General Organic Biochemistry ACS final Questions & Answers
-Zymogens (proenzyme)- to free active form
-produce enzyme only when substrate is present-common
in bacteria
methods organisms use to -allosteric enzymes-activate/deactivate
regulate enzyme activity -feedback inhibition
-protein modification, usually phosphorylation, to reversibly
activate or deactivate enzyme
oxidation gain in oxygen, oxygen bonds, loss of H, loss of e
reduction loss of oxygen, oxygen bonds, gain H, gain e
adenosine triphosphate- (coenzyme) transports chemical
energy within cells for metabolism. This is not a redox
ATP
coenzyme. ATP is continuously cycling to ADP and back to
ATP
expressed as an inactive apo-enzyme and must be activated
by its prosthetic group 4' phosphopantetheine. This forms a
Acyl Carrier Protein phosphate ester bond with the -OH on a serine in the
apoenzyme. The SH group attached to the Acyl function be
transferred.
a coenzyme which is tightly bound to an apoenzyme and
Prosthetic Group which is not consumed by the reaction. May be covalently
bonded
cofactor which is released from the active site after use and
Coenzyme usually reformed and rebound for the next use. Required by
some enzymes.
holoenzyme Apoenzyme + attatched Cofactors
Zymogen proenzyme, precursor to an enzyme
protein portion of multi component enzyme which requires a
Apoenzyme
cofactor
non protein component required by some enzymes for
Cofactor activity. Can be organic compounds, metalo-organic like
heme, or metal ions like Cu+2
-Lock and key model-enzyme is assumed to be the lock and
substrate the key and they fit exactly
enzyme-substrate models -induced-fit model-assumes that the enzyme active site is
more a flexible pocket whose conformation changes to
accommodate the substrate molecule
1 General Organic Biochemistry ACS final.pdf
-Zymogens (proenzyme)- to free active form
-produce enzyme only when substrate is present-common
in bacteria
methods organisms use to -allosteric enzymes-activate/deactivate
regulate enzyme activity -feedback inhibition
-protein modification, usually phosphorylation, to reversibly
activate or deactivate enzyme
oxidation gain in oxygen, oxygen bonds, loss of H, loss of e
reduction loss of oxygen, oxygen bonds, gain H, gain e
adenosine triphosphate- (coenzyme) transports chemical
energy within cells for metabolism. This is not a redox
ATP
coenzyme. ATP is continuously cycling to ADP and back to
ATP
expressed as an inactive apo-enzyme and must be activated
by its prosthetic group 4' phosphopantetheine. This forms a
Acyl Carrier Protein phosphate ester bond with the -OH on a serine in the
apoenzyme. The SH group attached to the Acyl function be
transferred.
a coenzyme which is tightly bound to an apoenzyme and
Prosthetic Group which is not consumed by the reaction. May be covalently
bonded
cofactor which is released from the active site after use and
Coenzyme usually reformed and rebound for the next use. Required by
some enzymes.
holoenzyme Apoenzyme + attatched Cofactors
Zymogen proenzyme, precursor to an enzyme
protein portion of multi component enzyme which requires a
Apoenzyme
cofactor
non protein component required by some enzymes for
Cofactor activity. Can be organic compounds, metalo-organic like
heme, or metal ions like Cu+2
-Lock and key model-enzyme is assumed to be the lock and
substrate the key and they fit exactly
enzyme-substrate models -induced-fit model-assumes that the enzyme active site is
more a flexible pocket whose conformation changes to
accommodate the substrate molecule
1 General Organic Biochemistry ACS final.pdf
