Leucine

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Leucine (abbreviated as Leu or L)[2] is a branched-chain α-amino acid with the chemical formula HO2CCH(NH2)CH2CH(CH3)2. It is an essential amino acid, which means that humans cannot synthesize it. Its codons are UUA, UUG, CUU, CUC, CUA, and CUG. With a hydrocarbon side chain, leucine is classified as a hydrophobic amino acid. It has an isobutyl R group. Leucine is a major component of the sub units in ferritin, astacin and other 'buffer' proteins.

Contents

Biosynthesis

As an essential amino acid, leucine is not synthesized in animals, hence it must be ingested, usually as a component of proteins. It is synthesized in plants and microorganisms via several steps starting from pyruvic acid. The initial part of the pathway also leads to valine. The intermediate α-ketovalerate is converted to α-isopropylmalate and then β-isopropylmalate, which is dehydrogenated to α-ketoisocaproate, which in the final step undergoes reductive amination. Enzymes involved in a typical leucine biosynthesis include[3]

Biology

Leucine is utilized in the liver, adipose tissue, and muscle tissue. In adipose and muscle tissue, leucine is used in the formation of sterols, and the combined usage of leucine in these two tissues is seven times greater than its use in the liver.[4]

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