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Identification
NameL-Glutamine
Accession NumberDB00130  (NUTR00026)
TypeSmall Molecule
GroupsApproved, Investigational, Nutraceutical
Description

A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from glutamic acid and ammonia. It is the principal carrier of nitrogen in the body and is an important energy source for many cells. [PubChem]

Structure
Thumb
Synonyms
SynonymLanguageCode
(2S)-2-amino-4-carbamoylbutanoic acidNot AvailableNot Available
(2S)-2,5-Diamino-5-oxopentanoic acidNot AvailableNot Available
(S)-2,5-diamino-5-oxopentanoic acidNot AvailableNot Available
Glutamic acid 5-amideNot AvailableNot Available
Glutamic acid amideNot AvailableNot Available
GLUTAMINENot AvailableNot Available
L-(+)-glutamineNot AvailableNot Available
L-2-aminoglutaramic acidNot AvailableNot Available
L-Glutamic acid gamma-amideNot AvailableNot Available
L-glutamic acid γ-amideNot AvailableNot Available
L-GlutaminNot AvailableNot Available
L-GlutamineNot AvailableNot Available
L-Glutaminsaeure-5-amidNot AvailableNot Available
L-Glutaminsäure-5-amidGermanNot Available
LevoglutamideNot AvailableNot Available
QNot AvailableNot Available
SaltsNot Available
Brand names
NameCompany
Earthlink Science Glutamine Chews ChocolateAmerifit
Glutamine ExpressGenetic Evolutionary Nutrition
Glutamine Fuel MegaTwinlab
Glutamine Fuel Powder Twinlab
L-Glutamine PowerChampion Nutrition
NutreStoreNot Available
Brand mixturesNot Available
Categories
CAS number56-85-9
WeightAverage: 146.1445
Monoisotopic: 146.069142196
Chemical FormulaC5H10N2O3
InChI KeyZDXPYRJPNDTMRX-VKHMYHEASA-N
InChI
InChI=1S/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1
IUPAC Name
(2S)-2-amino-4-carbamoylbutanoic acid
SMILES
N[C@@H](CCC(N)=O)C(O)=O
Mass Specshow(7.65 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; Primary Carboxylic Acid Amides; Polyamines; Carboxylic Acids; Enolates; Monoalkylamines
Substituentscarboxamide group; primary carboxylic acid amide; polyamine; enolate; carboxylic acid; amine; primary 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
IndicationUsed for nutritional supplementation, also for treating dietary shortage or imbalance.
PharmacodynamicsLike other amino acids, glutamine is biochemically important as a constituent of proteins. Glutamine is also crucial in nitrogen metabolism. Ammonia (formed by nitrogen fixation) is assimilated into organic compounds by converting glutamic acid to glutamine. The enzyme which accomplishes this is called glutamine synthetase. Glutamine can then be used as a nitrogen donor in the biosynthesis of many compounds, including other amino acids, purines, and pyrimidines.
Mechanism of actionSupplemental L-glutamine's possible immunomodulatory role may be accounted for in a number of ways. L-glutamine appears to play a major role in protecting the integrity of the gastrointestinal tract and, in particular, the large intestine. During catabolic states, the integrity of the intestinal mucosa may be compromised with consequent increased intestinal permeability and translocation of Gram-negative bacteria from the large intestine into the body. The demand for L-glutamine by the intestine, as well as by cells such as lymphocytes, appears to be much greater than that supplied by skeletal muscle, the major storage tissue for L-glutamine. L-glutamine is the preferred respiratory fuel for enterocytes, colonocytes and lymphocytes. Therefore, supplying supplemental L-glutamine under these conditions may do a number of things. For one, it may reverse the catabolic state by sparing skeletal muscle L-glutamine. It also may inhibit translocation of Gram-negative bacteria from the large intestine. L-glutamine helps maintain secretory IgA, which functions primarily by preventing the attachment of bacteria to mucosal cells. L-glutamine appears to be required to support the proliferation of mitogen-stimulated lymphocytes, as well as the production of interleukin-2 (IL-2) and interferon-gamma (IFN-gamma). It is also required for the maintenance of lymphokine-activated killer cells (LAK). L-glutamine can enhance phagocytosis by neutrophils and monocytes. It can lead to an increased synthesis of glutathione in the intestine, which may also play a role in maintaining the integrity of the intestinal mucosa by ameliorating oxidative stress. The exact mechanism of the possible immunomodulatory action of supplemental L-glutamine, however, remains unclear. It is conceivable that the major effect of L-glutamine occurs at the level of the intestine. Perhaps enteral L-glutamine acts directly on intestine-associated lymphoid tissue and stimulates overall immune function by that mechanism, without passing beyond the splanchnic bed.
AbsorptionAbsorption is efficient and occurs by an active transport mechanism
Volume of distributionNot Available
Protein bindingNot Available
Metabolism

Enterocytes, Hepatic

Route of eliminationNot Available
Half lifeNot Available
ClearanceNot Available
ToxicityDoses of L-glutamine up to 21 grams daily appear to be well tolerated. Reported adverse reactions are mainly gastrointestinal and not common. They include constipation and bloating. There is one older report of two hypomanic patients whose manic symptoms were exacerbated following the use of 2 to 4 grams daily of L-glutamine. The symptoms resolved when the L-glutamine was stopped. These patients were not rechallenged, nor are there any other reports of this nature.
Affected organisms
  • Humans and other mammals
Pathways
PathwayCategorySMPDB ID
Phenylacetate MetabolismMetabolicSMP00126
Mercaptopurine Metabolism PathwayDrug metabolismSMP00609
Nicotinate and Nicotinamide MetabolismMetabolicSMP00048
Canavan DiseaseDiseaseSMP00175
Salla Disease/Infantile Sialic Acid Storage DiseaseDiseaseSMP00240
Aspartate MetabolismMetabolicSMP00067
HypoacetylaspartiaDiseaseSMP00192
Tay-Sachs DiseaseDiseaseSMP00390
Sjogren Larsson SyndromeDiseaseSMP00217
Amino Sugar MetabolismMetabolicSMP00045
Sialuria or French Type SialuriaDiseaseSMP00216
G(M2)-Gangliosidosis: Variant B, Tay-sachs diseaseDiseaseSMP00534
Beta Ureidopropionase DeficiencyDiseaseSMP00172
Succinic semialdehyde dehydrogenase deficiencyDiseaseSMP00567
Ammonia RecyclingMetabolicSMP00009
Urea CycleMetabolicSMP00059
Ornithine Transcarbamylase Deficiency (OTC Deficiency)DiseaseSMP00205
HomocarnosinosisDiseaseSMP00385
Pyrimidine MetabolismMetabolicSMP00046
Argininosuccinic AciduriaDiseaseSMP00003
Dihydropyrimidinase DeficiencyDiseaseSMP00178
Carbamoyl Phosphate Synthetase DeficiencyDiseaseSMP00002
4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase DeficiencyDiseaseSMP00243
ArgininemiaDiseaseSMP00357
UMP Synthase Deiciency (Orotic Aciduria)DiseaseSMP00219
MNGIE (Mitochondrial Neurogastrointestinal Encephalopathy)DiseaseSMP00202
Glutamate MetabolismMetabolicSMP00072
Hyperinsulinism-Hyperammonemia SyndromeDiseaseSMP00339
Citrullinemia Type IDiseaseSMP00001
2-Hydroxyglutric Aciduria (D And L Form)DiseaseSMP00136
Warburg EffectMetabolicSMP00654
Molybdenium Cofactor DeficiencyDiseaseSMP00203
Purine Nucleoside Phosphorylase DeficiencyDiseaseSMP00210
Mitochondrial DNA depletion syndromeDiseaseSMP00536
Lesch-Nyhan Syndrome (LNS)DiseaseSMP00364
Xanthine Dehydrogenase Deficiency (Xanthinuria)DiseaseSMP00220
Xanthinuria type IIDiseaseSMP00513
Adenine phosphoribosyltransferase deficiency (APRT)DiseaseSMP00535
Purine MetabolismMetabolicSMP00050
Adenylosuccinate Lyase DeficiencyDiseaseSMP00167
Adenosine Deaminase DeficiencyDiseaseSMP00144
AICA-RibosiduriaDiseaseSMP00168
Myoadenylate deaminase deficiencyDiseaseSMP00537
Gout or Kelley-Seegmiller SyndromeDiseaseSMP00365
Xanthinuria type IDiseaseSMP00512
Azathioprine Action PathwayDrug actionSMP00427
Thioguanine Action PathwayDrug actionSMP00430
Mercaptopurine Action PathwayDrug actionSMP00428
SNP Mediated EffectsNot Available
SNP Mediated Adverse Drug ReactionsNot Available
ADMET
Predicted ADMET features
Property Value Probability
Human Intestinal Absorption - 0.5588
Blood Brain Barrier + 0.9604
Caco-2 permeable - 0.8957
P-glycoprotein substrate Non-substrate 0.7302
P-glycoprotein inhibitor I Non-inhibitor 0.964
P-glycoprotein inhibitor II Non-inhibitor 0.9919
Renal organic cation transporter Non-inhibitor 0.961
CYP450 2C9 substrate Non-substrate 0.845
CYP450 2D6 substrate Non-substrate 0.8496
CYP450 3A4 substrate Non-substrate 0.7544
CYP450 1A2 substrate Non-inhibitor 0.9583
CYP450 2C9 substrate Non-inhibitor 0.9741
CYP450 2D6 substrate Non-inhibitor 0.96
CYP450 2C19 substrate Non-inhibitor 0.9761
CYP450 3A4 substrate Non-inhibitor 0.8936
CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9932
Ames test Non AMES toxic 0.7849
Carcinogenicity Non-carcinogens 0.9136
Biodegradation Ready biodegradable 0.8854
Rat acute toxicity 1.2587 LD50, mol/kg Not applicable
hERG inhibition (predictor I) Weak inhibitor 0.9953
hERG inhibition (predictor II) Non-inhibitor 0.9828
Pharmacoeconomics
Manufacturers
  • Nutritional restart pharmaceutical lp
Packagers
Dosage formsNot Available
Prices
Unit descriptionCostUnit
L-glutamine crystals3.76USDg
Argiment packets2.43USDpacket
L-glutamine 500 mg tablet0.12USDtablet
Glutamic-500 tablet0.05USDtablet
Impact glutamine liquid0.05USDml
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents
CountryPatent NumberApprovedExpires (estimated)
United States52887031994-10-072011-10-07
Properties
Statesolid
Experimental Properties
PropertyValueSource
melting point185.5 dec °CPhysProp
water solubility4.13E+004 mg/L (at 25 °C)YALKOWSKY,SH & DANNENFELSER,RM (1992)
logP-3.64CHMELIK,J ET AL. (1991)
logS-0.55ADME Research, USCD
pKa2.17MERCK INDEX (1996)
Predicted Properties
PropertyValueSource
Water Solubility97.8ALOGPS
logP-3.3ALOGPS
logP-4ChemAxon
logS-0.17ALOGPS
pKa (Strongest Acidic)2.15ChemAxon
pKa (Strongest Basic)9.31ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area106.41 Å2ChemAxon
Rotatable Bond Count4ChemAxon
Refractivity33.11 m3·mol-1ChemAxon
Polarizability13.87 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Spectra
SpectraGC-MSMS/MSLC-MS1D NMR2D NMR
References
Synthesis Reference

Stephen Paul, “Novel preparation of fiber, L-glutamine and a soy derivative for the purpose of enhancement of isoflavone bioavailability.” U.S. Patent US20020076455, issued June 20, 2002.

US20020076455
General Reference
  1. Boza JJ, Dangin M, Moennoz D, Montigon F, Vuichoud J, Jarret A, Pouteau E, Gremaud G, Oguey-Araymon S, Courtois D, Woupeyi A, Finot PA, Ballevre O: Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers. Am J Physiol Gastrointest Liver Physiol. 2001 Jul;281(1):G267-74. Pubmed
  2. McAnena OJ, Moore FA, Moore EE, Jones TN, Parsons P: Selective uptake of glutamine in the gastrointestinal tract: confirmation in a human study. Br J Surg. 1991 Apr;78(4):480-2. Pubmed
  3. Morlion BJ, Stehle P, Wachtler P, Siedhoff HP, Koller M, Konig W, Furst P, Puchstein C: Total parenteral nutrition with glutamine dipeptide after major abdominal surgery: a randomized, double-blind, controlled study. Ann Surg. 1998 Feb;227(2):302-8. Pubmed
  4. Jian ZM, Cao JD, Zhu XG, Zhao WX, Yu JC, Ma EL, Wang XR, Zhu MW, Shu H, Liu YW: The impact of alanyl-glutamine on clinical safety, nitrogen balance, intestinal permeability, and clinical outcome in postoperative patients: a randomized, double-blind, controlled study of 120 patients. JPEN J Parenter Enteral Nutr. 1999 Sep-Oct;23(5 Suppl):S62-6. Pubmed
External Links
ResourceLink
KEGG DrugD00015
KEGG CompoundC00064
ChEBI18050
ChEMBLCHEMBL930
PharmGKBPA10090
IUPHAR723
Guide to Pharmacology723
HETGLN
PDRhealthhttp://www.pdrhealth.com/drug_info/nmdrugprofiles/nutsupdrugs/lgl_0125.shtml
WikipediaL-Glutamine
ATC CodesA16AA03
AHFS CodesNot Available
PDB Entries
FDA labelNot Available
MSDSshow(72.1 KB)
Interactions
Drug InteractionsNot Available
Food InteractionsNot Available

Targets

1. CTP synthase 1

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: antagonist

Components

Name UniProt ID Details
CTP synthase 1 P17812 Details

References:

  1. MacLeod TJ, Lunn FA, Bearne SL: The role of lysine residues 297 and 306 in nucleoside triphosphate regulation of E. coli CTP synthase: inactivation by 2’,3’-dialdehyde ATP and mutational analyses. Biochim Biophys Acta. 2006 Feb;1764(2):199-210. Epub 2005 Dec 27. Pubmed
  2. Taylor SD, Mirzaei F, Sharifi A, Bearne SL: Synthesis of methylene- and difluoromethylenephosphonate analogues of uridine-4-phosphate and 3-deazauridine-4-phosphate. J Org Chem. 2006 Dec 8;71(25):9420-30. Pubmed
  3. Fijolek A, Hofer A, Thelander L: Expression, purification, characterization, and in vivo targeting of trypanosome CTP synthetase for treatment of African sleeping sickness. J Biol Chem. 2007 Apr 20;282(16):11858-65. Epub 2007 Feb 28. Pubmed

2. Amidophosphoribosyltransferase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: product of

Components

Name UniProt ID Details
Amidophosphoribosyltransferase Q06203 Details

References:

  1. Jiang P, Pioszak AA, Ninfa AJ: Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli. Biochemistry. 2007 Apr 3;46(13):4117-32. Epub 2007 Mar 14. Pubmed
  2. Jiang P, Mayo AE, Ninfa AJ: Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate. Biochemistry. 2007 Apr 3;46(13):4133-46. Epub 2007 Mar 14. Pubmed

3. Glutamine synthetase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: product of

Components

Name UniProt ID Details
Glutamine synthetase P15104 Details

References:

  1. Mong JA, Blutstein T: Estradiol modulation of astrocytic form and function: implications for hormonal control of synaptic communication. Neuroscience. 2006;138(3):967-75. Epub 2005 Dec 2. Pubmed
  2. Rose C, Felipo V: Limited capacity for ammonia removal by brain in chronic liver failure: potential role of nitric oxide. Metab Brain Dis. 2005 Dec;20(4):275-83. Pubmed
  3. Miguel-Hidalgo JJ: Withdrawal from free-choice ethanol consumption results in increased packing density of glutamine synthetase-immunoreactive astrocytes in the prelimbic cortex of alcohol-preferring rats. Alcohol Alcohol. 2006 Jul-Aug;41(4):379-85. Epub 2006 Feb 16. Pubmed
  4. Chatauret N, Desjardins P, Zwingmann C, Rose C, Rao KV, Butterworth RF: Direct molecular and spectroscopic evidence for increased ammonia removal capacity of skeletal muscle in acute liver failure. J Hepatol. 2006 Jun;44(6):1083-8. Epub 2006 Jan 4. Pubmed
  5. Tan S, Evans R, Singh B: Herbicidal inhibitors of amino acid biosynthesis and herbicide-tolerant crops. Amino Acids. 2006 Mar;30(2):195-204. Epub 2006 Mar 20. Pubmed

Enzymes

1. Coagulation factor XIII A chain

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Coagulation factor XIII A chain P00488 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. Mitkevich OV, Shainoff JR, DiBello PM, Yee VC, Teller DC, Smejkal GB, Bishop PD, Kolotushkina IS, Fickenscher K, Samokhin GP: Coagulation factor XIIIa undergoes a conformational change evoked by glutamine substrate. Studies on kinetics of inhibition and binding of XIIIA by a cross-reacting antifibrinogen antibody. J Biol Chem. 1998 Jun 5;273(23):14387-91. Pubmed
  4. Wolff C, Lai CS: Fluorescence energy transfer detects changes in fibronectin structure upon surface binding. Arch Biochem Biophys. 1989 Feb 1;268(2):536-45. Pubmed
  5. Wolff C, Lai CS: Evidence that the two amino termini of plasma fibronectin are in close proximity: a fluorescence energy transfer study. Biochemistry. 1988 May 3;27(9):3483-7. Pubmed

2. Glutaminase kidney isoform, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Glutaminase kidney isoform, mitochondrial O94925 Details

References:

  1. Masson J, Darmon M, Conjard A, Chuhma N, Ropert N, Thoby-Brisson M, Foutz AS, Parrot S, Miller GM, Jorisch R, Polan J, Hamon M, Hen R, Rayport S: Mice lacking brain/kidney phosphate-activated glutaminase have impaired glutamatergic synaptic transmission, altered breathing, disorganized goal-directed behavior and die shortly after birth. J Neurosci. 2006 Apr 26;26(17):4660-71. Pubmed

3. Glutaminase liver isoform, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Glutaminase liver isoform, mitochondrial Q9UI32 Details

References:

  1. Sido B, Seel C, Hochlehnert A, Breitkreutz R, Droge W: Low intestinal glutamine level and low glutaminase activity in Crohn’s disease: a rational for glutamine supplementation? Dig Dis Sci. 2006 Dec;51(12):2170-9. Epub 2006 Nov 1. Pubmed
  2. Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I: Structure of a bacterial pyridoxal 5’-phosphate synthase complex. Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19284-9. Epub 2006 Dec 11. Pubmed
  3. Myers RS, Amaro RE, Luthey-Schulten ZA, Davisson VJ: Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase. Biochemistry. 2005 Sep 13;44(36):11974-85. Pubmed
  4. Benlloch M, Mena S, Ferrer P, Obrador E, Asensi M, Pellicer JA, Carretero J, Ortega A, Estrela JM: Bcl-2 and Mn-SOD antisense oligodeoxynucleotides and a glutamine-enriched diet facilitate elimination of highly resistant B16 melanoma cells by tumor necrosis factor-alpha and chemotherapy. J Biol Chem. 2006 Jan 6;281(1):69-79. Epub 2005 Nov 1. Pubmed
  5. Campos-Sandoval JA, Lopez de la Oliva AR, Lobo C, Segura JA, Mates JM, Alonso FJ, Marquez J: Expression of functional human glutaminase in baculovirus system: affinity purification, kinetic and molecular characterization. Int J Biochem Cell Biol. 2007;39(4):765-73. Epub 2006 Dec 21. Pubmed

4. Protein-glutamine gamma-glutamyltransferase 2

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Protein-glutamine gamma-glutamyltransferase 2 P21980 Details

References:

  1. Park SS, Kim JM, Kim DS, Kim IH, Kim SY: Transglutaminase 2 mediates polymer formation of I-kappaBalpha through C-terminal glutamine cluster. J Biol Chem. 2006 Nov 17;281(46):34965-72. Epub 2006 Sep 20. Pubmed
  2. Keresztessy Z, Csosz E, Harsfalvi J, Csomos K, Gray J, Lightowlers RN, Lakey JH, Balajthy Z, Fesus L: Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase 2. Protein Sci. 2006 Nov;15(11):2466-80. Pubmed

5. Protein-glutamine gamma-glutamyltransferase 5

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Protein-glutamine gamma-glutamyltransferase 5 O43548 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. Candi E, Paradisi A, Terrinoni A, Pietroni V, Oddi S, Cadot B, Jogini V, Meiyappan M, Clardy J, Finazzi-Agro A, Melino G: Transglutaminase 5 is regulated by guanine-adenine nucleotides. Biochem J. 2004 Jul 1;381(Pt 1):313-9. Pubmed

6. Protein-glutamine gamma-glutamyltransferase 6

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Protein-glutamine gamma-glutamyltransferase 6 O95932 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

7. Protein-glutamine gamma-glutamyltransferase K

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Protein-glutamine gamma-glutamyltransferase K P22735 Details

References:

  1. Boeshans KM, Mueser TC, Ahvazi B: A three-dimensional model of the human transglutaminase 1: insights into the understanding of lamellar ichthyosis. J Mol Model. 2007 Jan;13(1):233-46. Epub 2006 Sep 23. Pubmed

8. Protein-glutamine gamma-glutamyltransferase 4

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Protein-glutamine gamma-glutamyltransferase 4 P49221 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. Stenberg P, Curtis CG, Wing D, Tong YS, Credo RB, Gray A, Lorand L: Transamidase kinetics. Amide formation in the enzymic reactions of thiol esters with amines. Biochem J. 1975 Apr;147(1):155-63. Pubmed
  4. Mosher DF: Labeling of a major fibroblast surface protein (fibronectin) catalyzed by blood coagulation factor XIIa. Biochim Biophys Acta. 1977 Mar 28;491(1):205-10. Pubmed
  5. Coyne CP, Smith JE, Keeton K: Additive and synergistic pharmacologic inhibition of equine fibrinoligase (factor XIIIa*-like) biochemical activity. Am J Vet Res. 1992 Nov;53(11):2058-66. Pubmed

9. Protein-glutamine gamma-glutamyltransferase E

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Protein-glutamine gamma-glutamyltransferase E Q08188 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. Chen BS, Wang MR, Xu X, Cai Y, Xu ZX, Han YL, Wu M: Transglutaminase-3, an esophageal cancer-related gene. Int J Cancer. 2000 Dec 15;88(6):862-5. Pubmed
  4. Ikura K, Yu C, Nagao M, Sasaki R, Furuyoshi S, Kawabata N: Site-directed mutation in conserved anionic regions of guinea pig liver transglutaminase. Arch Biochem Biophys. 1995 Apr 20;318(2):307-13. Pubmed
  5. Ahvazi B, Steinert PM: A model for the reaction mechanism of the transglutaminase 3 enzyme. Exp Mol Med. 2003 Aug 31;35(4):228-42. Pubmed

10. Protein-glutamine gamma-glutamyltransferase Z

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Protein-glutamine gamma-glutamyltransferase Z Q96PF1 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

11. GMP synthase [glutamine-hydrolyzing]

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
GMP synthase [glutamine-hydrolyzing] P49915 Details

References:

  1. Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I: Structure of a bacterial pyridoxal 5’-phosphate synthase complex. Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19284-9. Epub 2006 Dec 11. Pubmed
  2. Myers RS, Amaro RE, Luthey-Schulten ZA, Davisson VJ: Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase. Biochemistry. 2005 Sep 13;44(36):11974-85. Pubmed
  3. Neuwirth M, Flicker K, Strohmeier M, Tews I, Macheroux P: Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase. Biochemistry. 2007 May 1;46(17):5131-9. Epub 2007 Apr 5. Pubmed
  4. Nakamura A, Yao M, Chimnaronk S, Sakai N, Tanaka I: Ammonia channel couples glutaminase with transamidase reactions in GatCAB. Science. 2006 Jun 30;312(5782):1954-8. Pubmed

12. Asparagine synthetase [glutamine-hydrolyzing]

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Asparagine synthetase [glutamine-hydrolyzing] P08243 Details

References:

  1. Li KK, Beeson WT 4th, Ghiviriga I, Richards NG: A convenient gHMQC-based NMR assay for investigating ammonia channeling in glutamine-dependent amidotransferases: studies of Escherichia coli asparagine synthetase B. Biochemistry. 2007 Apr 24;46(16):4840-9. Epub 2007 Mar 31. Pubmed
  2. Al Sarraj J, Vinson C, Thiel G: Regulation of asparagine synthetase gene transcription by the basic region leucine zipper transcription factors ATF5 and CHOP. Biol Chem. 2005 Sep;386(9):873-9. Pubmed
  3. Sheppard K, Akochy PM, Salazar JC, Soll D: The Helicobacter pylori amidotransferase GatCAB is equally efficient in glutamine-dependent transamidation of Asp-tRNAAsn and Glu-tRNAGln. J Biol Chem. 2007 Apr 20;282(16):11866-73. Epub 2007 Feb 28. Pubmed
  4. Barsch A, Carvalho HG, Cullimore JV, Niehaus K: GC-MS based metabolite profiling implies three interdependent ways of ammonium assimilation in Medicago truncatula root nodules. J Biotechnol. 2006 Dec 15;127(1):79-83. Epub 2006 Jun 21. Pubmed
  5. Reinert RB, Oberle LM, Wek SA, Bunpo P, Wang XP, Mileva I, Goodwin LO, Aldrich CJ, Durden DL, McNurlan MA, Wek RC, Anthony TG: Role of glutamine depletion in directing tissue-specific nutrient stress responses to L-asparaginase. J Biol Chem. 2006 Oct 20;281(42):31222-33. Epub 2006 Aug 24. Pubmed

13. Kynurenine--oxoglutarate transaminase 1

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Kynurenine--oxoglutarate transaminase 1 Q16773 Details

References:

  1. Fukushima T, Mitsuhashi S, Tomiya M, Iyo M, Hashimoto K, Toyo’oka T: Determination of kynurenic acid in human serum and its correlation with the concentration of certain amino acids. Clin Chim Acta. 2007 Feb;377(1-2):174-8. Epub 2006 Sep 30. Pubmed

14. Phosphoribosylformylglycinamidine synthase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Phosphoribosylformylglycinamidine synthase O15067 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. Jayaram HN, Lui MS, Plowman J, Pillwein K, Reardon MA, Elliott WL, Weber G: Oncolytic activity and mechanism of action of a novel L-cysteine derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate) monohydrochloride. Cancer Chemother Pharmacol. 1990;26(2):88-92. Pubmed
  4. Prajda N, Natsumeda Y, Ikegami T, Reardon MA, Szondy S, Hashimoto Y, Emrani J, Weber G: Enzymic programs of rat bone marrow and the impact of acivicin and tiazofurin. Biochem Pharmacol. 1988 Mar 1;37(5):875-80. Pubmed

15. Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial O75879 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

16. Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2 O94808 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. Hu Y, Riesland L, Paterson AJ, Kudlow JE: Phosphorylation of mouse glutamine-fructose-6-phosphate amidotransferase 2 (GFAT2) by cAMP-dependent protein kinase increases the enzyme activity. J Biol Chem. 2004 Jul 16;279(29):29988-93. Epub 2004 May 7. Pubmed
  4. Zitzler J, Link D, Schafer R, Liebetrau W, Kazinski M, Bonin-Debs A, Behl C, Buckel P, Brinkmann U: High-throughput functional genomics identifies genes that ameliorate toxicity due to oxidative stress in neuronal HT-22 cells: GFPT2 protects cells against peroxide. Mol Cell Proteomics. 2004 Aug;3(8):834-40. Epub 2004 Jun 4. Pubmed
  5. DeHaven JE, Robinson KA, Nelson BA, Buse MG: A novel variant of glutamine: fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle. Diabetes. 2001 Nov;50(11):2419-24. Pubmed

17. CAD protein

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
CAD protein P27708 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

18. Glutamine--tRNA ligase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Glutamine--tRNA ligase P47897 Details

References:

  1. Balg C, Blais SP, Bernier S, Huot JL, Couture M, Lapointe J, Chenevert R: Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases. Bioorg Med Chem. 2007 Jan 1;15(1):295-304. Epub 2006 Sep 29. Pubmed
  2. Fuchs BC, Bode BP: Stressing out over survival: glutamine as an apoptotic modulator. J Surg Res. 2006 Mar;131(1):26-40. Epub 2005 Sep 8. Pubmed
  3. Yamasaki S, Nakamura S, Terada T, Shimizu K: Mechanism of the difference in the binding affinity of E. coli tRNAGln to glutaminyl-tRNA synthetase caused by noninterface nucleotides in variable loop. Biophys J. 2007 Jan 1;92(1):192-200. Epub 2006 Oct 6. Pubmed
  4. Uter NT, Perona JJ: Active-site assembly in glutaminyl-tRNA synthetase by tRNA-mediated induced fit. Biochemistry. 2006 Jun 6;45(22):6858-65. Pubmed

19. Glutamine-dependent NAD(+) synthetase

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Glutamine-dependent NAD(+) synthetase Q6IA69 Details

References:

  1. Wojcik M, Seidle HF, Bieganowski P, Brenner C: Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste. J Biol Chem. 2006 Nov 3;281(44):33395-402. Epub 2006 Sep 5. 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, 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. Sodium-coupled neutral amino acid transporter 3

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Sodium-coupled neutral amino acid transporter 3 Q99624 Details

References:

  1. Umapathy NS, Li W, Mysona BA, Smith SB, Ganapathy V: Expression and function of glutamine transporters SN1 (SNAT3) and SN2 (SNAT5) in retinal Muller cells. Invest Ophthalmol Vis Sci. 2005 Nov;46(11):3980-7. Pubmed
  2. Conti F, Melone M: The glutamine commute: lost in the tube? Neurochem Int. 2006 May-Jun;48(6-7):459-64. Epub 2006 Mar 3. Pubmed
  3. Gajewski M, Seaver B, Esslinger CS: Design, synthesis, and biological activity of novel triazole amino acids used to probe binding interactions between ligand and neutral amino acid transport protein SN1. Bioorg Med Chem Lett. 2007 Aug 1;17(15):4163-6. Epub 2007 May 23. Pubmed

3. Neutral amino acid transporter B(0)

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Neutral amino acid transporter B(0) Q15758 Details

References:

  1. Bungard CI, McGivan JD: Identification of the promoter elements involved in the stimulation of ASCT2 expression by glutamine availability in HepG2 cells and the probable involvement of FXR/RXR dimers. Arch Biochem Biophys. 2005 Nov 15;443(1-2):53-9. Epub 2005 Sep 15. Pubmed
  2. Gegelashvili M, Rodriguez-Kern A, Pirozhkova I, Zhang J, Sung L, Gegelashvili G: High-affinity glutamate transporter GLAST/EAAT1 regulates cell surface expression of glutamine/neutral amino acid transporter ASCT2 in human fetal astrocytes. Neurochem Int. 2006 May-Jun;48(6-7):611-5. Epub 2006 Mar 3. Pubmed
  3. Oppedisano F, Pochini L, Galluccio M, Indiveri C: The glutamine/amino acid transporter (ASCT2) reconstituted in liposomes: transport mechanism, regulation by ATP and characterization of the glutamine/glutamate antiport. Biochim Biophys Acta. 2007 Feb;1768(2):291-8. Epub 2006 Sep 16. Pubmed
  4. Dun Y, Mysona B, Itagaki S, Martin-Studdard A, Ganapathy V, Smith SB: Functional and molecular analysis of D-serine transport in retinal Muller cells. Exp Eye Res. 2007 Jan;84(1):191-9. Epub 2006 Nov 13. Pubmed
  5. McGivan JD, Bungard CI: The transport of glutamine into mammalian cells. Front Biosci. 2007 Jan 1;12:874-82. Pubmed

4. Large neutral amino acids transporter small subunit 2

Kind: protein

Organism: Human

Pharmacological action: unknown

Actions: substrate

Components

Name UniProt ID Details
Large neutral amino acids transporter small subunit 2 Q9UHI5 Details

References:

  1. Umapathy NS, Li W, Mysona BA, Smith SB, Ganapathy V: Expression and function of glutamine transporters SN1 (SNAT3) and SN2 (SNAT5) in retinal Muller cells. Invest Ophthalmol Vis Sci. 2005 Nov;46(11):3980-7. Pubmed
  2. Kirchhoff P, Dave MH, Remy C, Kosiek O, Busque SM, Dufner M, Geibel JP, Verrey F, Wagner CA: An amino acid transporter involved in gastric acid secretion. Pflugers Arch. 2006 Mar;451(6):738-48. Epub 2005 Nov 25. Pubmed
  3. Ramadan T, Camargo SM, Herzog B, Bordin M, Pos KM, Verrey F: Recycling of aromatic amino acids via TAT1 allows efflux of neutral amino acids via LAT2-4F2hc exchanger. Pflugers Arch. 2007 Jun;454(3):507-16. Epub 2007 Feb 2. Pubmed
  4. 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
  5. Chubb S, Kingsland AL, Broer A, Broer S: Mutation of the 4F2 heavy-chain carboxy terminus causes y+ LAT2 light-chain dysfunction. Mol Membr Biol. 2006 May-Jun;23(3):255-67. Pubmed

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Drug created on June 13, 2005 07:24 / Updated on September 16, 2013 17:08