Bio Organic Mechanism Flashcards
Which situations are enzymes efficient in
What are the limitations of enzymes
What is a cofactor, coenzyme, prosthetic group, apoenzyme and holoenzyme
What is a vitamin
Give some examples of coenzymes in metabolism
What is the structure and function of vitamin B1
What is the structure and function of vitamin B2
What is the structure and function of vitamin B3
What is the structure and function of vitamin B5
What is the structure and function of vitamin B6
What is the structure and function of vitamin B7
Label the 2 components of biotin
Draw the structure of the carboxybiotnyl- enzyme
What is phase l of the mechanism of pyruvate carboxylase
What is phase lI of the mechanism of pyruvate carboxylate
What is the structure of pyruvate carboxylase
Draw some examples of structures that can be made in human cells
What is a tetrapyrole system
A tetrapyrole system refers to a molecular structure consisting of four pyrrole rings linked together. Pyrrole is a five-membered aromatic ring containing four carbon atoms and one nitrogen atom. When four pyrrole rings are connected in a specific arrangement, they form a tetrapyrole system
What areNAD+ and FAD examples of
Give the equation for the reduction of NAD+
How is FAD reduced
How does FMN and FAD link 2 e- and 1 e- transfer reactions
In 2e- transfer reactions, FMN and FAD can accept or donate two electrons at a time. The flavin cofactors alternate between their oxidized (quinone) and reduced (hydroquinone) forms. For example, during oxidative phosphorylation in mitochondria
In 1e- transfer reactions, FMN and FAD can also participate by accepting or donating one electron at a time. This is typically seen in reactions where the flavin cofactors act as intermediates in radical reactions
The ability of FMN and FAD to participate in both 2e- and 1e- transfer reactions stems from their chemical structure, which includes a flavin ring system capable of accepting or donating electrons, as well as a flexible adenine nucleotide portion that allows for interactions with various enzymes and substrates.
Give some examples of different haem structures
Why are different types of haem molecules needed
What does citrate synthase do
How does citrate synthase work
Draw the first step of the mechanism for citrate synthase
Draw the second step of the mechanism for citrate synthase
(Mechanism continues from previous flashcard)
What does aconitase do
What is the role of the Fe- S cluster in aconitase
Participates in binding the substrates in the reaction ( doesn’t play a redox role)
What is anti elimination
Draw the first step of the mechanism for the conversion of citrate to isocitrate
Draw the second step of the mechanism for the conversion of citrate to isocitrate
Draw the third step of the mechanism for the conversion of citrate to isocitrate
What is the role of isocitrate dehydrogenase
Draw the mechanism for the oxidative decarboxylation of isocitrate to alpha-ketoglutarate in tca cycle
Compare the oxidative decarboxylation of pyruvate and alpha- ketoglutarate
What is the role of succinyl CoA synthetase
Draw the mechanism for the conversion of succinylCoA to succinate in tca cycle
How is oxaloacetate regenerated from succincte
Using succinate dehydrogenase
What is the first step of the regenerationof oxaloacetate from succinate
Draw the general E1 elimination mechanism
Draw the general E2 mechanism
Draw the general E1cb mechanism
Draw the possible elimination reactions for succinate converted to fumerate in the regeneration of oxalacetate
What other role does haem b play in complex ll
How is fumerate converted to malate in the regeneration of oxalacetate
Using the enzyme , fumerase
How is malate converted to oxaloacetate
