a double bond/reverse rection in which a molecule is eliminated to leave a double bond
“to break”
lyases
the 4 subclass of lyases
dehydratases, decarboxylases, deaminases, hydratases
addition of H2O from a substrate
hydratases
removel of NH3 from a substrate
deaminases
removal of H2O from a substrate
dehydratases
removel of CO2 from a substrate
decarboxylases
catalyze the arrangemnt of atoms (isomerization) of a substrate in reactions that have 1 sub but 1 product
isomerases
2 subclass of isomerases
racemases, mutase
catalyze the bonding together of two substrate mol
ligases
formation of two substrate bonds with the help of ATP
synthetase
formation of new bond from substrate and CO2 with ATP
carboxylase
conversion of d-isomer to l-isomer or vice versa
racemases
transfer of one functional group from one place to another same molecule
mutase
enzyme model in which substrate and enzyme has the same shape
lock and key model
enzyme model in which enzyme is flexible to match the shape of the substrate
induced fit model
what is absolute specificity of enzyme?
catalyze only 1 reaction
linkage specificity ___
enzyme only act on a particular type of bond
streochemical specificity
only act on streoisomers
group specificity
only act on particular functional group
4 types of enzyme specificity
maximum number of molecules that one enzyme can accomodate per unit time
turnover number
pepsin ____ trypsin ___
acidic and basic
it blocks the active site so that no substrate can enter
competitive inhibitor
a substrate that only lies on another area of enzyme ( or allosteric site)
incompetitive inhibitor
an enzyme that has another site than that of an active site
allosteric enzyme
binding of molecule to the other site that affects the binding of a molecule at another site
allosteric control
+/- allosteric regulator difference
the inhibitor can leave, restoring the enzyme to its
uninhibited level of activity
reversible inhibition
the inhibitor remains permanently bound and the
enzyme is permanently inhibited
irreversible inhibition
