Glutamine 500mg capsules
Requires a prescription from a doctor or prescriber
A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes.
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Safety monitoring data
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4 branded products available
Therapeutically similar medicines
Similarity based on WHO Anatomical Therapeutic Chemical (ATC) classification and NHS BNF section grouping. Source data: NHS dm+d via TRUD (OGL v3.0), WHO ATC/DDD Index.
NHS prescribing volume and spending trends
Clinical guidelines and formulary information
British National Formulary
Glutamine
Source: British National Formulary, NICE. Joint Formulary Committee. Contains public sector information licensed under the Open Government Licence v3.0.
NICE clinical guidance(1)
Source: National Institute for Health and Care Excellence (NICE). Contains public sector information licensed under the Open Government Licence v3.0.
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Supply & product information
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Codes for healthcare professionals and prescribing systems
These codes are used by healthcare IT systems and prescribers to identify this medicine.
NHS UK identifiers
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SNOMED CT and dm+d codes from NHS TRUD (Technology Reference data Update Distribution), licensed under the Open Government Licence v3.0. BNF codes from NHS Business Services Authority (NHSBSA). ATC codes from the WHO Collaborating Centre for Drug Statistics Methodology (whocc.no).
Active and completed clinical studies from ClinicalTrials.gov
Source: ClinicalTrials.gov, a database of the U.S. National Library of Medicine (NLM), National Institutes of Health (NIH). Data accessed via ClinicalTrials.gov API v2. Trial information is provided for research purposes and does not constitute medical advice.
Pharmacology and chemical data from DrugBank
Key facts
Drug status
Approved
Major interactions
None known
Half-life
1 h
Mechanism
Supplemental L-glutamine's possible immunomodulatory role may be accounted for in a number of ways.
Food interactions
1 warning
Human targets
3 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Absorption
30 minutes
Half-life
1 h
Volume of distribution
200 mL
Metabolism
Elimination
Pharmacokinetic data: DrugBank · CC BY-NC 4.0
Used to reduce the acute complications of sickle cell disease in adult and pediatric patients 5 years of age and older [FDA Label].
Known interactions with other medications. Always consult a healthcare professional.
Showing 1 of 1 interactions
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.
The most common adverse effects observed in clinical trials of Endari were constipation (21%), nausea (19%), headache (18%), abdominal pain (17%), cough (16%), extremity pain (13%), back pain (12%), and chest pain (12%) [FDA Label].
The exact mechanism of L-glutamine's effect on NAD redox potential is unknown but is thought to involve increased amounts of reduced glutathione made available by glutamine supplementation [FDA Label]. This improvement in redox potential reduces the amount of oxidative damage which sickle red blood cells are more susceptible to. The reduction in cellular damage is thought to reduce chronic hemolysis and vaso-occlusive events.
L-glutamine improves nicotinamide adenine dinucleotide (NAD) redox potential [FDA Label].
How the body processes this drug — absorption, distribution, metabolism, and elimination
Proteins and enzymes this drug interacts with in the body
PMID:16267323 PMID:30158707 PMID:36289327
Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Plays a key role in ammonium detoxification during erythropoiesis: the glutamine synthetase activity is required to remove ammonium generated by porphobilinogen deaminase (HMBS) during heme biosynthesis to prevent ammonium accumulation and oxidative stress (By similarity). Essential for proliferation of fetal skin fibroblasts .
PMID:18662667
Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation .
PMID:30158707
May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ .
PMID:30158707
Plays a role in ribosomal 40S subunit biogenesis .
PMID:26711351
Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2 PMID:36289327
Enzymes involved in drug metabolism — important for understanding drug interactions
Proteins that transport this drug across cell membranes
PMID:10891391 PMID:20599747
The transport is elctrogenic, pH dependent and driven by the Na(+) electrochemical gradient .
PMID:10891391
Participates in the astroglia-derived glutamine transport into GABAergic interneurons for neurotransmitter GABA de novo synthesis (By similarity). May also contributes to amino acid transport in placental trophoblasts .
PMID:20599747
Also regulates synaptic plasticity PMID:12388062
PMID:10930503 PMID:15774260 PMID:15922329 PMID:16621798
The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier .
PMID:10930503 PMID:15774260
May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity).
Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity)
PMID:10823827
Mainly participates in the glutamate-GABA-glutamine cycle in brain where it transports L-glutamine from astrocytes in the intercellular space for the replenishment of both neurotransmitters glutamate and gamma-aminobutyric acid (GABA) in neurons and also functions as the major influx transporter in ganglion cells mediating the uptake of glutamine (By similarity). The transport activity is specific for L-glutamine, L-histidine and L-asparagine .
PMID:10823827
The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+) (By similarity). The transport is pH dependent, saturable, Li(+) tolerant and functions in both direction depending on the concentration gradients of its substrates and cotransported ions .
PMID:10823827
Also mediates an amino acid-gated H(+) conductance that is not stoichiometrically coupled to the amino acid transport but which influences the ionic gradients that drive the amino acid transport (By similarity).
In addition, may play a role in nitrogen metabolism, amino acid homeostasis, glucose metabolism and renal ammoniagenesis (By similarity)
PMID:17094966 PMID:23756778 PMID:26492990 PMID:29872227 PMID:34741534 PMID:8702519
The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way.
Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation .
PMID:23756778 PMID:24953180
The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system .
PMID:32733894
Can transport D-amino acids.
Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons .
PMID:17094966
Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development PMID:10708449 PMID:23492904
PMID:10446133
Transports non-alpha-amino acids such as beta-alanine with low affinity, and has a higher affinity for dipolar and cationic amino acids such as leucine and lysine .
PMID:18599538
Can also transport carnitine, butirylcarnitine and propionylcarnitine coupled to the transmembrane gradients of Na(+) and Cl(-) PMID:17855766
PMID:10080182 PMID:10655553 PMID:14603368 PMID:15756301 PMID:15776427 PMID:17329401 PMID:9829974 PMID:9878049
Also mediates arginine transport in non-polarized cells, such as monocytes, and is essential for the correct function of these cells .
PMID:15280038 PMID:31705628
The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (By similarity). In vitro, Na(+) and Li(+), but also H(+), are cotransported with the neutral amino acids (By similarity)
PMID:10903140 PMID:11311135 PMID:14603368 PMID:15756301 PMID:16785209 PMID:17329401 PMID:19562367 PMID:31705628 PMID:9829974
Also exchanges L-arginine with L-lysine in a sodium-independent manner .
PMID:10903140
The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 .
PMID:10903140
Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration (By similarity). May mediate transport of ornithine in retinal pigment epithelial (RPE) cells .
PMID:17197568
May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte (By similarity)
PMID:10049700 PMID:10574970 PMID:11557028 PMID:11564694 PMID:12117417 PMID:12225859 PMID:15769744 PMID:18262359 PMID:25998567 PMID:30867591 PMID:9751058
The heterodimer with SLC3A2 mediates the uptake of L-DOPA (By similarity). Functions as an amino acid exchanger .
PMID:11557028 PMID:12117417 PMID:12225859 PMID:30867591
May play a role in the transport of L-DOPA across the blood-brain barrier (By similarity). May act as the major transporter of tyrosine in fibroblasts (Probable).
May mediate blood-to-retina L-leucine transport across the inner blood-retinal barrier (By similarity). Can mediate the transport of thyroid hormones diiodothyronine (T2), triiodothyronine (T3) and thyroxine (T4) across the cell membrane .
PMID:11564694
When associated with LAPTM4B, the heterodimer formed by SLC3A2 and SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation .
PMID:25998567
Involved in the uptake of toxic methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes .
PMID:12117417
Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the membrane PMID:15769744
PMID:10391915 PMID:11311135 PMID:11847106 PMID:12716892 PMID:15081149 PMID:15918515 PMID:29355479 PMID:33298890 PMID:34848541
Has relatively symmetrical selectivities but strongly asymmetrical substrate affinities at both the intracellular and extracellular sides of the transporter .
PMID:11847106
This asymmetry allows SLC7A8 to regulate intracellular amino acid pools (mM concentrations) by exchange with external amino acids (uM concentration range), equilibrating the relative concentrations of different amino acids across the plasma membrane instead of mediating their net uptake .
PMID:10391915 PMID:11847106
May play an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney .
PMID:12716892
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 .
PMID:12117417
Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane .
PMID:15769744
Imports the thyroid hormone diiodothyronine (T2) and to a smaller extent triiodothyronine (T3) but not rT 3 or thyroxine (T4) (By similarity). Mediates the uptake of L-DOPA (By similarity).
May participate in auditory function (By similarity)
PMID:16825196 PMID:32494597 PMID:32817565 PMID:8663357
Has system b(0,+)-like activity with high affinity for extracellular cationic amino acids and L-cystine and lower affinity for intracellular neutral amino acids .
PMID:16825196 PMID:32494597 PMID:8663357
Substrate exchange is driven by high concentration of intracellular neutral amino acids and the intracellular reduction of L-cystine to L-cysteine .
PMID:8663357
Required for reabsorption of L-cystine and dibasic amino acids across the brush border membrane in renal proximal tubules
PMID:11827462 PMID:18337592 PMID:28754537
Mediates both uptake and efflux of 3,5,3'-triiodothyronine (T3) and 3,5,3',5'-tetraiodothyronine (T4) with high affinity, suggesting a role in the homeostasis of thyroid hormone levels .
PMID:18337592
Responsible for low affinity bidirectional transport of the aromatic amino acids, such as phenylalanine, tyrosine, tryptophan and L-3,4-dihydroxyphenylalanine (L-dopa) .
PMID:11827462 PMID:28754537
Plays an important role in homeostasis of aromatic amino acids (By similarity)
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ATC A16AA03
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
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Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Linked compound data from DrugBank Open Data (CC BY-NC 4.0)
L-Glutamine
Matched from: Glutamine
Additional database identifiers
ChemSpider
5746
BindingDB
18121
PDB
GLN
Guide to Pharmacology
723
ZINC
ZINC000001532526
HUGO Gene Nomenclature Committee (HGNC)
HGNC:2519
GenAtlas
CTPS
GeneCards
CTPS1
GenBank Gene Database
X52142
GenBank Protein Database
30293
Guide to Pharmacology
3215
UniProt Accession
PYRG1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9238
GenAtlas
PPAT
GeneCards
PPAT
GenBank Gene Database
D13757
GenBank Protein Database
219459
UniProt Accession
PUR1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4341
GenAtlas
GLUL
GeneCards
GLUL
GenBank Gene Database
Y00387
GenBank Protein Database
31833
UniProt Accession
GLNA_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:3531
GenAtlas
F13A1
GeneCards
F13A1
GenBank Gene Database
M22001
GenBank Protein Database
182309
UniProt Accession
F13A_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4331
GenAtlas
GLS
GeneCards
GLS
GenBank Gene Database
AF158555
GenBank Protein Database
5690372
Guide to Pharmacology
2891
UniProt Accession
GLSK_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:29570
GenAtlas
GLS2
GeneCards
GLS2
GenBank Gene Database
AF110330
GenBank Protein Database
6650606
UniProt Accession
GLSL_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11778
GenAtlas
TGM2
GeneCards
TGM2
GenBank Gene Database
M55153
GenBank Protein Database
339521
Guide to Pharmacology
3015
UniProt Accession
TGM2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11781
GenAtlas
TGM5
GeneCards
TGM5
GenBank Gene Database
AF035960
GenBank Protein Database
2895530
UniProt Accession
TGM5_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:16255
GenAtlas
TGM6
GeneCards
TGM6
GenBank Gene Database
AF540969
UniProt Accession
TGM3L_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11777
GenAtlas
TGM1
GeneCards
TGM1
GenBank Gene Database
M98447
GenBank Protein Database
1256959
UniProt Accession
TGM1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11780
GenAtlas
TGM4
GeneCards
TGM4
GenBank Gene Database
L34840
GenBank Protein Database
2766556
UniProt Accession
TGM4_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11779
GenAtlas
TGM3
GeneCards
TGM3
GenBank Gene Database
L10386
GenBank Protein Database
307504
UniProt Accession
TGM3_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:30790
GenAtlas
TGM7
GeneCards
TGM7
GenBank Gene Database
AF363393
GenBank Protein Database
15425755
UniProt Accession
TGM7_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4378
GenAtlas
GMPS
GeneCards
GMPS
GenBank Gene Database
U10860
GenBank Protein Database
595410
UniProt Accession
GUAA_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:753
GenAtlas
ASNS
GeneCards
ASNS
GenBank Gene Database
M27396
GenBank Protein Database
179100
UniProt Accession
ASNS_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:1564
GenAtlas
CCBL1
GeneCards
KYAT1
GenBank Gene Database
X82224
GenBank Protein Database
758591
UniProt Accession
KAT1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:8863
GenAtlas
PFAS
GeneCards
PFAS
GenBank Gene Database
AB002359
GenBank Protein Database
2224663
UniProt Accession
PUR4_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:8849
GenAtlas
PET112L
GeneCards
GATB
GenBank Gene Database
AF026851
GenBank Protein Database
3599964
UniProt Accession
GATB_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4242
GenAtlas
GFPT2
GeneCards
GFPT2
GenBank Gene Database
AB016789
GenBank Protein Database
4239883
UniProt Accession
GFPT2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:1424
GenAtlas
CAD
GeneCards
CAD
GenBank Gene Database
D78586
GenBank Protein Database
1228049
UniProt Accession
PYR1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9751
GenAtlas
QARS
GeneCards
QARS1
GenBank Gene Database
X76013
GenBank Protein Database
558586
UniProt Accession
SYQ_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:29832
GenAtlas
NADSYN1
GeneCards
NADSYN1
GenBank Gene Database
AB091316
GenBank Protein Database
28849201
UniProt Accession
NADE_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:13447
GeneCards
SLC38A1
UniProt Accession
S38A1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:13448
GeneCards
SLC38A2
UniProt Accession
S38A2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:18044
GenAtlas
SLC38A3
GeneCards
SLC38A3
GenBank Gene Database
AF244548
GenBank Protein Database
10242111
UniProt Accession
S38A3_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:10943
GenAtlas
SLC1A5
GeneCards
SLC1A5
GenBank Gene Database
U53347
GenBank Protein Database
1478281
Guide to Pharmacology
874
UniProt Accession
AAAT_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11047
GenAtlas
SLC6A14
GeneCards
SLC6A14
GenBank Gene Database
AF151978
GenBank Protein Database
5732680
Guide to Pharmacology
937
UniProt Accession
S6A14_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11065
GeneCards
SLC7A7
UniProt Accession
YLAT1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11064
GeneCards
SLC7A6
UniProt Accession
YLAT2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11063
GenAtlas
SLC7A5
GeneCards
SLC7A5
GenBank Gene Database
AF077866
GenBank Protein Database
3639058
UniProt Accession
LAT1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11066
GenAtlas
SLC7A8
GeneCards
SLC7A8
GenBank Gene Database
AF171669
GenBank Protein Database
6642960
UniProt Accession
LAT2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:11067
GenAtlas
SLC7A9
GeneCards
SLC7A9
GenBank Gene Database
AF141289
GenBank Protein Database
5916108
UniProt Accession
BAT1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:17027
GeneCards
SLC16A10
GenBank Gene Database
AB057445
GenBank Protein Database
18640047
UniProt Accession
MOT10_HUMAN
International reference pricing
Reference pricing from DrugBank. Prices are indicative and may not reflect current UK costs.
Source: DrugBank. Used under CC BY-NC 4.0 academic licence for non-commercial purposes.
Patent information
All patents expired, 1 expired
Source: DrugBank · CC BY-NC 4.0. Patent data sourced from national patent offices. Expiry dates may not reflect extensions, regulatory exclusivity periods, or legal challenges.
DrugBank citations
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