ListMoto - Alanine

--- Advertisement ---

(symbol Ala or A[2]) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated form, −NH3+, under biological conditions), an α-carboxylic acid group (which is in the deprotonated form, −COO−, under biological conditions), and a side chain methyl group, making it a nonpolar, aliphatic amino acid. It is non-essential in humans: because the body can synthesize it, it does not need to be present in the diet. It is one of the 20 amino acids encoded by the human genetic code, and is encoded by all codons starting with GC, namely GCU, GCC, GCA, and GCG. The L-isomer of alanine (left-handed) is the one that is incorporated into proteins. L- Alanine
is second only to leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins.[3] The right-handed form, D- Alanine
occurs in polypeptides in some bacterial cell walls[4]p. 131 and in some peptide antibiotics, and occurs in the tissues of many crustaceans and molluscs as an osmolyte.[5]


1 History and etymology 2 Structure 3 Sources

3.1 Dietary sources 3.2 Biosynthesis 3.3 Chemical synthesis 3.4 Degradation

4 Physiological function

4.1 Glucose–alanine cycle 4.2 Link to diabetes

5 Chemical properties

5.1 Free radical stability

6 References 7 External links

History and etymology[edit] Alanine
was first synthesized in 1850 by Adolph Strecker.[6][7][8] The amino acid was named Alanin in German, in reference to aldehyde, with the infix -an- for ease of pronunciation,[9] the German ending -in used in chemical compounds being analogous to English -ine. Structure[edit] Alanine
is an aliphatic amino acid, because the side-chain connected to the α-carbon atom is a methyl group (-CH3), making it the simplest α-amino acid except for glycine. The methyl side-chain of alanine is non-reactive and is therefore hardly ever directly involved in protein function.[10] Because alanine's side-chain cannot be phosphorylated (only compounds like 3-Phosphino-L-alanine[11] and 3-Hydroxyphosphinylalanine[12] are known), it is useful in loss of function experiments with respect to phosphorylation. Some techniques involve creating a library of genes, each of which has a point mutation at a different position in the area of interest, sometimes even every position in the whole gene: this is called "scanning mutagenesis". The simplest method, and the first to have been used, is so-called "alanine scanning", where every position in turn is mutated to alanine.[13] Sources[edit] Dietary sources[edit] Alanine
is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained through the diet. Alanine
is found in a wide variety of foods, but is particularly concentrated in meats. Biosynthesis[edit] Alanine
can be synthesized from pyruvate and branched chain amino acids such as valine, leucine, and isoleucine. Alanine
is most commonly produced by reductive amination of pyruvate, a two-step process. In the first step, α-ketoglutarate, ammonia and NADH
are converted by glutamate dehydrogenase to glutamate, NAD+ and water. In the second step, the amino group of the newly-formed glutamate is transferred to pyruvate by an aminotransferase enzyme, regenerating the α-ketoglutarate, and converting the pyruvate to alanine. The net result is that pyruvate and ammonia are converted to alanine, consuming one reducing equivalent.[4]p. 721 Because transamination reactions are readily reversible and pyruvate is present in all cells, alanine can be easily formed and thus has close links to metabolic pathways such as glycolysis, gluconeogenesis, and the citric acid cycle. Chemical synthesis[edit] Racemic
alanine can be prepared by the condensation of acetaldehyde with ammonium chloride in the presence of sodium cyanide by the Strecker reaction, or by the ammonolysis of 2-bromopropanoic acid:[14]

L- Alanine

Degradation[edit] Alanine
is broken down by oxidative deamination, the inverse reaction of the reductive amination reaction described above, catalyzed by the same enzymes. The direction of the process is largely controlled by the relative concentration of the substrates and products of the reactions involved.[4]p. 721 Physiological function[edit] Glucose–alanine cycle[edit] In mammals, alanine plays a key role in glucose–alanine cycle between tissues and liver. In muscle and other tissues that degrade amino acids for fuel, amino groups are collected in the form of glutamate by transamination. Glutamate
can then transfer its amino group to pyruvate, a product of muscle glycolysis, through the action of alanine aminotransferase, forming alanine and α-ketoglutarate. The alanine enters the bloodstream, and is transported to the liver. The alanine aminotransferase reaction takes place in reverse in the liver, where the regenerated pyruvate is used in gluconeogenesis, forming glucose which returns to the muscles through the circulation system. Glutamate
in the liver enters mitochondria and is broken down by glutamate dehydrogenase into α-ketoglutarate and ammonium, which in turn participates in the urea cycle to form urea which is excreted through the kidneys.[16] The glucose–alanine cycle enables pyruvate and glutamate to be removed from the muscle and safely transported to the liver, where glucose is regenerated from pyruvate and then returned to muscle: this moves the energetic burden of gluconeogenesis to the liver instead of the muscle, and all available ATP in the muscle can be devoted to muscle contraction.[16] It is a catabolic pathway, and relies upon protein breakdown in the muscle tissue. Whether and to what extent it occurs in non-mammals is unclear.[17][18] Link to diabetes[edit] Alterations in the alanine cycle that increase the levels of serum alanine aminotransferase (ALT) are linked to the development of type II diabetes.[19] Chemical properties[edit]

(S)- Alanine
(left) and (R)-alanine (right) in zwitterionic form at neutral pH

Free radical stability[edit] The deamination of an alanine molecule produces a stable alkyl free radical, CH3C•HCOO−. Deamination
can be induced in solid or aqueous alanine by radiation.[20] This property of alanine is used in dosimetric measurements in radiotherapy. When normal alanine is irradiated, the radiation causes certain alanine molecules to become free radicals, and, as these radicals are stable, the free radical content can later be measured by electron paramagnetic resonance in order to find out how much radiation the alanine was exposed to.[21] This is considered to be a biologically relevant measure of the amount of radiation damage that living tissue would suffer under the same radiation exposure.[21] Radiotherapy
treatment plans can be delivered in test mode to alanine pellets, which can then be measured to check that the intended pattern of radiation dose is correctly delivered by the treatment system. References[edit]

^ Dawson, R.M.C., et al., Data for Biochemical Research, Oxford, Clarendon Press, 1959. ^ "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on 9 October 2008. Retrieved 5 March 2018.  ^ Doolittle, R. F. (1989), "Redundancies in protein sequences", in Fasman, G. D., Prediction of Protein
Structures and the Principles of Protein
Conformation, New York: Plenum, pp. 599–623, ISBN 0-306-43131-9 . ^ a b c Mathews, Christopher K., (2000). Biochemistry. Van Holde, K. E., Ahern, Kevin G. (3rd ed.). San Francisco, Calif.: Benjamin Cummings. ISBN 0805330666. OCLC 42290721.  ^ Yoshimura, Tohru; Nishikawa, Toru; Homma, Hiroshi (2016-08-25). D-Amino Acids: Physiology, Metabolism, and Application. Springer. ISBN 9784431560777.  ^ Strecker, A. (1850). "Ueber die künstliche Bildung der Milchsäure und einen neuen, dem Glycocoll homologen" [On the artificial formation of lactic acid and a new substance homologous to glycine]. Annalen der Chemie und Pharmacie. 75 (1): 27–45. doi:10.1002/jlac.18500750103.  Strecker names alanine on p. 30. ^ Strecker, A. (1854). "Ueber einen neuen aus Aldehyd – Ammoniak und Blausäure entstehenden Körper" [On a new substance arising from acetaldehyde–ammonia [i.e., 1-aminoethanol] and hydrocyanic acid]. Annalen der Chemie und Pharmacie. 91 (3): 349–351. doi:10.1002/jlac.18540910309.  ^ "Alanine".  ^ "alanine". Oxford Dictionaries. Retrieved 2015-12-06.  ^ Textbook of Biotechnology. McGraw-Hill Education (I). 2012. ISBN 9780071070072.  ^ 3-Phosphino-L-alanine at Chemspider ^ https://pubchem.ncbi.nlm.nih.gov/compound/6330801 ^ Park, Sheldon J.; Cochran, Jennifer R. (2009-09-25). Protein Engineering and Design. CRC Press. ISBN 9781420076592.  ^ Kendall, E. C.; McKenzie, B. F. (1929). "dl-Alanine". Organic Syntheses. 9: 4. ; Collective Volume, 1, p. 21 . ^ http://drugsynthesis.blogspot.co.uk/2011/11/laboratory-synthesis-of-l-alanine.html ^ a b Nelson, David L.; Cox, Michael M. (2005), Principles of Biochemistry (4th ed.), New York: W. H. Freeman, pp. 684–85, ISBN 0-7167-4339-6 . ^ Fish Physiology: Nitrogen Excretion. Academic Press. 2001-09-07. p. 23. ISBN 9780080497518.  ^ Walsh, Patrick J.; Wright, Patricia A. (1995-08-31). Nitrogen Metabolism and Excretion. CRC Press. ISBN 9780849384110.  ^ "Elevated Alanine
Predicts New-Onset Type 2 Diabetes Independently of Classical Risk Factors, Metabolic Syndrome, and C-Reactive Protein
in the West of Scotland Coronary Prevention Study".  ^ Zagórski, Z. P.; Sehested, K. (1998), "Transients and stable radical from the deamination of α-alanine", J. Radioanal. Nucl. Chem., 232 (1–2): 139–41, doi:10.1007/BF02383729 . ^ a b Pedro,, Andreo, (2017). Fundamentals of ionizing radiation dosimetry. Burns, David T.,, Nahum, Alan E.,, Seuntjens, Jan P.,, Attix, Frank H., (2nd ed.). Weinheim, Germany: WILEY-VCH. p. 547. ISBN 9783527808236. OCLC 990023546. 

External links[edit]

MS spectrum

v t e

The encoded amino acid

General topics

Protein Peptide Genetic code

By properties


Branched-chain amino acids
Branched-chain amino acids
(Valine Isoleucine Leucine) Methionine Alanine Proline Glycine


Phenylalanine Tyrosine Tryptophan Histidine

Polar, uncharged

Asparagine Glutamine Serine Threonine

Positive charge (pKa)

(≈10.8) Arginine
(≈12.5) Histidine

Negative charge (pKa)

Aspartic acid
Aspartic acid
(≈3.9) Glutamic acid
Glutamic acid
(≈4.1) Cysteine
(≈8.3) Tyrosine

Amino acids
Amino acids
types: Encoded (proteins) Essential Non-proteinogenic Ketogenic Glucogenic Imino acids D-amino acids Dehydroamino acids

v t e

Amino acid
Amino acid
metabolism metabolic intermediates



Saccharopine Allysine α-Aminoadipic acid α-Ketoadipate Glutaryl-CoA Glutaconyl-CoA Crotonyl-CoA β-Hydroxybutyryl-CoA


β-Hydroxy β-methylbutyric acid β-Hydroxy β-methylbutyryl-CoA Isovaleryl-CoA α-Ketoisocaproic acid β-Ketoisocaproic acid β-Ketoisocaproyl-CoA β-Leucine β-Methylcrotonyl-CoA β-Methylglutaconyl-CoA β-Hydroxy β-methylglutaryl-CoA


N'-Formylkynurenine Kynurenine Anthranilic acid 3-Hydroxykynurenine 3-Hydroxyanthranilic acid 2-Amino-3-carboxymuconic semialdehyde 2-Aminomuconic semialdehyde 2-Aminomuconic acid Glutaryl-CoA




3-Phosphoglyceric acid

glycine→creatine: Glycocyamine Phosphocreatine Creatinine

G→glutamate→ α-ketoglutarate


Urocanic acid Imidazol-4-one-5-propionic acid Formiminoglutamic acid Glutamate-1-semialdehyde


1-Pyrroline-5-carboxylic acid


Agmatine Ornithine Citrulline Cadaverine Putrescine


cysteine+glutamate→glutathione: γ-Glutamylcysteine

G→propionyl-CoA→ succinyl-CoA


α-Ketoisovaleric acid Isobutyryl-CoA Methacrylyl-CoA 3-Hydroxyisobutyryl-CoA 3-Hydroxyisobutyric acid 2-Methyl-3-oxopropanoic acid


2,3-Dihydroxy-3-methylpentanoic acid 2-Methylbutyryl-CoA Tiglyl-CoA 2-Methylacetoacetyl-CoA


generation of homocysteine: S-Adenosyl methionine S-Adenosyl-L-homocysteine Homocysteine

conversion to cysteine: Cystathionine alpha-Ketobutyric acid+Cysteine


α-Ketobutyric acid





4-Hydroxyphenylpyruvic acid Homogentisic acid 4-Maleylacetoacetic acid


see urea cycle



sulfinic acid

v t e


Amino acid-derived

Major excitatory/inhibitory systems: Glutamate
system: Agmatine Aspartic acid
Aspartic acid
(aspartate) Cycloserine Glutamic acid
Glutamic acid
(glutamate) Glutathione Glycine GSNO GSSG Kynurenic acid NAA NAAG Proline Serine; GABA system: GABA GABOB GHB; Glycine
system: α-Alanine β-Alanine Glycine Hypotaurine Proline Sarcosine Serine Taurine; GHB system: GHB T-HCA (GHC)

Biogenic amines: Monoamines: 6-OHM Dopamine Epinephrine
(adrenaline) NAS (normelatonin) Norepinephrine
(noradrenaline) Serotonin
(5-HT); Trace amines: 3-Iodothyronamine N-Methylphenethylamine N-Methyltryptamine m-Octopamine p-Octopamine Phenylethanolamine Phenethylamine Synephrine Tryptamine m-Tyramine p-Tyramine; Others: Histamine

Neuropeptides: See here instead.


Endocannabinoids: 2-AG 2-AGE (noladin ether) 2-ALPI 2-OG AA-5-HT Anandamide
(AEA) DEA LPI NADA NAGly OEA Oleamide PEA RVD-Hpα SEA Virodhamine

Neurosteroids: See here instead.


Nucleosides: Adenosine
system: Adenosine ADP AMP ATP


Cholinergic system: Acetylcholine


Gasotransmitters: Carbon monoxide
Carbon monoxide
(CO) Hydrogen sulfide
Hydrogen sulfide
(H2S) Nitric oxide
Nitric oxide
(NO); Candidates: Acetaldehyde Ammonia
(NH3) Carbonyl sulfide
Carbonyl sulfide
(COS) Nitrous oxide
Nitrous oxide
(N2O) Sulfur dioxide
Sulfur dioxide

v t e

Ionotropic glutamate receptor
Ionotropic glutamate receptor


Agonists: Main site agonists: 5-Fluorowillardiine Acromelic acid (acromelate) AMPA BOAA Domoic acid Glutamate Ibotenic acid Proline Quisqualic acid Willardiine; Positive allosteric modulators: Aniracetam Cyclothiazide CX-516 CX-546 CX-614 Farampator
(CX-691, ORG-24448) CX-717 CX-1739 CX-1942 Diazoxide Hydrochlorothiazide
(HCTZ) IDRA-21 LY-392098 LY-395153 LY-404187 LY-451646 LY-503430 Mibampator
(LY-451395) Nooglutyl ORG-26576 Oxiracetam PEPA PF-04958242 Piracetam Pramiracetam S-18986 Tulrampator
(S-47445, CX-1632)

Antagonists: ACEA-1011 ATPO Becampanel Caroverine CNQX Dasolampanel DNQX Fanapanel
(MPQX) GAMS Kaitocephalin Kynurenic acid Kynurenine Licostinel
(ACEA-1021) NBQX PNQX Selurampanel Tezampanel Theanine Topiramate YM90K Zonampanel; Negative allosteric modulators: Barbiturates
(e.g., pentobarbital, sodium thiopental) Cyclopropane Enflurane Ethanol (alcohol) Evans blue GYKI-52466 GYKI-53655 Halothane Irampanel Isoflurane Perampanel Pregnenolone
sulfate Sevoflurane Talampanel; Unknown/unsorted antagonists: Minocycline


Agonists: Main site agonists: 5-Bromowillardiine 5-Iodowillardiine Acromelic acid (acromelate) AMPA ATPA Domoic acid Glutamate Ibotenic acid Kainic acid LY-339434 Proline Quisqualic acid SYM-2081; Positive allosteric modulators: Cyclothiazide Diazoxide Enflurane Halothane Isoflurane

Antagonists: ACEA-1011 CNQX Dasolampanel DNQX GAMS Kaitocephalin Kynurenic acid Licostinel
(ACEA-1021) LY-382884 NBQX NS102 Selurampanel Tezampanel Theanine Topiramate UBP-302; Negative allosteric modulators: Barbiturates
(e.g., pentobarbital, sodium thiopental) Enflurane Ethanol (alcohol) Evans blue NS-3763 Pregnenolone


Agonists: Main site agonists: AMAA Aspartate Glutamate Homocysteic acid
Homocysteic acid
(L-HCA) Homoquinolinic acid Ibotenic acid NMDA Proline Quinolinic acid Tetrazolylglycine Theanine; Glycine
site agonists: β-Fluoro-D-alanine ACBD ACC (ACPC) ACPD AK-51 Apimostinel
(NRX-1074) B6B21 CCG D-Alanine D-Cycloserine D-Serine DHPG Dimethylglycine Glycine HA-966 L-687414 L-Alanine L-Serine Milacemide Neboglamine
(nebostinel) Rapastinel
(GLYX-13) Sarcosine; Polyamine site agonists: Neomycin Spermidine Spermine; Other positive allosteric modulators: 24S-Hydroxycholesterol DHEA (prasterone) DHEA sulfate
DHEA sulfate
(prasterone sulfate) Epipregnanolone sulfate Pregnenolone
sulfate SAGE-201 SAGE-301 SAGE-718

Antagonists: Competitive antagonists: AP5
(APV) AP7 CGP-37849 CGP-39551 CGP-39653 CGP-40116 CGS-19755 CPP Kaitocephalin LY-233053 LY-235959 LY-274614 MDL-100453 Midafotel
(d-CPPene) NPC-12626 NPC-17742 PBPD PEAQX Perzinfotel PPDA SDZ-220581 Selfotel; Glycine
site antagonists: 4-Cl-KYN (AV-101) 5,7-DCKA 7-CKA ACC ACEA-1011 ACEA-1328 Apimostinel
(NRX-1074) AV-101 Carisoprodol CGP-39653 CNQX D-Cycloserine DNQX Felbamate Gavestinel GV-196771 Harkoseride Kynurenic acid Kynurenine L-689560 L-701324 Licostinel
(ACEA-1021) LU-73068 MDL-105519 Meprobamate MRZ 2/576 PNQX Rapastinel
(GLYX-13) ZD-9379; Polyamine site antagonists: Arcaine Co 101676 Diaminopropane Diethylenetriamine Huperzine A Putrescine; Uncompetitive pore blockers (mostly dizocilpine site): 2-MDP 3-HO-PCP 3-MeO-PCE 3-MeO-PCMo 3-MeO-PCP 4-MeO-PCP 8A-PDHQ 18-MC α-Endopsychosin Alaproclate Alazocine
(SKF-10047) Amantadine Aptiganel Argiotoxin-636 Arketamine ARL-12495 ARL-15896-AR ARL-16247 Budipine Coronaridine Delucemine
(NPS-1506) Dexoxadrol Dextrallorphan Dextromethadone Dextromethorphan Dextrorphan Dieticyclidine Diphenidine Dizocilpine Ephenidine Esketamine Etoxadrol Eticyclidine Fluorolintane Gacyclidine Ibogaine Ibogamine Indantadol Ketamine Ketobemidone Lanicemine Levomethadone Levomethorphan Levomilnacipran Levorphanol Loperamide Memantine Methadone Methorphan Methoxetamine Methoxphenidine Milnacipran Morphanol NEFA Neramexane Nitromemantine Noribogaine Norketamine Orphenadrine PCPr PD-137889 Pethidine
(meperidine) Phencyclamine Phencyclidine Propoxyphene Remacemide Rhynchophylline Rimantadine Rolicyclidine Sabeluzole Tabernanthine Tenocyclidine Tiletamine Tramadol; Ifenprodil (NR2B) site antagonists: Besonprodil Buphenine
(nylidrin) CO-101244 (PD-174494) Eliprodil Haloperidol Isoxsuprine Radiprodil (RGH-896) Rislenemdaz
(CERC-301, MK-0657) Ro 8-4304 Ro 25-6981 Safaprodil Traxoprodil
(CP-101606); NR2A-selective antagonists: MPX-004 MPX-007 TCN-201 TCN-213; Cations: Hydrogen Magnesium Zinc; Alcohols/volatile anesthetics/related: Benzene Butane Chloroform Cyclopropane Desflurane Diethyl ether Enflurane Ethanol (alcohol) Halothane Hexanol Isoflurane Methoxyflurane Nitrous oxide Octanol Sevoflurane Toluene Trichloroethane Trichloroethanol Trichloroethylene Urethane Xenon Xylene; Unknown/unsorted antagonists: ARR-15896 Bumetanide Caroverine Conantokin D-αAA Dexanabinol Flufenamic acid Flupirtine FPL-12495 FR-115427 Furosemide Hodgkinsine Ipenoxazone (MLV-6976) MDL-27266 Metaphit Minocycline MPEP Niflumic acid Pentamidine Pentamidine
isethionate Piretanide Psychotridine Transcrocetin

See also: Receptor/signaling modulators Metabotropic glutamate receptor modulators Glutamate
metabolism/transport modulators

v t e

receptor modulators

Receptor (ligands)


Agonists: β-Alanine β-ABA (BABA) β-AIBA Caesium D-Alanine D-Serine GABA Glycine Hypotaurine Ivermectin L-Alanine L-Proline L-Serine L-Threonine MDL-27531 Milacemide Picolinic acid Propofol Quisqualamine Sarcosine Taurine

Positive modulators: Alcohols (e.g., brometone, chlorobutanol (chloretone), ethanol (alcohol), tert-butanol (2M2P), tribromoethanol, trichloroethanol, trifluoroethanol) Alkylbenzene sulfonate Anandamide Barbiturates
(e.g., pentobarbital, sodium thiopental) Chlormethiazole D12-116 Dihydropyridines (e.g., nicardipine) Etomidate Ginseng
constituents (e.g., ginsenosides (e.g., ginsenoside-Rf)) Glutamic acid
Glutamic acid
(glutamate) Ivermectin Ketamine Neuroactive steroids (e.g., alfaxolone, pregnenolone (eltanolone), pregnenolone acetate, minaxolone, ORG-20599) Nitrous oxide Penicillin G Propofol Tamoxifen Tetrahydrocannabinol Triclofos Tropeines (e.g., atropine, bemesetron, cocaine, LY-278584, tropisetron, zatosetron) Volatiles/gases (e.g., chloral hydrate, chloroform, desflurane, diethyl ether (ether), enflurane, halothane, isoflurane, methoxyflurane, sevoflurane, toluene, trichloroethane (methyl chloroform), trichloroethylene) Xenon Zinc

Antagonists: 2-Aminostrychnine 2-Nitrostrychnine 4-Phenyl-4-formyl-N-methylpiperidine αEMBTL Bicuculline Brucine Cacotheline Caffeine Colchicine Colubrine Cyanotriphenylborate Dendrobine Diaboline Endocannabinoids (e.g., 2-AG, anandamide (AEA)) Gaboxadol
(THIP) Gelsemine iso-THAZ Isobutyric acid Isonipecotic acid Isostrychnine Laudanosine N-Methylbicuculline N-Methylstrychnine N,N-Dimethylmuscimol Nipecotic acid Pitrazepin Pseudostrychnine Quinolines (e.g., 4-hydroxyquinoline, 4-hydroxyquinoline-3-carboxylic acid, 5,7-CIQA, 7-CIQ, 7-TFQ, 7-TFQA) RU-5135 Sinomenine Strychnine Thiocolchicoside Tutin

Negative modulators: Amiloride Benzodiazepines (e.g., bromazepam, clonazepam, diazepam, flunitrazepam, flurazepam) Corymine Cyanotriphenylborate Daidzein Dihydropyridines (e.g., nicardipine, nifedipine, nitrendipine) Furosemide Genistein Ginkgo constituents (e.g., bilobalide, ginkgolides (e.g., ginkgolide A, ginkgolide B, ginkgolide C, ginkgolide J, ginkgolide M)) Imipramine NBQX Neuroactive steroids (e.g., 3α-androsterone sulfate, 3β-androsterone sulfate, deoxycorticosterone, DHEA sulfate, pregnenolone sulfate, progesterone) Opioids (e.g., codeine, dextromethorphan, dextrorphan, levomethadone, levorphanol, morphine, oripavine, pethidine, thebaine) Picrotoxin
(i.e., picrotin and picrotoxinin) PMBA Riluzole Tropeines (e.g., bemesetron, LY-278584, tropisetron, zatosetron) Verapamil Zinc


See here instead.

Transporter (blockers)


ACPPB ALX-1393 ALX-5407 (NFPS) AMG-747 ASP2535 Bitopertin
(RG1678/RO4917838) CP-802079 Ethanol (alcohol) Glycyldodecylamide GSK1018921 LY-2365109 ORG-24598 ORG-25935
(SCH-900435) PF-02545920 PF-03463275 PF-04958242 Sarcosine SSR-103,800 SSR-504,734


Amoxapine Ethanol (alcohol) NAGly Opiranserin (VVZ-149) ORG-25543 VVZ-368

See also Receptor/signaling modulators GABA receptor modulators GABAA receptor positive modulators Ionotropic glutamate receptor
Ionotropic glutamate receptor

Authority control