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targets (6) transporters (2)
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Identification
Name L-Leucine
Accession Number DB00149 (NUTR00033)
Type small molecule
Groups approved, nutraceutical
Description

An essential branched-chain amino acid important for hemoglobin formation. [PubChem]
Structure Thumb
Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure
Synonyms
(2S)-2-Amino-4-methylpentanoic acid
(S)-(+)-Leucine
(S)-2-Amino-4-methylpentanoic acid
(S)-2-Amino-4-methylvaleric acid
(S)-Leucine
1-Leucine
2-Amino-4-methylpentanoic acid
2-Amino-4-methylvaleric acid
alpha-Amino-gamma-methylvaleric acid
alpha-Aminoisocaproic acid
L-(-)-2-Amino-4-methylpentanoic acid
L-(+)-Leucine
L-a-Aminoisocaproic acid
Leu
Leucin
Leucine
First Prev Next Last
Salts Not Available
Brand names Not Available
Brand mixtures
Brand Name Ingredients
Hard Body BCAA (MLO Products) L-Leucine + L-Isoleucine + L-Valine
Hi-Test Muscle Octane BCAA's (Anabol Naturals) L-Leucine + L-Isoleucine + L-Valine
Categories
  • Dietary supplement
  • Micronutrient
  • Essential Amino Acids
CAS number 61-90-5
Weight Average: 131.1729
Monoisotopic: 131.094628665
Chemical Formula C6H13NO2
InChI Key InChIKey=ROHFNLRQFUQHCH-YFKPBYRVSA-N
InChI
InChI=1S/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1
Plain Text
IUPAC Name
(2S)-2-amino-4-methylpentanoic acid
SMILES
CC(C)C[C@H](N)C(O)=O
Plain Text
Mass Spec show (8.19 KB)
Taxonomy
Kingdom Not Available
Classes Not Available
Substructures Not Available
Pharmacology
Indication Indicated to assist in the prevention of the breakdown of muscle proteins that sometimes occur after trauma or severe stress.
Pharmacodynamics An essential amino acid. (Claim) Leucine helps with the regulation of blood-sugar levels, the growth and repair of muscle tissue (such as bones, skin and muscles), growth hormone production, wound healing as well as energy regulation. It can assist to prevent the breakdown of muscle proteins that sometimes occur after trauma or severe stress. It may also be beneficial for individuals with phenylketonuria - a condition in which the body cannot metabolize the amino acid phenylalanine
Mechanism of action This group of essential amino acids are identified as the branched-chain amino acids, BCAAs. Because this arrangement of carbon atoms cannot be made by humans, these amino acids are an essential element in the diet. The catabolism of all three compounds initiates in muscle and yields NADH and FADH2 which can be utilized for ATP generation. The catabolism of all three of these amino acids uses the same enzymes in the first two steps. The first step in each case is a transamination using a single BCAA aminotransferase, with a-ketoglutarate as amine acceptor. As a result, three different a-keto acids are produced and are oxidized using a common branched-chain a-keto acid dehydrogenase, yielding the three different CoA derivatives. Subsequently the metabolic pathways diverge, producing many intermediates. The principal product from valine is propionylCoA, the glucogenic precursor of succinyl-CoA. Isoleucine catabolism terminates with production of acetylCoA and propionylCoA; thus isoleucine is both glucogenic and ketogenic. Leucine gives rise to acetylCoA and acetoacetylCoA, and is thus classified as strictly ketogenic. There are a number of genetic diseases associated with faulty catabolism of the BCAAs. The most common defect is in the branched-chain a-keto acid dehydrogenase. Since there is only one dehydrogenase enzyme for all three amino acids, all three a-keto acids accumulate and are excreted in the urine. The disease is known as Maple syrup urine disease because of the characteristic odor of the urine in afflicted individuals. Mental retardation in these cases is extensive. Unfortunately, since these are essential amino acids, they cannot be heavily restricted in the diet; ultimately, the life of afflicted individuals is short and development is abnormal The main neurological problems are due to poor formation of myelin in the CNS.
Absorption Not Available
Volume of distribution Not Available
Protein binding Not Available
Metabolism Not Available
Route of elimination Not Available
Half life Not Available
Clearance Not Available
Toxicity Not Available
Affected organisms
  • Humans and other mammals
Pathways Not Available
Pharmacoeconomics
Manufacturers Not Available
Packagers
Dosage forms
Form Route Strength
Capsule Oral
Powder Oral
Tablet Oral
Prices
Unit description Cost Unit
Leucine powder 1.62 USD each
L-leucine powder 0.28 USD g
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents Not Available
Properties
State solid
Experimental Properties
Property Value Source
melting point 293 °C PhysProp
water solubility 2.15E+004 mg/L (at 25 °C) YALKOWSKY,SH & DANNENFELSER,RM (1992)
logP -1.52 HANSCH,C ET AL. (1995)
pKa 2.35 (at 13 °C) KORTUM,G ET AL (1961)
Predicted Properties
Property Value Source
water solubility 6.98e+01 g/l ALOGPS
logP -1.8 ALOGPS
logP -1.6 ChemAxon
logS -0.27 ALOGPS
pKa (strongest acidic) 2.79 ChemAxon
pKa (strongest basic) 9.52 ChemAxon
physiological charge 0 ChemAxon
hydrogen acceptor count 3 ChemAxon
hydrogen donor count 2 ChemAxon
polar surface area 63.32 ChemAxon
rotatable bond count 3 ChemAxon
refractivity 34.17 ChemAxon
polarizability 14.16 ChemAxon
References
Synthesis Reference Not Available
General Reference Not Available
External Links
Resource Link
ChEBI 15603 Link_out
ChEMBL 15603 Link_out
PharmGKB PA450197 Link_out
HET LEU Link_out
PDRhealth http://www.pdrhealth.com/drug_info/nmdrugprofiles/nutsupdrugs/bra_0042.shtml Link_out
Wikipedia http://en.wikipedia.org/wiki/L-Leucine Link_out
ATC Codes Not Available
AHFS Codes Not Available
PDB Entries
FDA label Not Available
MSDS show (72.6 KB)
Interactions
Drug Interactions Not Available
Food Interactions Not Available
Targets

1. Probable leucyl-tRNA synthetase, mitochondrial

Pharmacological action: unknown
Organism class: human
UniProt ID: Q15031 Link_out
Gene: LARS2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Ma JJ, Zhao MW, Wang ED: Split leucine-specific domain of leucyl-tRNA synthetase from the hyperthermophilic bacterium Aquifex aeolicus. Biochemistry. 2006 Dec 12;45(49):14809-16. Pubmed
  2. Zhu B, Zhao MW, Eriani G, Wang ED: A present-day aminoacyl-tRNA synthetase with ancestral editing properties. RNA. 2007 Jan;13(1):15-21. Epub 2006 Nov 9. Pubmed
  3. Vu MT, Martinis SA: A unique insert of leucyl-tRNA synthetase is required for aminoacylation and not amino acid editing. Biochemistry. 2007 May 1;46(17):5170-6. Epub 2007 Apr 4. Pubmed
  4. Hsu JL, Rho SB, Vannella KM, Martinis SA: Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles. J Biol Chem. 2006 Aug 11;281(32):23075-82. Epub 2006 Jun 14. Pubmed
  5. Lue SW, Kelley SO: A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation. Biochemistry. 2007 Apr 17;46(15):4466-72. Epub 2007 Mar 23. Pubmed

2. Branched-chain-amino-acid aminotransferase, mitochondrial

Pharmacological action: unknown

Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids

Organism class: human
UniProt ID: O15382 Link_out
Gene: BCAT2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
  3. Berger BJ, English S, Chan G, Knodel MH: Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis. J Bacteriol. 2003 Apr;185(8):2418-31. Pubmed

3. Branched-chain-amino-acid aminotransferase, cytosolic

Pharmacological action: unknown

Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine

Organism class: human
UniProt ID: P54687 Link_out
Gene: BCAT1 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Chen CD, Huang TF, Lin CH, Guan HH, Hsieh YC, Lin YH, Huang YC, Liu MY, Chang WC, Chen CJ: Purification, crystallization and preliminary X-ray crystallographic analysis of branched-chain aminotransferase from Deinococcus radiodurans. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt 6):492-4. Epub 2007 May 5. Pubmed
  2. Saito M, Nishimura K, Wakabayashi S, Kurihara T, Nagata Y: Purification of branched-chain amino acid aminotransferase from Helicobacter pylori NCTC 11637. Amino Acids. 2007 Sep;33(3):445-9. Epub 2006 Nov 2. Pubmed

4. Leucine carboxyl methyltransferase 2

Pharmacological action: unknown

May methylate the carboxyl group of leucine residues to form alpha-leucine ester residues

Organism class: human
UniProt ID: O60294 Link_out
Gene: LCMT2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed

5. Leucine carboxyl methyltransferase 1

Pharmacological action: unknown

Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits (PPP2CA) to form alpha-leucine ester residues

Organism class: human
UniProt ID: Q9UIC8 Link_out
Gene: LCMT1 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed

6. Leucyl-tRNA synthetase, cytoplasmic

Pharmacological action: unknown
Organism class: human
UniProt ID: Q9P2J5 Link_out
Gene: LARS Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Ma JJ, Zhao MW, Wang ED: Split leucine-specific domain of leucyl-tRNA synthetase from the hyperthermophilic bacterium Aquifex aeolicus. Biochemistry. 2006 Dec 12;45(49):14809-16. Pubmed
  2. Karkhanis VA, Boniecki MT, Poruri K, Martinis SA: A viable amino acid editing activity in the leucyl-tRNA synthetase CP1-splicing domain is not required in the yeast mitochondria. J Biol Chem. 2006 Nov 3;281(44):33217-25. Epub 2006 Sep 6. Pubmed
  3. Vu MT, Martinis SA: A unique insert of leucyl-tRNA synthetase is required for aminoacylation and not amino acid editing. Biochemistry. 2007 May 1;46(17):5170-6. Epub 2007 Apr 4. Pubmed
  4. Hsu JL, Rho SB, Vannella KM, Martinis SA: Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles. J Biol Chem. 2006 Aug 11;281(32):23075-82. Epub 2006 Jun 14. Pubmed
  5. Dohm JC, Vingron M, Staub E: Horizontal gene transfer in aminoacyl-tRNA synthetases including leucine-specific subtypes. J Mol Evol. 2006 Oct;63(4):437-47. Epub 2006 Sep 4. Pubmed
Transporters

1. Monocarboxylate transporter 10

Actions: inhibitor

Sodium-independent transporter that mediates the update of aromatic acid. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells (By similarity)

UniProt ID: Q8TF71 Link_out
Gene: SLC16A10 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Kim DK, Kanai Y, Matsuo H, Kim JY, Chairoungdua A, Kobayashi Y, Enomoto A, Cha SH, Goya T, Endou H: The human T-type amino acid transporter-1: characterization, gene organization, and chromosomal location. Genomics. 2002 Jan;79(1):95-103. Pubmed
  2. Kim DK, Kanai Y, Chairoungdua A, Matsuo H, Cha SH, Endou H: Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters. J Biol Chem. 2001 May 18;276(20):17221-8. Epub 2001 Feb 20. Pubmed

2. Monocarboxylate transporter 8

Actions: substrate

Very active and specific thyroid hormone transporter. Stimulates cellular uptake of thyroxine (T4), triiodothyronine (T3), reverse triiodothyronine (rT3) and diidothyronine. Does not transport Leu, Phe, Trp or Tyr

UniProt ID: P36021 Link_out
Gene: SLC16A2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Friesema EC, Ganguly S, Abdalla A, Manning Fox JE, Halestrap AP, Visser TJ: Identification of monocarboxylate transporter 8 as a specific thyroid hormone transporter. J Biol Chem. 2003 Oct 10;278(41):40128-35. Epub 2003 Jul 18. Pubmed
Comments
Drug created on June 13, 2005 07:24 / Updated on February 08, 2013 16:19