Acyl Carrier Protein
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expressed as an inactive apo-enzyme and must be activated by its
prosthetic group 4' phosphopantetheine. This forms a phosphate
ester bond with the -OH on a serine in the apoenzyme. The SH group
attached to the Acyl function be transferred.
, buffer
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required for pH control. Only the very acidic parts of the digestive
system can operate unbuffered due to high H+ availability. Most
other systems operate on CO2 buffers.
methods organisms use to regulate enzyme activity
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-Zymogens (proenzyme)- to free active form
-produce enzyme only when substrate is present-common in bacteria
-allosteric enzymes-activate/deactivate
-feedback inhibition
-protein modification, usually phosphorylation, to reversibly activate
or deactivate enzyme
enzyme-substrate models
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-Lock and key model-enzyme is assumed to be the lock and
substrate the key and they fit exactly
-induced-fit model-assumes that the enzyme active site is more a
flexible pocket whose conformation changes to accommodate the
substrate molecule
Give this one a try later!
expressed as an inactive apo-enzyme and must be activated by its
prosthetic group 4' phosphopantetheine. This forms a phosphate
ester bond with the -OH on a serine in the apoenzyme. The SH group
attached to the Acyl function be transferred.
, buffer
Give this one a try later!
required for pH control. Only the very acidic parts of the digestive
system can operate unbuffered due to high H+ availability. Most
other systems operate on CO2 buffers.
methods organisms use to regulate enzyme activity
Give this one a try later!
-Zymogens (proenzyme)- to free active form
-produce enzyme only when substrate is present-common in bacteria
-allosteric enzymes-activate/deactivate
-feedback inhibition
-protein modification, usually phosphorylation, to reversibly activate
or deactivate enzyme
enzyme-substrate models
Give this one a try later!
-Lock and key model-enzyme is assumed to be the lock and
substrate the key and they fit exactly
-induced-fit model-assumes that the enzyme active site is more a
flexible pocket whose conformation changes to accommodate the
substrate molecule
