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Identification
NameL-Leucine
Accession NumberDB00149  (NUTR00033)
TypeSmall Molecule
GroupsApproved, Nutraceutical
Description

An essential branched-chain amino acid important for hemoglobin formation. [PubChem]

Structure
Thumb
Synonyms
SynonymLanguageCode
(2S)-2-Amino-4-methylpentanoic acidNot AvailableNot Available
(2S)-alpha-2-Amino-4-methylvaleric acidNot AvailableNot Available
(2S)-alpha-LeucineNot AvailableNot Available
(S)-(+)-LeucineNot AvailableNot Available
(S)-LeucineNot AvailableNot Available
2-Amino-4-methylvaleric acidNot AvailableNot Available
LNot AvailableNot Available
L-LeucinNot AvailableNot Available
L-LeucineNot AvailableNot Available
L-LeuzinNot AvailableNot Available
LeuNot AvailableNot Available
LeucineNot AvailableNot Available
Prescription ProductsNot Available
Generic Prescription ProductsNot Available
Over the Counter ProductsNot Available
International BrandsNot Available
Brand mixtures
Brand NameIngredients
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
SaltsNot Available
Categories
CAS number61-90-5
WeightAverage: 131.1729
Monoisotopic: 131.094628665
Chemical FormulaC6H13NO2
InChI KeyROHFNLRQFUQHCH-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
IUPAC Name
(2S)-2-amino-4-methylpentanoic acid
SMILES
CC(C)C[C@H](N)C(O)=O
Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentL-alpha-amino acids
Alternative Parents
Substituents
  • L-alpha-amino acid
  • Methyl-branched fatty acid
  • Branched fatty acid
  • Amino fatty acid
  • Fatty acyl
  • Fatty acid
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Hydrocarbon derivative
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Primary aliphatic amine
  • Carbonyl group
  • Amine
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Pharmacology
IndicationIndicated to assist in the prevention of the breakdown of muscle proteins that sometimes occur after trauma or severe stress.
PharmacodynamicsAn 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 actionThis 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.
AbsorptionNot Available
Volume of distributionNot Available
Protein bindingNot Available
MetabolismNot Available
Route of eliminationNot Available
Half lifeNot Available
ClearanceNot Available
ToxicityNot Available
Affected organisms
  • Humans and other mammals
Pathways
PathwayCategorySMPDB ID
Leucine Stimulation on Insulin SignalingSignalingSMP00682
2-Methyl-3-Hydroxybutryl CoA Dehydrogenase DeficiencyDiseaseSMP00137
3-Methylglutaconic Aciduria Type IDiseaseSMP00139
Beta-Ketothiolase DeficiencyDiseaseSMP00173
3-Methylcrotonyl Coa Carboxylase Deficiency Type IDiseaseSMP00237
Isovaleric AciduriaDiseaseSMP00238
Propionic AcidemiaDiseaseSMP00236
3-Methylglutaconic Aciduria Type IIIDiseaseSMP00140
3-Methylglutaconic Aciduria Type IVDiseaseSMP00141
3-hydroxyisobutyric acid dehydrogenase deficiencyDiseaseSMP00521
Isovaleric acidemiaDiseaseSMP00524
Maple Syrup Urine DiseaseDiseaseSMP00199
Methylmalonic AciduriaDiseaseSMP00200
Isobutyryl-coa dehydrogenase deficiencyDiseaseSMP00523
Valine, Leucine and Isoleucine DegradationMetabolicSMP00032
3-Hydroxy-3-Methylglutaryl-CoA Lyase DeficiencyDiseaseSMP00138
Methylmalonate Semialdehyde Dehydrogenase DeficiencyDiseaseSMP00384
3-hydroxyisobutyric aciduriaDiseaseSMP00522
Azithromycin Action PathwayDrug actionSMP00247
Gentamicin Action PathwayDrug actionSMP00254
Streptomycin Action PathwayDrug actionSMP00259
Chloramphenicol Action PathwayDrug actionSMP00729
Roxithromycin Action PathwayDrug actionSMP00251
Amikacin Action PathwayDrug actionSMP00253
Spectinomycin Action PathwayDrug actionSMP00258
Lymecycline Action PathwayDrug actionSMP00295
Lincomycin Action PathwayDrug actionSMP00728
Clomocycline Action PathwayDrug actionSMP00262
Clarithromycin Action PathwayDrug actionSMP00248
Kanamycin Action PathwayDrug actionSMP00255
Demeclocycline Action PathwayDrug actionSMP00290
Minocycline Action PathwayDrug actionSMP00292
Troleandomycin Action PathwayDrug actionSMP00730
Erythromycin Action PathwayDrug actionSMP00250
Telithromycin Action PathwayDrug actionSMP00252
Netilmicin Action PathwayDrug actionSMP00257
Tetracycline Action PathwayDrug actionSMP00294
Tigecycline Action PathwayDrug actionSMP00712
Paromomycin Action PathwayDrug actionSMP00714
Methacycline Action PathwayDrug actionSMP00727
Clindamycin Action PathwayDrug actionSMP00249
Neomycin Action PathwayDrug actionSMP00256
Doxycycline Action PathwayDrug actionSMP00291
Oxytetracycline Action PathwayDrug actionSMP00293
Tobramycin Action PathwayDrug actionSMP00711
Arbekacin Action PathwayDrug actionSMP00713
Rolitetracycline Action PathwayDrug actionSMP00726
Josamycin Action PathwayDrug actionSMP00731
SNP Mediated EffectsNot Available
SNP Mediated Adverse Drug ReactionsNot Available
ADMET
Predicted ADMET features
PropertyValueProbability
Human Intestinal AbsorptionNot AvailableNot Available
Blood Brain BarrierNot AvailableNot Available
Caco-2 permeableNot AvailableNot Available
P-glycoprotein substrateNot AvailableNot Available
P-glycoprotein inhibitor INot AvailableNot Available
P-glycoprotein inhibitor IINot AvailableNot Available
Renal organic cation transporterNot AvailableNot Available
CYP450 2C9 substrateNot AvailableNot Available
CYP450 2D6 substrateNot AvailableNot Available
CYP450 3A4 substrateNot AvailableNot Available
CYP450 1A2 substrateNot AvailableNot Available
CYP450 2C9 substrateNot AvailableNot Available
CYP450 2D6 substrateNot AvailableNot Available
CYP450 2C19 substrateNot AvailableNot Available
CYP450 3A4 substrateNot AvailableNot Available
CYP450 inhibitory promiscuityNot AvailableNot Available
Ames testNot AvailableNot Available
CarcinogenicityNot AvailableNot Available
BiodegradationNot AvailableNot Available
Rat acute toxicityNot AvailableNot applicable
hERG inhibition (predictor I)Not AvailableNot Available
hERG inhibition (predictor II)Not AvailableNot Available
Pharmacoeconomics
ManufacturersNot Available
Packagers
Dosage formsNot Available
Prices
Unit descriptionCostUnit
Leucine powder1.62USD each
L-leucine powder0.28USD g
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
PatentsNot Available
Properties
StateSolid
Experimental Properties
PropertyValueSource
melting point293 °CPhysProp
water solubility2.15E+004 mg/L (at 25 °C)YALKOWSKY,SH & DANNENFELSER,RM (1992)
logP-1.52HANSCH,C ET AL. (1995)
pKa2.35 (at 13 °C)KORTUM,G ET AL (1961)
Predicted Properties
PropertyValueSource
Water Solubility69.8 mg/mLALOGPS
logP-1.8ALOGPS
logP-1.6ChemAxon
logS-0.27ALOGPS
pKa (Strongest Acidic)2.79ChemAxon
pKa (Strongest Basic)9.52ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area63.32 Å2ChemAxon
Rotatable Bond Count3ChemAxon
Refractivity34.17 m3·mol-1ChemAxon
Polarizability14.16 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Mass Spec (NIST)Download (8.19 KB)
SpectraGC-MSMS/MSLC-MS1D NMR2D NMR
References
Synthesis Reference

Takayasu Tsuchida, Haruo Momose, Yoshio Hirose, “Process for producing L-leucine.” U.S. Patent US3970519, issued February, 1975.

US3970519
General ReferenceNot Available
External Links
ATC CodesNot Available
AHFS CodesNot Available
PDB Entries
FDA labelNot Available
MSDSDownload (72.6 KB)
Interactions
Drug InteractionsNot Available
Food InteractionsNot Available

Targets

1. Probable leucine--tRNA ligase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Probable leucine--tRNA ligase, mitochondrial Q15031 Details

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. Leucine carboxyl methyltransferase 2

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Leucine carboxyl methyltransferase 2 O60294 Details

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. Leucine carboxyl methyltransferase 1

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Leucine carboxyl methyltransferase 1 Q9UIC8 Details

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

4. Leucine--tRNA ligase, cytoplasmic

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Leucine--tRNA ligase, cytoplasmic Q9P2J5 Details

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

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

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Branched-chain-amino-acid aminotransferase, mitochondrial O15382 Details

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

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

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Branched-chain-amino-acid aminotransferase, cytosolic P54687 Details

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

Transporters

1. Monocarboxylate transporter 10

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: inhibitor

Components

Name UniProt ID Details
Monocarboxylate transporter 10 Q8TF71 Details

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

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Monocarboxylate transporter 8 P36021 Details

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

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Drug created on June 13, 2005 07:24 / Updated on December 09, 2014 20:48