Leucine

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]

Leucine (abbreviated as Leu or L)^[1] is an α-amino acid with the chemical formula HO₂CCH(NH₂)CH₂CH(CH₃)₂. It is an essential amino acid, which means that humans cannot synthesise it. Its codons are UUA, UUG, CUU, CUC, CUA, and CUG. With a hydrocarbon side chain, leucine is classified as a hydrophobic amino acid.

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^[2]

• Acetolactate synthase,
• Acetohydroxy acid isomeroreductase,
• Dihydroxyacid dehydratase,
• α-Isopropylmalate synthase,
• α-Isopropylmalate isomerase,
• Leucine aminotransferase.

• Photo-reactive leucine

• Leucine biosynthesis
• Leucine content in food
• Computational Chemistry Wiki
• Leucine prevents muscle loss in rats
• Leucine helps regulate appetite in rats

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