Biological Chemistry: Vitamins and Coenzymes

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These flashcards cover key concepts from the Biological Chemistry lecture regarding Vitamins and Coenzymes, focusing on their functions, classifications, and biochemical roles.

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16 Terms

1
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What is the function of cofactors in enzymes?

Cofactors bind to the active site and assist in the reaction mechanism.

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What is an apoenzyme?

An apoenzyme is an enzyme lacking its cofactor.

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What is a holoenzyme?

A holoenzyme is an enzyme with its cofactor.

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What type of cofactor stays with the enzyme?

A prosthetic group.

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What is an example of an inorganic cation cofactor?

Metal ions such as Fe2+, Cu2+, or Zn2+.

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What condition is caused by thiamine (B₁) deficiency?

Beriberi, which includes weight loss, heart problems, and neurological dysfunction.

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What role does NAD(Nicotinamide adenine dinucleotide) play in the cell?

NAD acts as a soluble electron carrier involved in oxidation-reduction reactions, primarily in catabolic pathways.

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How is riboflavin (B2) related to coenzymes?

Riboflavin is the precursor to flavin coenzymes FMN and FAD.

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What is the significance of Vitamin C in biochemical reactions?

Vitamin C acts as a reducing agent and is important in maintaining metal cofactors, collagen synthesis, and acts as an antioxidant.

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What is the function of tetrahydrofolate (THF)?

THF acts as a carrier for one-carbon units in various metabolic reactions.

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What does Vitamin K contribute to in the body?

Vitamin K is involved in blood coagulation.

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What are the main functions of Vitamin E?

Vitamin E protects cell membranes from oxidation, aids in red blood cell formation, and promotes circulatory health.

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What happens to retinol when acting in photoreceptors of the eye?

Retinol acts as the precursor for the visual pigment 11-cis-retinal.

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What deficiency results from a lack of Vitamin B12?

Pernicious anemia.

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How is biotin related to carboxylase enzymes?

Biotin is active in carboxylase enzymes for the transfer of carbon units.

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