Bio Organic Mechanism Flashcards by Joey Pang

Q

Which situations are enzymes efficient in

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Q

What are the limitations of enzymes

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Q

What is a cofactor, coenzyme, prosthetic group, apoenzyme and holoenzyme

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Q

What is a vitamin

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Q

Give some examples of coenzymes in metabolism

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Q

What is the structure and function of vitamin B1

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Q

What is the structure and function of vitamin B2

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Q

What is the structure and function of vitamin B3

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Q

What is the structure and function of vitamin B5

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Q

What is the structure and function of vitamin B6

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Q

What is the structure and function of vitamin B7

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Q

Label the 2 components of biotin

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Q

Draw the structure of the carboxybiotnyl- enzyme

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Q

What is phase l of the mechanism of pyruvate carboxylase

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Q

What is phase lI of the mechanism of pyruvate carboxylate

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Q

What is the structure of pyruvate carboxylase

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Q

Draw some examples of structures that can be made in human cells

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Q

What is a tetrapyrole system

A

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

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Q

What areNAD+ and FAD examples of

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Q

Give the equation for the reduction of NAD+

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Q

How is FAD reduced

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Q

How does FMN and FAD link 2 e- and 1 e- transfer reactions

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A

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.

Q

Give some examples of different haem structures

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Q

Why are different types of haem molecules needed

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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

Draw the mechanism for the conversion of malate to oxaloacetate