Exam Questions Flashcards
What are Coenymzes ? and what do they do to the enzyme ?
these are organic compounds, often containing a vitamin molecule as part of their structure.
Coenzymes are not permanently bound to the enzyme but may be temporarily and loosely bound for the duration of the reaction and then move away once it is completed. For example NAD, which transfers hydrogen away from one molecule in a dehydrogenase reaction and takes it to another molecule
Is the rate of reaction closer to the maximum for completive ?
The rate of reaction will be closer to the maximum when there is more ‘real’ substrate, (e.g. arabinose competes with glucose for the active sites on glucose oxidase enzyme).
What are non-competive inhibitors and do they bind to the active site ?
: these molecules are not necessarily anything like the substrate in shape. They bind with the enzyme, but not at the active site. This binding does change the shape of the enzyme though, so the reaction rate decreases.
What are the four types of specifity ?
Absolute specificity - the enzyme will catalyze only one reaction.
Group specificity - the enzyme will act only on molecules that have specific functional groups, such as amino, phosphate and methyl groups.
Linkage specificity - the enzyme will act on a particular type of chemical bond regardless of the rest of the molecular structure.
Stereo chemical specificity - the enzyme will act on a particular steric or optical isomer.
Excergonic Reaction
Products have less energy reaction
What is a specific Property for Proline ?
Its a cyclic pyrrolidine
What is the force for globular proteins In terms of Tertiary structures ?
Hydrophobic Efffect.
What type of Reversible enzyme inhibitor binds to both the free enzyme and ES complex ?
Non-competive
