DrugBank: L-Threonine (DB00156)

targets (3) transporters (1)

Identification

Name

L-Threonine

Accession Number

DB00156 (NUTR00057)

Type

small molecule

Groups

approved, nutraceutical

Description

An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins. [PubChem]

Structure

Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure

Synonyms

(S)-Threonine
[R-(R,S)]-2-Amino-3-hydroxybutanoic acid
2-Amino-3-hydroxybutyric acid
L-(-)-Threonine
Threonin
Threonine

Salts

Not Available

Brand names

Not Available

Brand mixtures

Not Available

Categories

Dietary supplement
Micronutrient
Essential Amino Acids

CAS number

72-19-5

Weight

Average: 119.1192
Monoisotopic: 119.058243159

Chemical Formula

C₄H₉NO₃

InChI Key

InChIKey=AYFVYJQAPQTCCC-GBXIJSLDSA-N

InChI

InChI=1S/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)/t2-,3+/m1/s1

Plain Text

IUPAC Name

(2S,3R)-2-amino-3-hydroxybutanoic acid

SMILES

C[C@@H](O)[C@H](N)C(O)=O

Plain Text

Mass Spec

show (8.11 KB)

Taxonomy

Kingdom

Organic

Classes

Amino Acids
Carboxylic Acids and Derivatives

Substructures

Amino Acids
Hydroxy Compounds
Acetates
Aliphatic and Aryl Amines
Carboxylic Acids and Derivatives
Amino Alcohols
Alcohols and Polyols

Pharmacology

Indication

L-Threonine makes up collagen, elastin, and enamel protein. It aids proper fat metabolism in the liver, helps the digestive and intestinal tracts function more smoothly, and assists in metabolism and assimilation.

Pharmacodynamics

L-Threonine is an essential amino acid that helps to maintain the proper protein balance in the body. It is important for the formation of collagen, elastin, and tooth enamel, and aids liver and lipotropic function when combined with aspartic acid and methionine.

Mechanism of action

L-Threonine is a precursor to the amino acids glycine and serine. It acts as a lipotropic in controlling fat build-up in the liver. May help combat mental illness and may be very useful in indigestion and intestinal malfunctions. Also, threonine prevents excessive liver fat. Nutrients are more readily absorbed when threonine is present.

Absorption

Not Available

Volume of distribution

Not Available

Protein binding

Not Available

Metabolism

Hepatic

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

Hospira Inc.
Novis PR Inc.
Spectrum Pharmaceuticals
V Sab Medical Labs Inc.

Dosage forms

Not Available

Prices

Unit description	Cost	Unit
L-threonine crystal	4.57 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	256 dec °C	PhysProp
water solubility	9.7E+004 mg/L (at 25 °C)	YALKOWSKY,SH & DANNENFELSER,RM (1992)
logP	-2.94	HANSCH,C ET AL. (1995)
logS	-0.09	ADME Research, USCD
pKa	5.60	Not Available

Predicted Properties

Property	Value	Source
water solubility	4.77e+02 g/l	ALOGPS
logP	-3	ALOGPS
logP	-3.5	ChemAxon
logS	0.6	ALOGPS
pKa (strongest acidic)	2.21	ChemAxon
pKa (strongest basic)	9	ChemAxon
physiological charge	0	ChemAxon
hydrogen acceptor count	4	ChemAxon
hydrogen donor count	3	ChemAxon
polar surface area	83.55	ChemAxon
rotatable bond count	2	ChemAxon
refractivity	26.46	ChemAxon
polarizability	11.12	ChemAxon

References

Synthesis Reference

Not Available

General Reference

Not Available

External Links

Resource	Link
KEGG Drug	D00041
KEGG Compound	C00188
PubChem Compound	6288
PubChem Substance	46506798
ChemSpider	6051
ChEBI	16857
ChEMBL	16857
PharmGKB	PA451673
HET	THR
Wikipedia	http://en.wikipedia.org/wiki/L-Threonine

ATC Codes

Not Available

AHFS Codes

Not Available

PDB Entries

1NYR

FDA label

Not Available

MSDS

show (72.6 KB)

Interactions

Drug Interactions

Not Available

Food Interactions

Not Available

Targets
1. Threonine synthase-like 1 Pharmacological action: unknown Organism class: human UniProt ID: Q8IYQ7 Gene: THNSL1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed 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 2. Threonyl-tRNA synthetase, cytoplasmic Pharmacological action: unknown Organism class: human UniProt ID: P26639 Gene: TARS Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed 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 Torres-Larios A, Sankaranarayanan R, Rees B, Dock-Bregeon AC, Moras D: Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase. J Mol Biol. 2003 Aug 1;331(1):201-11. Pubmed Ruan B, Bovee ML, Sacher M, Stathopoulos C, Poralla K, Francklyn CS, Soll D: A unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases. J Biol Chem. 2005 Jan 7;280(1):571-7. Epub 2004 Oct 26. Pubmed Cusack S, Yaremchuk A, Krikliviy I, Tukalo M: tRNA(Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase. Structure. 1998 Jan 15;6(1):101-8. Pubmed 3. Threonyl-tRNA synthetase, mitochondrial Pharmacological action: unknown ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr) Organism class: human UniProt ID: Q9BW92 Gene: TARS2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Caillet J, Graffe M, Eyermann F, Romby P, Springer M: Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype. J Bacteriol. 2007 Oct;189(19):6839-48. Epub 2007 Jul 20. Pubmed

Targets

1. Threonine synthase-like 1

Pharmacological action: unknown
Organism class: human
UniProt ID: Q8IYQ7 Link_out

Gene: THNSL1 Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
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

2. Threonyl-tRNA synthetase, cytoplasmic

Pharmacological action: unknown
Organism class: human
UniProt ID: P26639 Link_out

Gene: TARS Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
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
Torres-Larios A, Sankaranarayanan R, Rees B, Dock-Bregeon AC, Moras D: Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase. J Mol Biol. 2003 Aug 1;331(1):201-11. Pubmed
Ruan B, Bovee ML, Sacher M, Stathopoulos C, Poralla K, Francklyn CS, Soll D: A unique hydrophobic cluster near the active site contributes to differences in borrelidin inhibition among threonyl-tRNA synthetases. J Biol Chem. 2005 Jan 7;280(1):571-7. Epub 2004 Oct 26. Pubmed
Cusack S, Yaremchuk A, Krikliviy I, Tukalo M: tRNA(Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase. Structure. 1998 Jan 15;6(1):101-8. Pubmed

3. Threonyl-tRNA synthetase, mitochondrial

Pharmacological action: unknown

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)

Organism class: human
UniProt ID: Q9BW92 Link_out

Gene: TARS2 Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Caillet J, Graffe M, Eyermann F, Romby P, Springer M: Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype. J Bacteriol. 2007 Oct;189(19):6839-48. Epub 2007 Jul 20. 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 Gene: SLC16A10 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: 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

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:

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