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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2014-11-03 18:51:55 UTC
HMDB IDHMDB00641
Secondary Accession NumbersNone
Metabolite Identification
Common NameL-Glutamine
DescriptionGlutamine (Gln) is one of the 20 amino acids encoded by the standard genetic code. Its side chain is an amide; it is formed by replacing a side-chain hydroxyl of glutamic acid with an amine functional group. glutamine is found in foods high in proteins, such as fish, red meat, beans, and dairy products. glutamine is a supplement that is used in weightlifting, bodybuilding, endurance and other sports, as well as by those who suffer from muscular cramps or pain particularly elderly people. The main use of glutamine within the diet of either group is as a means of replenishing the body's stores of amino acids that have been used during exercise or everyday activities. Studies which are looking into problems with excessive consumption of glutamine thus far have proved inconclusive. However, normal supplementation is healthy mainly because glutamine is supposed to be supplemented after prolonged periods of exercise (for example, a workout or exercise in which amino acids are required for use) and replenishes amino acid stores; this being the main reason glutamine is recommended during fasting or for people who suffer from physical trauma, immune deficiencies, or cancer. There is a significant body of evidence that links glutamine-enriched diets with intestinal effects; aiding maintenance of gut barrier function, intestinal cell proliferation and differentiation, as well as generally reducing septic morbidity and the symptoms of Irritable Bowel Syndrome. The reason for such "cleansing" properties is thought to stem from the fact that the intestinal extraction rate of glutamine is higher than that for other amino acids, and is therefore thought to be the most viable option when attempting to alleviate conditions relating to the gastrointestinal tract. These conditions were discovered after comparing plasma concentration within the gut between glutamine-enriched and non glutamine-enriched diets. However, even though glutamine is thought to have "cleansing" properties and effects, it is unknown to what extent glutamine has clinical benefits, due to the varied concentrations of glutamine in varieties of food. It is also known that glutamine has various effects in reducing healing time after operations. Hospital waiting times after abdominal surgery are reduced by providing parenteral nutrition regimens containing amounts of glutamine to patients. Clinical trials have revealed that patients on supplementation regimes containing glutamine have improved nitrogen balances, generation of cysteinyl-leukotrienes from polymorphonuclear neutrophil granulocytes and improved lymphocyte recovery and intestinal permeability (in postoperative patients) - in comparison to those who had no glutamine within their dietary regime; all without any side-effects. (http://en.wikipedia.org/wiki/glutamine).
Structure
Thumb
Synonyms
  1. (2S)-2,5-diamino-5-oxopentanoate
  2. (2S)-2,5-diamino-5-oxopentanoic acid
  3. (2S)-2-amino-4-carbamoylbutanoate
  4. (2S)-2-amino-4-carbamoylbutanoic acid
  5. (S)-2,5-Diamino-5-oxopentanoate
  6. (S)-2,5-Diamino-5-oxopentanoic acid
  7. 2-Aminoglutaramic acid
  8. Cebrogen
  9. gamma-Glutamine
  10. Glavamin
  11. Glumin
  12. Glutamic acid 5-amide
  13. Glutamic acid amide
  14. Glutamine
  15. L-(+)-Glutamine
  16. L-2-Aminoglutaramic acid
  17. L-2-Aminoglutaramidic acid
  18. L-Glutamic acid 5-amide
  19. L-Glutamic acid gamma-amide
  20. L-Glutamid
  21. L-Glutamide
  22. L-Glutamin
  23. L-Glutamine
  24. L-Glutaminsaeure-5-amid
  25. Levoglutamid
  26. Levoglutamida
  27. Levoglutamide
  28. Levoglutamidum
  29. Levoglutamina
  30. Polyglutamine
  31. Stimulina
Chemical FormulaC5H10N2O3
Average Molecular Weight146.1445
Monoisotopic Molecular Weight146.069142196
IUPAC Name(2S)-2-amino-4-carbamoylbutanoic acid
Traditional NameL-glutamine
CAS Registry Number56-85-9
SMILES
N[C@@H](CCC(N)=O)C(O)=O
InChI Identifier
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
InChI KeyZDXPYRJPNDTMRX-VKHMYHEASA-N
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassAmino Acids, Peptides, and Analogues
ClassAmino Acids and Derivatives
Sub ClassAlpha Amino Acids and Derivatives
Other Descriptors
  • Aliphatic Acyclic Compounds
  • alpha-amino acid(ChEBI)
Substituents
  • Carboxamide Group
  • Carboxylic Acid
  • Primary Aliphatic Amine (Alkylamine)
  • Primary Carboxylic Acid Amide
Direct ParentAlpha Amino Acids and Derivatives
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Component of Alanine and aspartate metabolism
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Aminosugars metabolism
  • Component of D-Glutamine and D-glutamate metabolism
  • Component of Glutamate metabolism
  • Component of Nitrogen metabolism
  • Component of Peptidoglycan biosynthesis
  • Component of Purine metabolism
  • Energy source
  • Essential amino acid
  • Non-essential amino acid
  • RNA component
ApplicationNot Available
Cellular locations
  • Extracellular
  • Mitochondria
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point185 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility41.3 mg/mLYALKOWSKY,SH & DANNENFELSER,RM (1992)
LogP-3.64CHMELIK,J ET AL. (1991)
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
Polarizability13.85 Å3ChemAxon
Spectra
SpectraGC-MSMS/MSLC-MSMS1D NMR2D NMR
Biological Properties
Cellular Locations
  • Extracellular
  • Mitochondria
Biofluid Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Saliva
  • Urine
Tissue Location
  • Adipose Tissue
  • Fibroblasts
  • Gut
  • Intestine
  • Kidney
  • Muscle
  • Myelin
  • Neuron
  • Pancreas
  • Placenta
  • Prostate
  • Skeletal Muscle
  • Spleen
  • Stratum Corneum
  • Testes
Pathways
NameSMPDB LinkKEGG Link
Amino Sugar MetabolismSMP00045map00520
Ammonia RecyclingSMP00009map00910
Glutamate MetabolismSMP00072map00250
Phenylacetate MetabolismSMP00126map00360
Purine MetabolismSMP00050map00230
Pyrimidine MetabolismSMP00046map00240
Transcription/TranslationSMP00019Not Available
Urea CycleSMP00059map00330
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified492.6 +/- 93.6 uMAdult (>18 years old)Not SpecifiedNormal details
BloodDetected and Quantified542.5 (376.0-709.0) uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified490.6 +/- 84.3 uMAdult (>18 years old)MaleNormal details
BloodDetected and Quantified591.0 +/- 66.0 uMChildren (1-13 years old)FemaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified645.0 +/- 64.0 uMAdult (>18 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified578.0 +/- 85.0 uMAdult (>18 years old)FemaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified905.0 +/- 250.0 uMNewborn (0-30 days old)Not SpecifiedNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified600.0 +/- 70.0 uMChildren (1-13 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified586.0 (502.0-670.0) uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified510.4 +/- 118.2 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified432 +/- 204 uMNot SpecifiedBothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified570.0 +/- 240.0 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified623.6 +/- 71.6 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified518.0 +/- 81.0 uMAdult (>18 years old)MaleNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified425.0 +/- 70.5 uMAdult (>18 years old)FemaleNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified444.0 +/- 84.0 uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
Cerebrospinal Fluid (CSF)Detected and Quantified363.3 +/- 97.6 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified627.0 (482.0-772.0) uMAdult (>18 years old)BothNormal details
SalivaDetected and Quantified36.60 +/- 31.81 uMAdult (>18 years old)FemaleNormal details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)BothNormal details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected and Quantified8.4 +/- 2.7 uMAdult (>18 years old)Male
Normal
details
SalivaDetected and Quantified6.9 +/- 0.36 uMAdult (>18 years old)Male
Normal
details
SalivaDetected and Quantified6.6 +/- 2.1 uMAdult (>18 years old)Male
Normal
details
SalivaDetected and Quantified42.32 +/- 39.22 uMAdult (>18 years old)BothNormal
    • Dame, ZT. et al. ...
details
SalivaDetected and Quantified4.8 +/- 4.5 uMAdult (>18 years old)Male
Normal
details
SalivaDetected and Quantified>10 uMAdult (>18 years old)BothNormal details
UrineDetected and Quantified36.8 (14.5-59.2) umol/mmol creatinineAdult (>18 years old)BothNormal
    details
    UrineDetected but not QuantifiedNot ApplicableAdult (>18 years old)BothNormal details
    UrineDetected and Quantified33.98 umol/mmol creatinineAdult (>18 years old)MaleNormal
      • Shaykhutdinov RA,...
    details
    UrineDetected and Quantified118.96 +/- 89.94 umol/mmol creatinineInfant (0-1 year old)BothNormal details
    UrineDetected but not QuantifiedNot ApplicableAdult (>18 years old)Both
    Normal
    details
    UrineDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
    Normal
    details
    UrineDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
    Normal
    details
    UrineDetected and Quantified33.32 +/- 10.78 umol/mmol creatinineAdult (>18 years old)BothNormal details
    UrineDetected and Quantified39.9 (18.4-72.5) umol/mmol creatinineAdult (>18 years old)Both
    Normal
    details
    UrineDetected and Quantified37.2 (19.1-77.9) umol/mmol creatinineAdult (>18 years old)Both
    Normal
    details
    UrineDetected and Quantified20.0 (9.0-33.0) umol/mmol creatinineAdult (>18 years old)BothNormal details
    Abnormal Concentrations
    BiofluidStatusValueAgeSexConditionReferenceDetails
    BloodDetected and Quantified376.8 +/- 114.3 uMAdult (>18 years old)Not SpecifiedHeart Transplant details
    BloodDetected and Quantified650.0 +/- 98.0 uMAdult (>18 years old)MaleSchizophrenia details
    BloodDetected and Quantified673.0 +/- 96.0 uMAdult (>18 years old)FemaleSchizophrenia details
    BloodDetected and Quantified900.0 (700.0-1100.0) uMChildren (1-13 years old)BothCarbamoyl Phosphate Synthetase Deficiency details
    BloodDetected and Quantified228.34 +/- 12.00 uMElderly (>65 years old)BothAlzheimer's disease details
    BloodDetected and Quantified476.0 (455.0-498.0) uMAdult (>18 years old)Both
    Epilepsy
    details
    BloodDetected and Quantified495.0 (477.0-513.0) uMChildren (1-13 years old)Both
    Epilepsy
    details
    BloodDetected and Quantified611.0 (591.0-630.0) uMAdult (>18 years old)Both
    Epilepsy
    details
    Cerebrospinal Fluid (CSF)Detected and Quantified1875.3 +/- 285.8 uMChildren (1-13 years old)Not Specified
    Leukemia
    details
    Cerebrospinal Fluid (CSF)Detected and Quantified1061.0 +/- 230.2 uMChildren (1-13 years old)Not SpecifiedLeukemia details
    Cerebrospinal Fluid (CSF)Detected and Quantified902 uMNot SpecifiedNot Specifiedpropionic acidemia details
    Cerebrospinal Fluid (CSF)Detected and Quantified1146.6 +/- 10.6 uMAdult (>18 years old)BothAlzheimer's disease details
    Cerebrospinal Fluid (CSF)Detected and Quantified254.0 (152.0-356.0) uMAdult (>18 years old)BothAlzheimer's disease details
    SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)BothOral cancer details
    SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)FemaleBreast cancer details
    SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Not SpecifiedPancreatic cancer details
    SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Not SpecifiedPeriodontal diseases details
    SalivaDetected and Quantified22.30 +/- 10.19 uMAdult (>18 years old)MaleAlzheimer's disease details
    SalivaDetected and Quantified19.49 +/- 3.73 uMAdult (>18 years old)MaleFrontotemporal lobe dementia details
    SalivaDetected and Quantified48.74 +/- 50.79 uMAdult (>18 years old)BothLewy body disease details
    UrineDetected and Quantified1.17 +/- 0.49 umol/mmol creatinineAdult (>18 years old)BothAlzheimer's disease details
    UrineDetected and Quantified31.4 +/- 2.3 umol/mmol creatinineAdult (>18 years old)Both3-Hydroxy-3- methylglutaryl-CoA lyase (HL) deficency details
    UrineDetected and Quantified37.5 +/- 0.6 umol/mmol creatinineAdult (>18 years old)BothPropionic acidemia details
    UrineDetected and Quantified52.8 +/- 26.3 umol/mmol creatinineAdult (>18 years old)BothMaple syrup urine disease details
    UrineDetected and Quantified319.9 +/- 47.1 umol/mmol creatinineAdult (>18 years old)BothAminoaciduria details
    Associated Disorders and Diseases
    Disease References
    Alzheimer's disease
    1. Redjems-Bennani N, Jeandel C, Lefebvre E, Blain H, Vidailhet M, Gueant JL: Abnormal substrate levels that depend upon mitochondrial function in cerebrospinal fluid from Alzheimer patients. Gerontology. 1998;44(5):300-4. Pubmed: 9693263
    2. Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. Pubmed: 17031479
    Carbamoyl Phosphate Synthetase Deficiency
    1. MetaGene
    Epilepsy
    1. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. Pubmed: 14992292
    Schizophrenia
    1. Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. Pubmed: 2480613
    Leukemia
    1. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. Pubmed: 15911239
    Associated OMIM IDs
    DrugBank IDDB00130
    DrugBank Metabolite IDNot Available
    Phenol Explorer Compound IDNot Available
    Phenol Explorer Metabolite IDNot Available
    FoodDB IDFDB012164
    KNApSAcK IDC00001359
    Chemspider ID5746
    KEGG Compound IDC00064
    BioCyc IDGLN
    BiGG ID33714
    Wikipedia LinkL-Glutamine
    NuGOwiki LinkHMDB00641
    Metagene LinkHMDB00641
    METLIN ID5614
    PubChem Compound5961
    PDB IDGLN
    ChEBI ID18050
    References
    Synthesis ReferenceJiao, Qingcai; Qian, Shaosong; Chen, Ran; Wu, Xiaoyan. Synthesis of L-glutamine. Faming Zhuanli Shenqing Gongkai Shuomingshu (2005), 7 pp.
    Material Safety Data Sheet (MSDS)Download (PDF)
    General References
    1. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
    2. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. Pubmed: 12097436
    3. Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. Pubmed: 15627241
    4. Commodari F, Arnold DL, Sanctuary BC, Shoubridge EA: 1H NMR characterization of normal human cerebrospinal fluid and the detection of methylmalonic acid in a vitamin B12 deficient patient. NMR Biomed. 1991 Aug;4(4):192-200. Pubmed: 1931558
    5. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. Pubmed: 6696735
    6. Redjems-Bennani N, Jeandel C, Lefebvre E, Blain H, Vidailhet M, Gueant JL: Abnormal substrate levels that depend upon mitochondrial function in cerebrospinal fluid from Alzheimer patients. Gerontology. 1998;44(5):300-4. Pubmed: 9693263
    7. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. Pubmed: 6198473
    8. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. Pubmed: 15911239
    9. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. Pubmed: 12297216
    10. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. Pubmed: 14992292
    11. Frayn KN, Khan K, Coppack SW, Elia M: Amino acid metabolism in human subcutaneous adipose tissue in vivo. Clin Sci (Lond). 1991 May;80(5):471-4. Pubmed: 1851687
    12. Rutten EP, Engelen MP, Wouters EF, Schols AM, Deutz NE: Metabolic effects of glutamine and glutamate ingestion in healthy subjects and in persons with chronic obstructive pulmonary disease. Am J Clin Nutr. 2006 Jan;83(1):115-23. Pubmed: 16400059
    13. Szebenyi G, Morfini GA, Babcock A, Gould M, Selkoe K, Stenoien DL, Young M, Faber PW, MacDonald ME, McPhaul MJ, Brady ST: Neuropathogenic forms of huntingtin and androgen receptor inhibit fast axonal transport. Neuron. 2003 Sep 25;40(1):41-52. Pubmed: 14527432
    14. Wada A, Yoshida R, Oda K, Fukuba E, Uchida N, Kitagaki H: Acute encephalopathy associated with intravenous immunoglobulin therapy. AJNR Am J Neuroradiol. 2005 Oct;26(9):2311-5. Pubmed: 16219838
    15. Pennisi P, Gavrilova O, Setser-Portas J, Jou W, Santopietro S, Clemmons D, Yakar S, LeRoith D: Recombinant human insulin-like growth factor-I treatment inhibits gluconeogenesis in a transgenic mouse model of type 2 diabetes mellitus. Endocrinology. 2006 Jun;147(6):2619-30. Epub 2006 Mar 2. Pubmed: 16513827
    16. Avila J, Barbaro B, Gangemi A, Romagnoli T, Kuechle J, Hansen M, Shapiro J, Testa G, Sankary H, Benedetti E, Lakey J, Oberholzer J: Intra-ductal glutamine administration reduces oxidative injury during human pancreatic islet isolation. Am J Transplant. 2005 Dec;5(12):2830-7. Pubmed: 16302995
    17. Cooper AJ: Ammonia metabolism in normal and portacaval-shunted rats. Adv Exp Med Biol. 1990;272:23-46. Pubmed: 2103690
    18. Melis GC, Boelens PG, van der Sijp JR, Popovici T, De Bandt JP, Cynober L, van Leeuwen PA: The feeding route (enteral or parenteral) affects the plasma response of the dipetide Ala-Gln and the amino acids glutamine, citrulline and arginine, with the administration of Ala-Gln in preoperative patients. Br J Nutr. 2005 Jul;94(1):19-26. Pubmed: 16115328
    19. Choudry HA, Pan M, Karinch AM, Souba WW: Branched-chain amino acid-enriched nutritional support in surgical and cancer patients. J Nutr. 2006 Jan;136(1 Suppl):314S-8S. Pubmed: 16365105
    20. Coeffier M, Miralles-Barrachina O, Le Pessot F, Lalaude O, Daveau M, Lavoinne A, Lerebours E, Dechelotte P: Influence of glutamine on cytokine production by human gut in vitro. Cytokine. 2001 Feb 7;13(3):148-54. Pubmed: 11161457
    21. van der Hulst RR, von Meyenfeldt MF, Deutz NE, Soeters PB: Glutamine extraction by the gut is reduced in depleted [corrected] patients with gastrointestinal cancer. Ann Surg. 1997 Jan;225(1):112-21. Pubmed: 8998127
    22. 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: 1903318
    23. 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: 9488531
    24. 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: 10483898
    25. 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: 11408280

    Enzymes

    General function:
    Involved in metabolic process
    Specific function:
    Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
    Gene Name:
    GFPT2
    Uniprot ID:
    O94808
    Molecular weight:
    76929.885
    Reactions
    L-Glutamine + Fructose 6-phosphate → L-Glutamic acid + Glucosamine 6-phosphatedetails
    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: 17139284
    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: 17016423
    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: 15133036
    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: 15181156
    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: 11679416
    General function:
    Involved in metabolic process
    Specific function:
    Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
    Gene Name:
    GFPT1
    Uniprot ID:
    Q06210
    Molecular weight:
    78805.81
    Reactions
    L-Glutamine + Fructose 6-phosphate → L-Glutamic acid + Glucosamine 6-phosphatedetails
    General function:
    Involved in amidophosphoribosyltransferase activity
    Specific function:
    Not Available
    Gene Name:
    PPAT
    Uniprot ID:
    Q06203
    Molecular weight:
    57398.52
    Reactions
    5-Phosphoribosylamine + Pyrophosphate + L-Glutamic acid → L-Glutamine + Phosphoribosyl pyrophosphate + Waterdetails
    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: 17355124
    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: 17355125
    General function:
    Involved in 1-aminocyclopropane-1-carboxylate synthase activity
    Specific function:
    Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.
    Gene Name:
    CCBL1
    Uniprot ID:
    Q16773
    Molecular weight:
    47874.765
    Reactions
    L-Glutamine + Phenylpyruvic acid → 2-Keto-glutaramic acid + L-Phenylalaninedetails
    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: 17112493
    General function:
    Involved in nucleotide binding
    Specific function:
    Not Available
    Gene Name:
    QARS
    Uniprot ID:
    P47897
    Molecular weight:
    87797.97
    Reactions
    Adenosine triphosphate + L-Glutamine + tRNA(Gln) → Adenosine monophosphate + Pyrophosphate + L-glutaminyl-tRNA(Gln)details
    Adenosine triphosphate + L-Glutamine + tRNA(Gln) → Adenosine monophosphate + Pyrophosphate + Glutaminyl-tRNAdetails
    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: 17049867
    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: 16154153
    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: 17028132
    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: 16734422
    General function:
    Involved in asparagine synthase (glutamine-hydrolyzing) activity
    Specific function:
    Not Available
    Gene Name:
    ASNS
    Uniprot ID:
    P08243
    Molecular weight:
    62167.855
    Reactions
    Adenosine triphosphate + L-Aspartic acid + L-Glutamine + Water → Adenosine monophosphate + Pyrophosphate + L-Asparagine + L-Glutamic aciddetails
    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: 17397190
    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: 16164412
    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: 17329242
    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: 16870293
    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: 16931516
    General function:
    Involved in catalytic activity
    Specific function:
    Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.
    Gene Name:
    GMPS
    Uniprot ID:
    P49915
    Molecular weight:
    76714.79
    Reactions
    Adenosine triphosphate + Xanthylic acid + L-Glutamine + Water → Adenosine monophosphate + Pyrophosphate + Guanosine monophosphate + L-Glutamic aciddetails
    6-Thioxanthine 5'-monophosphate + Adenosine triphosphate + L-Glutamine + Water → 6-Thioguanosine monophosphate + Adenosine monophosphate + Pyrophosphate + L-Glutamic aciddetails
    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: 17159152
    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: 16142895
    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: 17408246
    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: 16809541
    General function:
    Involved in protein-glutamine gamma-glutamyltransferase activity
    Specific function:
    Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity). In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath.
    Gene Name:
    TGM3
    Uniprot ID:
    Q08188
    Molecular weight:
    76631.26
    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: 17139284
    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: 17016423
    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: 11093806
    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: 7733658
    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: 14508061
    General function:
    Involved in protein-glutamine gamma-glutamyltransferase activity
    Specific function:
    Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
    Gene Name:
    TGM2
    Uniprot ID:
    P21980
    Molecular weight:
    77328.21
    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: 16987813
    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: 17075129
    General function:
    Involved in glutamate-ammonia ligase activity
    Specific function:
    This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts.
    Gene Name:
    GLUL
    Uniprot ID:
    P15104
    Molecular weight:
    42064.15
    Reactions
    Adenosine triphosphate + L-Glutamic acid + Ammonia → ADP + Phosphoric acid + L-Glutaminedetails
    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: 16326016
    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: 16382338
    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: 16484281
    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: 16530878
    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: 16547651
    General function:
    Involved in protein-glutamine gamma-glutamyltransferase activity
    Specific function:
    Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
    Gene Name:
    F13A1
    Uniprot ID:
    P00488
    Molecular weight:
    83267.785
    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: 17139284
    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: 17016423
    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: 9603949
    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: 2913946
    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: 3390446
    General function:
    Involved in glutaminase activity
    Specific function:
    Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.
    Gene Name:
    GLS2
    Uniprot ID:
    Q9UI32
    Molecular weight:
    66322.225
    Reactions
    L-Glutamine + Water → L-Glutamic acid + Ammoniadetails
    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: 17078002
    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: 17159152
    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: 16142895
    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: 16263711
    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: 17267261
    General function:
    Involved in CTP synthase activity
    Specific function:
    Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
    Gene Name:
    CTPS1
    Uniprot ID:
    P17812
    Molecular weight:
    66689.9
    Reactions
    Adenosine triphosphate + Uridine triphosphate + L-Glutamine + Water → ADP + Phosphoric acid + Cytidine triphosphate + L-Glutamic aciddetails
    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: 16427816
    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: 17137369
    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: 17331943
    General function:
    Involved in protein-glutamine gamma-glutamyltransferase activity
    Specific function:
    Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes.
    Gene Name:
    TGM5
    Uniprot ID:
    O43548
    Molecular weight:
    71918.045
    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: 17139284
    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: 17016423
    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: 15038793
    General function:
    Involved in glutaminase activity
    Specific function:
    Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity.
    Gene Name:
    GLS
    Uniprot ID:
    O94925
    Molecular weight:
    65459.525
    Reactions
    L-Glutamine + Water → L-Glutamic acid + Ammoniadetails
    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: 16641247
    General function:
    Involved in protein-glutamine gamma-glutamyltransferase activity
    Specific function:
    Associated with the mammalian reproductive process. Catalyzes the cross-linking of proteins and the conjugation of polyamines to specific proteins in the seminal tract.
    Gene Name:
    TGM4
    Uniprot ID:
    P49221
    Molecular weight:
    77144.595
    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: 17139284
    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: 17016423
    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: 239698
    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: 849457
    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: 1361314
    General function:
    Involved in protein-glutamine gamma-glutamyltransferase activity
    Specific function:
    Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum.
    Gene Name:
    TGM1
    Uniprot ID:
    P22735
    Molecular weight:
    89786.14
    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: 17024410
    General function:
    Involved in protein-glutamine gamma-glutamyltransferase activity
    Specific function:
    Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins (By similarity).
    Gene Name:
    TGM6
    Uniprot ID:
    O95932
    Molecular weight:
    70515.44
    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: 17139284
    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: 17016423
    General function:
    Involved in protein-glutamine gamma-glutamyltransferase activity
    Specific function:
    Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
    Gene Name:
    TGM7
    Uniprot ID:
    Q96PF1
    Molecular weight:
    79940.615
    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: 17139284
    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: 17016423
    General function:
    Involved in catalytic activity
    Specific function:
    Not Available
    Gene Name:
    PFAS
    Uniprot ID:
    O15067
    Molecular weight:
    144733.165
    Reactions
    Adenosine triphosphate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-Glutamine + Water → ADP + Phosphoric acid + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-Glutamic aciddetails
    Adenosine triphosphate + 5'-Phosphoribosyl-N-formylglycinamide + L-Glutamine + Water → ADP + Phosphoric acid + Phosphoribosylformylglycineamidine + L-Glutamic aciddetails
    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: 17139284
    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: 17016423
    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: 2347042
    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: 3345200
    General function:
    Involved in carbon-nitrogen ligase activity, with glutamine as amido-N-donor
    Specific function:
    Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
    Gene Name:
    PET112
    Uniprot ID:
    O75879
    Molecular weight:
    61863.57
    Reactions
    Adenosine triphosphate + L-glutamyl-tRNA(Gln) + L-Glutamine → ADP + Phosphoric acid + L-glutaminyl-tRNA(Gln) + L-Glutamic aciddetails
    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: 17139284
    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: 17016423
    General function:
    Involved in NAD+ synthase (glutamine-hydrolyzing) activity
    Specific function:
    Not Available
    Gene Name:
    NADSYN1
    Uniprot ID:
    Q6IA69
    Molecular weight:
    79283.945
    Reactions
    Adenosine triphosphate + Nicotinic acid adenine dinucleotide + L-Glutamine + Water → Adenosine monophosphate + Pyrophosphate + NAD + L-Glutamic aciddetails
    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: 16954203
    General function:
    Involved in hydrolase activity
    Specific function:
    This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
    Gene Name:
    CAD
    Uniprot ID:
    P27708
    Molecular weight:
    242981.73
    Reactions
    Adenosine triphosphate + L-Glutamine + Carbonic acid + Water → ADP + Phosphoric acid + L-Glutamic acid + Carbamoyl phosphatedetails
    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: 17139284
    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: 17016423
    General function:
    Involved in CTP synthase activity
    Specific function:
    Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides.
    Gene Name:
    CTPS2
    Uniprot ID:
    Q9NRF8
    Molecular weight:
    65677.005
    Reactions
    Adenosine triphosphate + Uridine triphosphate + L-Glutamine + Water → ADP + Phosphoric acid + Cytidine triphosphate + L-Glutamic aciddetails
    General function:
    Involved in glycine N-acyltransferase activity
    Specific function:
    Acyltransferase which transfers an acyl group to the N-terminus of glutamine. Can use phenylacetyl-CoA as an acyl donor.
    Gene Name:
    GLYATL1
    Uniprot ID:
    Q969I3
    Molecular weight:
    35100.895
    Reactions
    Acyl-CoA + L-Glutamine → Coenzyme A + N-acyl-L-glutaminedetails
    General function:
    Involved in glutamate-ammonia ligase activity
    Specific function:
    ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
    Gene Name:
    PIG59
    Uniprot ID:
    A8YXX4
    Molecular weight:
    42064.1
    General function:
    Involved in carbon-nitrogen ligase activity, with glutamine as amido-N-donor
    Specific function:
    Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
    Gene Name:
    QRSL1
    Uniprot ID:
    Q9H0R6
    Molecular weight:
    57459.915
    Reactions
    Adenosine triphosphate + L-glutamyl-tRNA(Gln) + L-Glutamine → ADP + Phosphoric acid + L-glutaminyl-tRNA(Gln) + L-Glutamic aciddetails
    General function:
    Not Available
    Specific function:
    Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
    Gene Name:
    GATC
    Uniprot ID:
    O43716
    Molecular weight:
    15085.885
    Reactions
    Adenosine triphosphate + L-glutamyl-tRNA(Gln) + L-Glutamine → ADP + Phosphoric acid + L-glutaminyl-tRNA(Gln) + L-Glutamic aciddetails

    Transporters

    General function:
    Involved in sodium:dicarboxylate symporter activity
    Specific function:
    Has a broad substrate specificity, a preference for zwitterionic amino acids, and a sodium-dependence. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated amino acids, anionic amino acids, and cationic amino acids. Act as a cell surface receptor for feline endogenous virus RD114, baboon M7 endogenous virus and type D simian retroviruses
    Gene Name:
    SLC1A5
    Uniprot ID:
    Q15758
    Molecular weight:
    56597.6
    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: 16197915
    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: 16516348
    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: 17046712
    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: 17094966
    5. McGivan JD, Bungard CI: The transport of glutamine into mammalian cells. Front Biosci. 2007 Jan 1;12:874-82. Pubmed: 17127344
    General function:
    Involved in transport
    Specific function:
    Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. 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. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney
    Gene Name:
    SLC7A8
    Uniprot ID:
    Q9UHI5
    Molecular weight:
    58381.1
    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: 16249471
    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: 16308696
    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: 17273864
    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: 17504263
    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: 16785209
    General function:
    Amino acid transport and metabolism
    Specific function:
    Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission
    Gene Name:
    SLC38A3
    Uniprot ID:
    Q99624
    Molecular weight:
    55772.4
    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: 16249471
    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: 16517023
    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: 17561393
    General function:
    Involved in transmembrane transport
    Specific function:
    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
    Gene Name:
    SLC16A10
    Uniprot ID:
    Q8TF71
    Molecular weight:
    55492.1
    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: 11278508