Welcome to DrugBank 4.0! If you prefer, you can still go back to version 3.0.
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
LeuNot AvailableNot Available
LeucineNot AvailableNot Available
SaltsNot Available
Brand namesNot 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
CategoriesNot Available
CAS number61-90-5
WeightAverage: 131.1729
Monoisotopic: 131.094628665
Chemical FormulaC6H13NO2
InChI KeyInChIKey=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
IUPAC Name
(2S)-2-amino-4-methylpentanoic acid
SMILES
CC(C)C[C@H](N)C(O)=O
Mass Specshow(8.19 KB)
Taxonomy
KingdomOrganic Compounds
SuperclassOrganic Acids and Derivatives
ClassCarboxylic Acids and Derivatives
SubclassAmino Acids, Peptides, and Analogues
Direct parentAlpha Amino Acids and Derivatives
Alternative parentsAmino Fatty Acids; Enolates; Polyamines; Carboxylic Acids; Monoalkylamines
Substituentscarboxylic acid; enolate; polyamine; primary amine; amine; primary aliphatic amine; organonitrogen compound
Classification descriptionThis compound belongs to the alpha amino acids and derivatives. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon), or a derivative thereof.
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
Metabolism
Route of eliminationNot Available
Half lifeNot Available
ClearanceNot Available
ToxicityNot Available
Affected organisms
  • Humans and other mammals
PathwaysNot Available
SNP Mediated EffectsNot Available
SNP Mediated Adverse Drug ReactionsNot Available
ADMET
Predicted ADMET features
Property Value Probability
Human Intestinal Absorption Not Available Not Available
Blood Brain Barrier Not Available Not Available
Caco-2 permeable Not Available Not Available
P-glycoprotein substrate Not Available Not Available
P-glycoprotein inhibitor I Not Available Not Available
P-glycoprotein inhibitor II Not Available Not Available
Renal organic cation transporter Not Available Not Available
CYP450 2C9 substrate Not Available Not Available
CYP450 2D6 substrate Not Available Not Available
CYP450 3A4 substrate Not Available Not Available
CYP450 1A2 substrate Not Available Not Available
CYP450 2C9 substrate Not Available Not Available
CYP450 2D6 substrate Not Available Not Available
CYP450 2C19 substrate Not Available Not Available
CYP450 3A4 substrate Not Available Not Available
CYP450 inhibitory promiscuity Not Available Not Available
Ames test Not Available Not Available
Carcinogenicity Not Available Not Available
Biodegradation Not Available Not Available
Rat acute toxicity Not Available Not applicable
hERG inhibition (predictor I) Not Available Not Available
hERG inhibition (predictor II) Not Available Not Available
Pharmacoeconomics
ManufacturersNot Available
Packagers
Dosage forms
FormRouteStrength
CapsuleOral
PowderOral
TabletOral
Prices
Unit descriptionCostUnit
Leucine powder1.62USDeach
L-leucine powder0.28USDg
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 solubility6.98e+01 g/lALOGPS
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 area63.32ChemAxon
rotatable bond count3ChemAxon
refractivity34.17ChemAxon
polarizability14.16ChemAxon
number of rings0ChemAxon
bioavailability1ChemAxon
rule of fiveYesChemAxon
Ghose filterNoChemAxon
Veber's ruleNoChemAxon
MDDR-like ruleNoChemAxon
Spectra
Spectra
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
ResourceLink
ChEBI15603
ChEMBLCHEMBL291962
PharmGKBPA450197
HETLEU
PDRhealthhttp://www.pdrhealth.com/drug_info/nmdrugprofiles/nutsupdrugs/bra_0042.shtml
WikipediaL-Leucine
ATC CodesNot Available
AHFS CodesNot Available
PDB Entries
FDA labelNot Available
MSDSshow(72.6 KB)
Interactions
Drug InteractionsNot Available
Food InteractionsNot Available

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. 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

3. 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

4. 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

5. 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

6. 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

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

Comments
Drug created on June 13, 2005 07:24 / Updated on September 24, 2013 12:24