Leucine
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.
Biosynthesis
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[2]
- Acetolactate synthase,
- Acetohydroxy acid isomeroreductase,
- Dihydroxyacid dehydratase,
- α-Isopropylmalate synthase,
- α-Isopropylmalate isomerase,
- Leucine aminotransferase.
References
References
- ↑ IUPAC-IUBMB Joint Commission on Biochemical Nomenclature. “Nomenclature and Symbolism for Amino Acids and Peptides”. Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc. Retrieved 2007-05-17.
- ↑ Nelson, D. L.; Cox, M. M. “Lehninger, Principles of Biochemistry” 3rd Ed. Worth Publishing: New York, 2000. ISBN 1-57259-153-6.
External links
External links
- 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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