Editing Alanine

{{short description|Α-amino acid that is used in the biosynthesis of proteins}}
{{distinguish|text = the chemical compound [[Allantoin]], or the phenyl compound [[Aniline]]}}
{{chembox
| Name = Alanine
| ImageFile = L-Alanin - L-Alanine.svg
| ImageSize = 170px
| ImageName = Alanine in non-ionic form
| ImageCaption = [[Skeletal formula]] of <small>L</small>-alanine (neutral form)
| ImageFileL2 = Alanine-from-xtal-3D-bs-17.png
| ImageSizeL2 = 120px
| ImageCaptionL2 = [[Ball-and-stick model]] (zwitterionic form)
| ImageFileR2 = L-alanine-from-xtal-Mercury-3D-sf.png
| ImageSizeR2 = 120px
| ImageCaptionR2 = [[Space-filling model]] (zwitterionic form)
| IUPACName = Alanine<ref>{{cite book |author=[[International Union of Pure and Applied Chemistry]] |date=2014 |title=Nomenclature of Organic Chemistry: IUPAC Recommendations and Preferred Names 2013 |publisher=[[Royal Society of Chemistry|The Royal Society of Chemistry]] |pages=1392 |doi=10.1039/9781849733069 |isbn=978-0-85404-182-4}}</ref>
| SystematicName = 2-Aminopropanoic acid
| OtherNames = Alanic acid<br/>Alaninic acid<br/>2-Aminopropionic acid
| Section1 = {{Chembox Identifiers
| index1_label = D/L
| index2_label = D
| index_label = L <!-- needs to be L (natural isomer) so drugbank etc. take correct index_label -->
| UNII2_Ref = {{fdacite|correct|FDA}}
| UNII2 = E3UDS4613U
| UNII1_Ref = {{fdacite|correct|FDA}}
| UNII1 = 1FU7983T0U
| UNII_Ref = {{fdacite|correct|FDA}}
| UNII = OF5P57N2ZX
| StdInChI_Ref = 
| StdInChI = 1S/C3H7NO2/c1-2(4)3(5)6/h2H,4H2,1H3,(H,5,6)/t2-/m0/s1
| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}
| StdInChIKey = QNAYBMKLOCPYGJ-REOHCLBHSA-N
| InChIKey1 = QNAYBMKLOCPYGJ-UHFFFAOYSA-N
| InChIKey2 = QNAYBMKLOCPYGJ-UWTATZPHSA-N
| CASNo2 = 338-69-2
| CASNo2_Ref = {{cascite|correct|CAS}}
| CASNo1_Ref = {{cascite|correct|??}}
| CASNo1 = 302-72-7
| CASNo_Ref = {{cascite|correct|??}}
| CASNo = 56-41-7
| EC_number = 206-126-4
| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID = 5735
| ChemSpiderID1_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID1 = 582
| ChemSpiderID2_Ref = {{chemspidercite|correct|chemspider}}
| ChemSpiderID2 = 64234
| ChEMBL_Ref = {{ebicite|correct|EBI}}
| ChEMBL = 279597
| PubChem = 5950
| PubChem2 = 71080
| PubChem1 = 602
| IUPHAR_ligand = 720
| KEGG_Ref = {{keggcite|correct|kegg}}
| KEGG = C00041
| KEGG1 = C01401
| KEGG2 = C00133
| ChEBI_Ref = {{ebicite|correct|EBI}}
| ChEBI = 16977
| ChEBI1 = 16449
| ChEBI2 = 15570
| Beilstein = 1720248
| Gmelin = 49628
| 3DMet =  B00011
| DrugBank = DB00160
| DTXSID = DTXSID20873899
| SMILES = C[C@@H](C(=O)O)N
| SMILES3 = C[C@@H](C(=O)[O-])[NH3+]
| SMILES3_Comment = L [[Zwitterion]]
| SMILES2 = C[C@H](C(=O)O)N
| SMILES4 = C[C@H](C(=O)[O-])[NH3+]
| SMILES4_Comment = D [[Zwitterion]]
}}
| Section2 = {{Chembox Properties
| C=3 | H=7 | N=1 | O=2
| Appearance = white powder
| Density = 1.424 g/cm<sup>3</sup>
| MeltingPtC = 258
| MeltingPt_notes = (sublimes)
| BoilingPt =
| pKa = {{Unbulleted list
 | 2.34 (carboxyl; H<sub>2</sub>O)
 | 9.87 (amino; H<sub>2</sub>O)<ref name="CRC97">{{cite book | veditors = Haynes WM | year = 2016 | title = CRC Handbook of Chemistry and Physics | edition = 97th | publisher = [[CRC Press]] | isbn = 978-1-4987-5428-6 | pages=5–88 | title-link = CRC Handbook of Chemistry and Physics }}</ref>
}}
| Solubility = 167.2 g/L (25 °C)
| MagSus = {{val|-50.5|e=-6|u=cm3/mol}}
| LogP = −0.68<ref name="chemsrc">{{Cite web|url=https://www.chemsrc.com/en/cas/56-41-7_414822.html#MSDSDiv|title=L-alanine MSDS | work = ChemSrc }}</ref>
 }}
| Section3 = 
| Section4 = 
| Section5 = 
| Section6 = 
| Section7 = {{Chembox Hazards
| MainHazards = 
| FlashPt = 
| AutoignitionPt = 
  }}
}}
[[File:Alanine-spin.gif|thumb|Spin view of ball-stick model]]
'''Alanine''' (symbol '''Ala''' or '''A'''),<ref>{{cite web | url = http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | title = Nomenclature and Symbolism for Amino Acids and Peptides | publisher = [[IUPAC]]-[[International Union of Biochemistry and Molecular Biology|IUB]] Joint Commission on Biochemical Nomenclature | year = 1983 | access-date = 5 March 2018 | archive-date = 9 October 2008 |url-status = dead| archive-url = https://web.archive.org/web/20081009023202/http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | df = dmy-all }}</ref> or '''α-alanine''', is an α-[[amino acid]] that is used in the biosynthesis of [[protein]]s. It contains an [[amine|amine group]] and a [[carboxylic acid|carboxylic acid group]], both attached to the central carbon atom which also carries a [[methyl group]] side chain.  Consequently it is classified as a [[Chemical polarity|non-polar]], [[Aliphatic compound|aliphatic]] α-amino acid. Under biological conditions, it exists in its [[zwitterion]]ic form with its amine group [[protonated]] (as {{chem2|\sNH3+}}) and its carboxyl group [[deprotonated]] (as {{chem2|\sCO2-}}).  It is non-essential to humans as it can be synthesized [[human metabolism|metabolically]] and does not need to be present in the diet. It is [[Genetic code|encoded]] by all [[codons]] starting with [[Guanine|G]][[Cytosine|C]] (GC[[Uracil|U]], GCC, GC[[Adenine|A]], and GCG).

The <small>L</small>-[[isomer]] of alanine ([[chirality|left-handed]]) is the one that is incorporated into proteins. <small>L</small>-alanine is second only to [[L-leucine|<small>L</small>-leucine]] in rate of occurrence, accounting for 7.8% of the [[primary structure]] in a sample of 1,150 [[proteins]].<ref>{{cite book | vauthors = Doolittle RF | author-link = Russell Doolittle | veditors = Fasman GD | year = 1989 | chapter = Redundancies in Protein Sequences | title = Prediction of Protein Structures and the Principles of Protein Conformation | location = New York | publisher = [[Plenum Publishing Corporation|Plenum]] | pages = 599–623 | isbn = 978-0-306-43131-9 | chapter-url = https://books.google.com/books?id=wdb_JfCDzZsC&pg=PA599}}</ref> The right-handed form, <small>D</small>-alanine, occurs in [[peptides]] in some [[bacterial cell wall]]s<ref name=":0">{{cite book|title = Biochemistry|url = https://archive.org/details/biochemistry0003math|url-access = registration| vauthors = Mathews CK, Van Holde KE, Ahern KG |year = 2000|publisher = [[Benjamin/Cummings Publishing]]|isbn = 978-0-8053-3066-3 |edition = 3rd|location = San Francisco, CA|oclc = 42290721}}</ref>{{rp|131}} (in [[peptidoglycan]]) and in some [[peptide antibiotic]]s, and occurs in the tissues of many [[crustacean]]s and [[Mollusca|molluscs]] as an [[osmolyte]].<ref>{{cite book|chapter-url = https://books.google.com/books?id=DxDpDAAAQBAJ&pg=PA270|title = D-Amino Acids: Physiology, Metabolism, and Application | veditors = Yoshimura T, Nishikawa T, Homma H |year = 2016|chapter = Alanine Racemase and D-Amino Acid Oxidase in Aquatic Animals| vauthors = Yoshikawa N, Sarower MG, Abe H |pages = 269–282|publisher = [[Springer Japan]]|isbn = 978-4-431-56077-7 }}</ref>

==History and etymology==
Alanine was first synthesized in 1850 when [[Adolph Strecker]] combined [[acetaldehyde]] and [[ammonia]] with [[hydrogen cyanide]].<ref>{{cite journal | author-link = Adolph Strecker | vauthors = Strecker A | title = Ueber die künstliche Bildung der Milchsäure und einen neuen, dem Glycocoll homologen Körper | trans-title = On the artificial formation of lactic acid and a new substance homologous to glycine | language = de | journal = [[Liebigs Annalen|Annalen der Chemie und Pharmacie]] | year = 1850 | volume = 75 | issue = 1 | url = https://babel.hathitrust.org/cgi/pt?id=uva.x002457934;view=1up;seq=39 | doi = 10.1002/jlac.18500750103 | pages = 27–45}}  Strecker names alanine on p. 30.</ref><ref>{{cite journal | author-link = Adolph Strecker | vauthors = Strecker A | title = Ueber einen neuen aus Aldehyd – Ammoniak und Blausäure entstehenden Körper | trans-title = On a new substance arising from acetaldehyde–ammonia [i.e., 1-aminoethanol] and hydrocyanic acid | language = de | journal = [[Liebigs Annalen|Annalen der Chemie und Pharmacie]] | year = 1854 | volume = 91 | issue = 3 | url = https://babel.hathitrust.org/cgi/pt?id=uva.x002457942;view=1up;seq=363 | doi = 10.1002/jlac.18540910309 | pages = 349–351 }}</ref><ref>{{cite web|title = Alanine|url = http://www.aminoacidsguide.com/Ala.html|date = 10 June 2018 | access-date = 14 April 2019|website = AminoAcidsGuide.com}}</ref> The amino acid was named ''[[:wikt:Alanin#German|Alanin]]'' in German, in reference to [[aldehyde]], with the [[interfix]] ''-an-'' for ease of pronunciation,<ref>{{cite web |url=http://oxforddictionaries.com/definition/american_english/alanine |archive-url=https://web.archive.org/web/20141224115518/http://www.oxforddictionaries.com/definition/american_english/alanine |url-status=dead |archive-date=December 24, 2014 |title = Alanine |work=Oxford Dictionaries |access-date=2015-12-06}}</ref> the German ending ''[[:wikt:-in#German|-in]]'' used in chemical compounds being analogous to English ''[[-ine]]''.

== Structure ==
Alanine is an [[aliphatic compound|aliphatic]] amino acid, because the side-chain connected to the [[alpha carbon|α-carbon]] atom is a [[methyl]] group (-CH<sub>3</sub>). Alanine is the simplest α-amino acid after [[glycine]]. The methyl side-chain of alanine is non-reactive and is therefore hardly ever directly involved in protein function.<ref>{{cite book | veditors = Patna BK, Kara TC, Ghosh SN, Dalai AK |url=https://books.google.com/books?id=MITRpqnrHYQC&pg=PT47|title=Textbook of Biotechnology |date=2012 |publisher=McGraw-Hill Education |isbn=978-0-07-107007-2 |language=en}}</ref> Alanine is a [[essential amino acid|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.

==Sources==

===Biosynthesis===
Alanine can be synthesized from [[pyruvate]] and [[Branched-chain amino acids|branched chain amino acids]] such as [[valine]], [[leucine]], and [[isoleucine]].

Alanine is produced by [[reductive amination]] of [[pyruvate]], a two-step process. In the first step, [[Alpha-Ketoglutaric acid|α-ketoglutarate]], [[ammonia]] and [[NADH]] are converted by [[glutamate dehydrogenase]] to [[glutamate]], NAD<sup>+</sup> 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]].<ref name=":0" />{{rp|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]].<ref>{{Citation |last1=Melkonian |first1=Erica A. |title=Physiology, Gluconeogenesis |date=2023 |url=http://www.ncbi.nlm.nih.gov/books/NBK541119/ |work=StatPearls |access-date=2023-07-09 |place=Treasure Island (FL) |publisher=StatPearls Publishing |pmid=31082163 |last2=Asuka |first2=Edinen |last3=Schury |first3=Mark P.}}</ref>

===Chemical synthesis===
{{See also|Hell–Volhard–Zelinsky halogenation}}
<small>L</small>-Alanine is produced industrially by decarboxylation of [[L-aspartate|<small>L</small>-aspartate]] by the action of [[aspartate 4-decarboxylase]].  Fermentation routes to <small>L</small>-alanine are complicated by [[alanine racemase]].<ref>{{Ullmann| vauthors = Drauz K, Grayson IG, Kleemann A, Krimmer HP, Leuchtenberger W, Weckbecker C |year=2006|doi=10.1002/14356007.a02_057.pub2}}</ref>

[[Racemic]] alanine can be prepared by the condensation of [[acetaldehyde]] with [[ammonium chloride]] in the presence of [[sodium cyanide]] by the [[Strecker amino acid synthesis|Strecker reaction]],<ref>{{OrgSynth | vauthors = Kendall EC, McKenzie BF | title = ''dl''-Alanine | prep = cv1p0021 | volume = 9 | pages = 4 | year = 1929 | collvol = 1 | collvolpages = 21 | doi = 10.15227/orgsyn.009.0004}}.</ref>
<!--- Note: This Org Synth manuscript is in two parts; the Kendall and McKenzie part used above relates to the Strecker synthesis, whilst the second part by Tobie and Ayres relates to preparing alanine from 2-bromopropanoic acid.  Please be careful if checking / changing these reference, which do share most citation details. --->
:[[File:Synthesis_of_alanine_-_1.png|415px]]

or by the [[ammonolysis]] of [[2-bromopropanoic acid]].<ref>{{OrgSynth | vauthors = Tobie WC, Ayres GB | title = ''dl''-Alanine | prep = cv1p0021 | year = 1941 | collvol = 1 | collvolpages = 21 | doi = 10.15227/orgsyn.009.0004 }}</ref> <!---Note above applies here too--->
:[[File:Synthesis_of_alanine_-_2.png|300px]]

=== Degradation ===
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.<ref name=":0" />{{rp|721}}

==Alanine world hypothesis==
Alanine is one of the twenty [[Proteinogenic amino acid|canonical α-amino acids]] used as building blocks (monomers) for the ribosome-mediated biosynthesis of proteins. Alanine is believed to be one of the earliest amino acids to be included in the genetic code standard repertoire.<ref>{{cite journal | vauthors = Trifonov EN | title = Consensus temporal order of amino acids and evolution of the triplet code | journal = Gene | volume = 261 | issue = 1 | pages = 139–51 | date = December 2000 | pmid = 11164045 | doi = 10.1016/S0378-1119(00)00476-5 }}</ref><ref>{{cite journal | vauthors = Higgs PG, Pudritz RE | title = A thermodynamic basis for prebiotic amino acid synthesis and the nature of the first genetic code | journal = Astrobiology | volume = 9 | issue = 5 | pages = 483–90 | date = June 2009 | pmid = 19566427 | doi = 10.1089/ast.2008.0280 | arxiv = 0904.0402 | s2cid = 9039622 | bibcode = 2009AsBio...9..483H }}</ref><ref>{{cite journal | vauthors = Kubyshkin V, Budisa N | title = The Alanine World Model for the Development of the Amino Acid Repertoire in Protein Biosynthesis | journal = International Journal of Molecular Sciences | volume = 20 | issue = 21 | pages = 5507 | date = November 2019 | pmid = 31694194 | pmc = 6862034 | doi = 10.3390/ijms20215507 | doi-access = free }}</ref><ref name=":2">{{cite journal | vauthors = Ntountoumi C, Vlastaridis P, Mossialos D, Stathopoulos C, Iliopoulos I, Promponas V, Oliver SG, Amoutzias GD | display-authors = 6 | title = Low complexity regions in the proteins of prokaryotes perform important functional roles and are highly conserved | journal = Nucleic Acids Research | volume = 47 | issue = 19 | pages = 9998–10009 | date = November 2019 | pmid = 31504783 | pmc = 6821194 | doi = 10.1093/nar/gkz730 }}</ref> 
On the basis of this fact the "alanine world" hypothesis was proposed.<ref>{{cite journal | vauthors = Kubyshkin V, Budisa N | title = Anticipating alien cells with alternative genetic codes: away from the alanine world! | journal = Current Opinion in Biotechnology | volume = 60 | pages = 242–249 | date = December 2019 | pmid = 31279217 | doi = 10.1016/j.copbio.2019.05.006 | doi-access = free }}</ref> This hypothesis explains the evolutionary choice of amino acids in the repertoire of the genetic code from a chemical point of view. In this model the selection of monomers (i.e. amino acids) for [[Protein translation|ribosomal protein synthesis]] is rather limited to those alanine derivatives that are suitable for building [[Alpha helix|α-helix]] or [[Beta sheet|β-sheet]] [[secondary structure|secondary structural]] elements. Dominant secondary structures in life as we know it are α-helices and β-sheets and most canonical amino acids can be regarded as chemical derivatives of alanine. Therefore, most canonical amino acids in proteins can be exchanged with alanine by point mutations while the secondary structure remains intact. The fact that alanine mimics the secondary structure preferences of the majority of the encoded amino acids is practically exploited in [[alanine scanning]] mutagenesis. In addition, classical [[X-ray crystallography]] often employs the polyalanine-backbone model<ref>{{cite journal | vauthors = Karmali AM, Blundell TL, Furnham N | title = Model-building strategies for low-resolution X-ray crystallographic data | journal = Acta Crystallographica. Section D, Biological Crystallography | volume = 65 | issue = Pt 2 | pages = 121–7 | date = February 2009 | pmid = 19171966 | pmc = 2631632 | doi = 10.1107/S0907444908040006 | doi-access = free | bibcode = 2009AcCrD..65..121K }}</ref> to determine three-dimensional structures of proteins using [[molecular replacement]]—a model-based [[phase problem|phasing]] method.

==Physiological function==
===Glucose–alanine cycle===
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 [[Glutamic acid|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 ion|ammonium]], which in turn participates in the [[urea cycle]] to form [[urea]] which is excreted through the kidneys.<ref name="Lehninger">{{Lehninger4th|pages=684–85|name-list-style=vanc}}.</ref>

The glucose–alanine cycle enables pyruvate and glutamate to be removed from muscle and safely transported to the liver. Once there, pyruvate is used to regenerate glucose, after which the glucose returns to muscle to be metabolized for energy: this moves the energetic burden of gluconeogenesis to the liver instead of the muscle, and all available [[Adenosine triphosphate|ATP]] in the muscle can be devoted to muscle contraction.<ref name="Lehninger"/> 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.<ref>{{Cite book|url=https://books.google.com/books?id=P42VIrgYpKoC&pg=PA23|title=Fish Physiology: Nitrogen Excretion|date=2001-09-07|publisher=Academic Press|isbn=978-0-08-049751-8 |pages=23|language=en}}</ref><ref>{{Cite book|url=https://books.google.com/books?id=H5d2k2b1cWQC&pg=PA172 |title=Nitrogen Metabolism and Excretion| vauthors = Walsh PJ, Wright PA |date=1995-08-31|publisher=CRC Press|isbn=978-0-8493-8411-0 |language=en}}</ref>

===Link to diabetes===
Alterations in the alanine cycle that increase the levels of serum [[alanine aminotransferase]] (ALT) are linked to the development of type II diabetes.<ref>{{cite journal | vauthors = Sattar N, Scherbakova O, Ford I, O'Reilly DS, Stanley A, Forrest E, Macfarlane PW, Packard CJ, Cobbe SM, Shepherd J | display-authors = 6 | title = Elevated Alanine Aminotransferase 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 | journal = Diabetes | volume = 53 | issue = 11 | pages = 2855–60 | date = November 2004 | pmid = 15504965 | doi = 10.2337/diabetes.53.11.2855 | doi-access = free }}</ref>

==Chemical properties==
[[File:Zwitterion-Alanine.png|thumb|250px|(''S'')-Alanine (left) and (''R'')-alanine (right) in zwitterionic form at neutral pH]]

Alanine is useful in [[genetic engineering|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.<ref>{{cite book|url=https://books.google.com/books?id=ycVoWFqDTmAC&pg=PA94|title=Protein Engineering and Design| vauthors = Park SJ, Cochran JR |date=2009-09-25|publisher=CRC Press|isbn=978-1-4200-7659-2 |language=en}}</ref>

Hydrogenation of alanine gives the [[amino alcohol]] [[alaninol]], which is a useful chiral building block.

===Free radical===
The [[deamination]] of an alanine molecule produces the [[Radical (chemistry)|free radical]] CH<sub>3</sub>C<sup>•</sup>HCO<sub>2</sub><sup>−</sup>. Deamination can be induced in solid or aqueous alanine by radiation that causes [[homolysis (chemistry)|homolytic cleavage]] of the carbon&ndash;nitrogen bond.<ref>{{cite journal | journal = [[J. Radioanal. Nucl. Chem.]] | title = Transients and Stable Radical from the Deamination of α-Alanine | vauthors = Zagórski ZP, Sehested K | doi = 10.1007/BF02383729 | year = 1998 | volume = 232 | issue = 1–2 | pages = 139–41| bibcode = 1998JRNC..232..139Z | s2cid = 97855573 }}.</ref>

This property of alanine is used in [[dosimetry|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.<ref name=":1">{{cite book|title = Fundamentals of Ionizing Radiation Dosimetry| vauthors = Andreo P, Burns DT, Nahum AE, Seuntjens J, Attix FH |publisher = [[Wiley-VCH]] |year = 2017|isbn = 978-3-527-80823-6|edition = 2nd|location = Weinheim, Germany|pages = 547–556|oclc = 990023546|chapter-url = https://books.google.com/books?id=nhknDwAAQBAJ&pg=PA547|chapter = Alanine Dosimetry}}</ref> 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.<ref name=":1" /> 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.<ref>{{Cite journal |last1=Biglin |first1=Emma R. |last2=Aitkenhead |first2=Adam H. |last3=Price |first3=Gareth J. |last4=Chadwick |first4=Amy L. |last5=Santina |first5=Elham |last6=Williams |first6=Kaye J. |last7=Kirkby |first7=Karen J. |date=2022-04-26 |title=A preclinical radiotherapy dosimetry audit using a realistic 3D printed murine phantom |journal=Scientific Reports |volume=12 |issue=1 |pages=6826 |doi=10.1038/s41598-022-10895-5 |issn=2045-2322 |pmc=9042835 |pmid=35474242|bibcode=2022NatSR..12.6826B }}</ref>

== References ==
{{Reflist|30em}}

{{Amino acids}}
{{Amino acid metabolism intermediates}}
{{Neurotransmitters}}
{{Ionotropic glutamate receptor modulators}}
{{Glycine receptor modulators}}

{{Authority control}}

[[Category:Alpha-Amino acids]]
[[Category:Proteinogenic amino acids]]
[[Category:Glucogenic amino acids]]
[[Category:Glycine receptor agonists]]
[[Category:NMDA receptor agonists]]