Why is biotin used as a coenzyme for pyruvate carboxylase?

Biotin functions as a cofactor that aids in the transfer of CO2 groups to various target macromolecules. Biotin has nine host enzymes with which it is associated. Humans only have four of these enzymes: Pyruvate carboxylase (formation of oxaloacetate from pyruvate)

Click to see complete answer. Similarly one may ask, why is acetyl CoA an activator of pyruvate carboxylase?

A high level of acetyl-CoA inside mitochondria is required for optimal activity of pyruvate carboxylase. Acetyl-CoA serves as an allosteric activator of this enzyme, even though acetyl-CoA itself does not partake in the reaction.

Subsequently, question is, why is pyruvate converted to Oxaloacetate? Pyruvate is first converted by pyruvate carboxylase to oxaloacetate (OAA) in the mitochondrion requiring hydrolysis of one molecule of ATP. However, during starvation when cytosolic NADH concentration is low and mitochrondrial NADH levels are high oxaloacetate can be used as a shuttle of reducing equivalents.

Subsequently, question is, what is the function of biotin in fatty acid synthesis?

Biotin is important in fatty acid synthesis, branched-chain amino acid catabolism, and gluconeogenesis. It covalently attaches to the epsilon-amino group of specific lysine residues in these carboxylases. This biotinylation reaction requires ATP and is catalyzed by holocarboxylase synthetase.

What coenzyme is required for the conversion of pyruvate to oxaloacetate?

acetyl Coenzyme A