Banner
Identification
Name L-Alanine
Accession Number DB00160 (NUTR00013)
Type small molecule
Groups approved, nutraceutical
Description

A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases immunity, and provides energy for muscle tissue, brain, and the central nervous system. [PubChem]
Structure Thumb
Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure
Synonyms
(2S)-2-Aminopropanoic acid
(S)-(+)-Alanine
(S)-2-Aminopropanoic acid
(S)-Alanine
2-Aminopropanoic acid
2-Aminopropionic acid
a-Alanine
a-Aminopropionic acid
ALA
Alanine
L-(+)-Alanine
L-2-Aminopropanoic acid
L-2-Aminopropionic acid
L-a-Alanine
L-a-Aminopropionic acid
First Prev Next Last
Salts Not Available
Brand names Not Available
Brand mixtures
Brand Name Ingredients
Aminosyn Glycine + Histidine + L-Alanine + L-Arginine + L-Isoleucine + L-Leucine + L-Lysine (L-Lysine Acetate) + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Tryptophan
Aminosyn II Glutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Isoleucine + L-Leucine + L-Lysine (L-Lysine Acetate) + L-Phenylalanine + L-Proline + L-Threonine + L-Valine + Methionine + N-Acetyl-L-Tyrosine + Serine + Tryptophan
Primene Glutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine + L-Isoleucine + L-Leucine + L-Lysine + L-Ornithine Dihydrochloride + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Taurine + Tryptophan
Renamin (Amino Acids) Injection Glycine + Histidine + L-Alanine + L-Arginine + L-Isoleucine + L-Leucine + L-Lysine Hydrochloride + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Tryptophan
Travasol Amino Acid Injection With Electrolytes Dextrose + Glycine + Histidine + L-Alanine + L-Arginine + L-Isoleucine + L-Leucine + L-Lysine (L-Lysine Hydrochloride) + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Magnesium Chloride + Methionine + Potassium Phosphate Dibasic + Serine + Sodium Acetate + Sodium Chloride + Tryptophan
Travasol Amino Acid Injection Without Electrolytes Dextrose + Glycine + Histidine + L-Alanine + L-Arginine + L-Isoleucine + L-Leucine Hydrochloride + L-Lysine Hydrochloride + L-Phenylalanine Hydrochloride + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Tryptophan
Categories
  • Dietary supplement
  • Micronutrient
  • Non-Essential Amino Acids
CAS number 56-41-7
Weight Average: 89.0932
Monoisotopic: 89.047678473
Chemical Formula C3H7NO2
InChI Key InChIKey=QNAYBMKLOCPYGJ-REOHCLBHSA-N
InChI
InChI=1S/C3H7NO2/c1-2(4)3(5)6/h2H,4H2,1H3,(H,5,6)/t2-/m0/s1
Plain Text
IUPAC Name
(2S)-2-aminopropanoic acid
SMILES
C[C@H](N)C(O)=O
Plain Text
Mass Spec show (6.76 KB)
Taxonomy
Kingdom Organic
Classes
  • Amino Acids
Substructures
  • Amino Acids
  • Hydroxy Compounds
  • Acetates
  • Aliphatic and Aryl Amines
  • Carboxylic Acids and Derivatives
Pharmacology
Indication Used for protein synthesis.
Pharmacodynamics Is an important source of energy for muscle tissue, the brain and central nervous system; strengthens the immune system by producing antibodies; helps in the metabolism of sugars and organic acids.
Mechanism of action L-Alanine is a non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases immunity, and provides energy for muscle tissue, brain, and the central nervous system. BCAAs are used as a source of energy for muscle cells. During prolonged exercise, BCAAs are released from skeletal muscles and their carbon backbones are used as fuel, while their nitrogen portion is used to form another amino acid, Alanine. Alanine is then converted to Glucose by the liver. This form of energy production is called the Alanine-Glucose cycle, and it plays a major role in maintaining the body's blood sugar balance.
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 Not Available
Prices
Unit description Cost Unit
L-alanine powder 2.35 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 300 dec °C PhysProp
water solubility 1.64E+005 mg/L (at 25 °C) YALKOWSKY,SH & DANNENFELSER,RM (1992)
logP -2.85 SANGSTER (1994)
pKa 2.34 (at 25 °C) KORTUM,G ET AL (1961)
Predicted Properties
Property Value Source
water solubility 4.47e+02 g/l ALOGPS
logP -3 ALOGPS
logP -2.8 ChemAxon
logS 0.7 ALOGPS
pKa (strongest acidic) 2.47 ChemAxon
pKa (strongest basic) 9.48 ChemAxon
physiological charge 0 ChemAxon
hydrogen acceptor count 3 ChemAxon
hydrogen donor count 2 ChemAxon
polar surface area 63.32 ChemAxon
rotatable bond count 1 ChemAxon
refractivity 20.5 ChemAxon
polarizability 8.52 ChemAxon
References
Synthesis Reference Not Available
General Reference Not Available
External Links
Resource Link
KEGG Compound C01401 Link_out
PubChem Compound 5950 Link_out
PubChem Substance 46504866 Link_out
ChemSpider 5735 Link_out
ChEBI 16977 Link_out
ChEMBL 16977 Link_out
Therapeutic Targets Database DAP000805 Link_out
PharmGKB PA448055 Link_out
IUPHAR 720 Link_out
Guide to Pharmacology 720 Link_out
HET ALA Link_out
ATC Codes Not Available
AHFS Codes Not Available
PDB Entries
FDA label Not Available
MSDS show (71.9 KB)
Interactions
Drug Interactions Not Available
Food Interactions Not Available
Targets

1. Serine--pyruvate aminotransferase

Pharmacological action: unknown
Organism class: human
UniProt ID: P21549 Link_out
Gene: AGXT 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. Salido EC, Li XM, Lu Y, Wang X, Santana A, Roy-Chowdhury N, Torres A, Shapiro LJ, Roy-Chowdhury J: Alanine-glyoxylate aminotransferase-deficient mice, a model for primary hyperoxaluria that responds to adenoviral gene transfer. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18249-54. Epub 2006 Nov 16. Pubmed
  4. Amoroso A, Pirulli D, Florian F, Puzzer D, Boniotto M, Crovella S, Zezlina S, Spano A, Mazzola G, Savoldi S, Ferrettini C, Berutti S, Petrarulo M, Marangella M: AGXT gene mutations and their influence on clinical heterogeneity of type 1 primary hyperoxaluria. J Am Soc Nephrol. 2001 Oct;12(10):2072-9. Pubmed
  5. Pirulli D, Puzzer D, Ferri L, Crovella S, Amoroso A, Ferrettini C, Marangella M, Mazzola G, Florian F: Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene. Hum Genet. 1999 Jun;104(6):523-5. Pubmed

2. 4-aminobutyrate aminotransferase, mitochondrial

Pharmacological action: unknown
Actions: inhibitor

Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine

Organism class: human
UniProt ID: P80404 Link_out
Gene: ABAT Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Amadasi A, Bertoldi M, Contestabile R, Bettati S, Cellini B, di Salvo ML, Borri-Voltattorni C, Bossa F, Mozzarelli A: Pyridoxal 5’-phosphate enzymes as targets for therapeutic agents. Curr Med Chem. 2007;14(12):1291-324. Pubmed
  2. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. Pubmed

3. Kynureninase

Pharmacological action: unknown

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic (AA) and 3- hydroxyanthranilic acids (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity

Organism class: human
UniProt ID: Q16719 Link_out
Gene: KYNU Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Christensen M, Duno M, Lund AM, Skovby F, Christensen E: Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase. J Inherit Metab Dis. 2007 Apr;30(2):248-55. Epub 2007 Mar 1. Pubmed
  2. Lima S, Khristoforov R, Momany C, Phillips RS: Crystal structure of Homo sapiens kynureninase. Biochemistry. 2007 Mar 13;46(10):2735-44. Epub 2007 Feb 15. Pubmed

4. Probable alanyl-tRNA synthetase, mitochondrial

Pharmacological action: unknown

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)

Organism class: human
UniProt ID: Q5JTZ9 Link_out
Gene: AARS2 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. Nagan MC, Beuning P, Musier-Forsyth K, Cramer CJ: Importance of discriminator base stacking interactions: molecular dynamics analysis of A73 microhelix(Ala) variants. Nucleic Acids Res. 2000 Jul 1;28(13):2527-34. Pubmed
  4. McClain WH, Gabriel K, Schneider J: Specific function of a G.U wobble pair from an adjacent helical site in tRNA(Ala) during recognition by alanyl-tRNA synthetase. RNA. 1996 Feb;2(2):105-9. Pubmed
  5. Buechter DD, Schimmel P: Minor groove recognition of the critical acceptor helix base pair by an appended module of a class II tRNA synthetase. Biochemistry. 1995 May 9;34(18):6014-9. Pubmed

5. Alanine--glyoxylate aminotransferase 2-like 2

Pharmacological action: unknown
Organism class: human
UniProt ID: Q8IUZ5 Link_out
Gene: AGXT2L2 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. Alanine aminotransferase 2

Pharmacological action: unknown

L-alanine + 2-oxoglutarate = pyruvate + L- glutamate

Organism class: human
UniProt ID: Q8TD30 Link_out
Gene: GPT2 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. Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. Pubmed
  4. Jadhao SB, Yang RZ, Lin Q, Hu H, Anania FA, Shuldiner AR, Gong DW: Murine alanine aminotransferase: cDNA cloning, functional expression, and differential gene regulation in mouse fatty liver. Hepatology. 2004 May;39(5):1297-302. Pubmed
  5. Rajamohan F, Nelms L, Joslin DL, Lu B, Reagan WJ, Lawton M: cDNA cloning, expression, purification, distribution, and characterization of biologically active canine alanine aminotransferase-1. Protein Expr Purif. 2006 Jul;48(1):81-9. Epub 2006 Jan 30. Pubmed

7. Alanine aminotransferase 1

Pharmacological action: unknown

Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles

Organism class: human
UniProt ID: P24298 Link_out
Gene: GPT Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Miyashita Y, Dolferus R, Ismond KP, Good AG: Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana. Plant J. 2007 Mar;49(6):1108-21. Epub 2007 Feb 22. Pubmed
  2. Gray S, Wang B, Orihuela Y, Hong EG, Fisch S, Haldar S, Cline GW, Kim JK, Peroni OD, Kahn BB, Jain MK: Regulation of gluconeogenesis by Kruppel-like factor 15. Cell Metab. 2007 Apr;5(4):305-12. Pubmed
  3. Taracha E, Habrat B, Chrapusta SJ, Lehner M, Wislowska A, Woronowicz BT, Bogulas M, Charewicz J, Markuszewski C, Plaznik A: Combining markers of nephrotoxicity and hepatotoxicity for improved monitoring and detection of chronic alcohol abuse. Clin Chem Lab Med. 2006;44(12):1446-52. Pubmed
  4. Chen CH, Lee RP, Wu WT, Liao KW, Hsu N, Hsu BG: Fluvastatin ameliorates endotoxin induced multiple organ failure in conscious rats. Resuscitation. 2007 Jul;74(1):166-74. Epub 2007 Mar 13. Pubmed

8. Cysteine desulfurase, mitochondrial

Pharmacological action: unknown

Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters

Organism class: human
UniProt ID: Q9Y697 Link_out
Gene: NFS1 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. You D, Wang L, Yao F, Zhou X, Deng Z: A novel DNA modification by sulfur: DndA is a NifS-like cysteine desulfurase capable of assembling DndC as an iron-sulfur cluster protein in Streptomyces lividans. Biochemistry. 2007 May 22;46(20):6126-33. Epub 2007 May 1. Pubmed
  2. Zeng J, Zhang Y, Liu Y, Zhang X, Xia L, Liu J, Qiu G: Expression, purification and characterization of a cysteine desulfurase, IscS, from Acidithiobacillus ferrooxidans. Biotechnol Lett. 2007 Jul 28;. Pubmed

9. Proton-coupled amino acid transporter 1

Pharmacological action: unknown

Neutral amino acid/proton symporter. Has a pH-dependent electrogenic transport activity for small amino acids such as glycine, alanine and proline. Besides small apolar L-amino acids, it also recognize their D-enantiomers and selected amino acid derivatives such as gamma-aminobutyric acid

Organism class: human
UniProt ID: Q7Z2H8 Link_out
Gene: SLC36A1 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. Miyauchi S, Abbot EL, Zhuang L, Subramanian R, Ganapathy V, Thwaites DT: Isolation and function of the amino acid transporter PAT1 (slc36a1) from rabbit and discrimination between transport via PAT1 and system IMINO in renal brush-border membrane vesicles. Mol Membr Biol. 2005 Nov-Dec;22(6):549-59. Pubmed

10. Large neutral amino acids transporter small subunit 2

Pharmacological action: unknown

Sodium-independent, high-affinity transport of large neutral amino acids. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids

Organism class: human
UniProt ID: Q9UHI5 Link_out
Gene: SLC7A8 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Broer S, Broer A, Hansen JT, Bubb WA, Balcar VJ, Nasrallah FA, Garner B, Rae C: Alanine metabolism, transport, and cycling in the brain. J Neurochem. 2007 Sep;102(6):1758-70. Epub 2007 May 14. Pubmed

11. Alanine--glyoxylate aminotransferase 2, mitochondrial

Pharmacological action: unknown
Organism class: human
UniProt ID: Q9BYV1 Link_out
Gene: AGXT2 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. Okuno E, Ishikawa T, Kawai J, Kido R: Alanine:glyoxylate aminotransferase activities in liver of Suncus murinus (insectivora). Comp Biochem Physiol B. 1988;90(4):773-8. Pubmed
  4. Takada Y, Mori T, Noguchi T: The effect of vitamin B6 deficiency on alanine: glyoxylate aminotransferase isoenzymes in rat liver. Arch Biochem Biophys. 1984 Feb 15;229(1):1-6. Pubmed

12. Alanyl-tRNA synthetase, cytoplasmic

Pharmacological action: unknown
Organism class: human
UniProt ID: P49588 Link_out
Gene: AARS 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. Nagan MC, Beuning P, Musier-Forsyth K, Cramer CJ: Importance of discriminator base stacking interactions: molecular dynamics analysis of A73 microhelix(Ala) variants. Nucleic Acids Res. 2000 Jul 1;28(13):2527-34. Pubmed
  4. McClain WH, Gabriel K, Schneider J: Specific function of a G.U wobble pair from an adjacent helical site in tRNA(Ala) during recognition by alanyl-tRNA synthetase. RNA. 1996 Feb;2(2):105-9. Pubmed
  5. Buechter DD, Schimmel P: Minor groove recognition of the critical acceptor helix base pair by an appended module of a class II tRNA synthetase. Biochemistry. 1995 May 9;34(18):6014-9. Pubmed

13. Neutral amino acid transporter A

Pharmacological action: unknown

Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence

Organism class: human
UniProt ID: P43007 Link_out
Gene: SLC1A4 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Zhang Z, Papageorgiou G, Corrie JE, Grewer C: Pre-steady-state currents in neutral amino acid transporters induced by photolysis of a new caged alanine derivative. Biochemistry. 2007 Mar 27;46(12):3872-80. Epub 2007 Feb 21. Pubmed
  2. Takasaki C, Miura E, Watanabe M: Segmental and complementary expression of L-serine biosynthetic enzyme 3-phosphoglycerate dehydrogenase and neutral amino acid transporter ASCT1 in the mouse kidney. Biomed Res. 2007 Apr;28(2):61-9. Pubmed
  3. Zhang Z, Grewer C: The sodium-coupled neutral amino acid transporter SNAT2 mediates an anion leak conductance that is differentially inhibited by transported substrates. Biophys J. 2007 Apr 1;92(7):2621-32. Epub 2007 Jan 19. Pubmed
  4. Pinho MJ, Pinto V, Serrao MP, Jose PA, Soares-da-Silva P: Underexpression of the Na+-dependent neutral amino acid transporter ASCT2 in the spontaneously hypertensive rat kidney. Am J Physiol Regul Integr Comp Physiol. 2007 Jul;293(1):R538-47. Epub 2007 May 2. Pubmed
  5. Wu Y, Shen D, Chen Z, Clayton S, Vadgama JV: Taxol induced apoptosis regulates amino acid transport in breast cancer cells. Apoptosis. 2007 Mar;12(3):593-612. Epub 2006 Dec 29. 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, 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
Comments
Drug created on June 13, 2005 07:24 / Updated on February 08, 2013 16:19