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{{DISPLAYTITLE:''beta''-Alanine}} |
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{{DISPLAYTITLE:β-Alanine}} |
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{{chembox |
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{{chembox |
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| Watchedfields = changed |
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| verifiedrevid = 412506321 |
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| verifiedrevid = 443667077 |
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| Name=β-Alanine |
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| Name=β-Alanine |
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| ImageFile = Beta-alanine structure.svg |
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| ImageFile = Beta-alanine structure.svg |
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| ImageSize = 150px |
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| ImageSize = 180 |
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| ImageAlt = Skeletal formula of beta alanine |
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| IUPACName = 3-Aminopropanoic acid |
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| ImageFile1 = |
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| OtherNames = β-Alanine<br>3-Aminopropionic acid |
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| ImageSize1 = 180 |
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| Section1 = {{Chembox Identifiers |
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| ImageAlt1 = |
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| UNII_Ref = {{fdacite|correct|FDA}} |
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| IUPACName = β-Alanine |
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| SystematicName = 3-Aminopropanoic acid |
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| OtherNames = 3-Aminopropionic acid |
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|Section1={{Chembox Identifiers |
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| UNII_Ref = {{fdacite|correct|FDA}} |
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| UNII = 11P2JDE17B |
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| UNII = 11P2JDE17B |
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| KEGG_Ref = {{keggcite|correct|kegg}} |
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| KEGG_Ref = {{keggcite|correct|kegg}} |
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| KEGG = D07561 |
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| KEGG = D07561 |
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| InChI = 1/C3H7NO2/c4-2-1-3(5)6/h1-2,4H2,(H,5,6) |
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| InChI = 1/C3H7NO2/c4-2-1-3(5)6/h1-2,4H2,(H,5,6) |
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| InChIKey = UCMIRNVEIXFBKS-UHFFFAOYAL |
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| InChIKey = UCMIRNVEIXFBKS-UHFFFAOYAL |
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| ChEMBL_Ref = {{ebicite|correct|EBI}} |
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| ChEMBL_Ref = {{ebicite|correct|EBI}} |
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| ChEMBL = 297569 |
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| ChEMBL = 297569 |
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| StdInChIKey = UCMIRNVEIXFBKS-UHFFFAOYSA-N |
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| StdInChIKey = UCMIRNVEIXFBKS-UHFFFAOYSA-N |
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| CASNo = 107-95-9 |
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| CASNo = 107-95-9 |
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| CASNo_Ref = {{cascite|correct|CAS}} |
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| CASNo_Ref = {{cascite|correct|CAS}} |
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| EC-number = 203-536-5 |
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| EC_number = 203-536-5 |
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| PubChem = 239 |
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| PubChem = 239 |
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| IUPHAR_ligand = 2365 |
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| IUPHAR_ligand = 2365 |
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| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} |
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| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} |
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| ChemSpiderID = 234 |
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| ChemSpiderID = 234 |
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| ChEBI_Ref = {{ebicite|correct|EBI}} |
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| ChEBI = 16958 |
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| ChEBI = 16958 |
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| DrugBank_Ref = {{drugbankcite|correct|drugbank}} |
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| DrugBank = DB03107 |
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| SMILES = O=C(O)CCN |
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| SMILES = O=C(O)CCN |
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| Section2 = {{Chembox Properties |
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|Section2={{Chembox Properties |
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| Reference = <ref>{{Merck11th|196}}.</ref><ref>{{RubberBible62nd|page=C-83}}.</ref> |
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| Properties_ref = <ref>{{Merck11th|196}}.</ref><ref>{{RubberBible62nd|page=C-83}}.</ref> |
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| C=3 | H=7 | N=1 | O=2 |
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| C=3 | H=7 | N=1 | O=2 |
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| MolarMass = 89.093 g/mol |
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| MolarMass = 89.093 g/mol |
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| Appearance = Bipyramidal crystals |
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| Appearance = white bipyramidal crystals |
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| Density = 1.437 g/cm<sup>3</sup> (19 °C) |
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| Odor = odorless |
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| Density = 1.437 g/cm<sup>3</sup> (19 °C) |
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| MeltingPt = 207 °C decomp. |
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| MeltingPtC = 207 |
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| MeltingPt_notes = (decomposes) |
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| BoilingPt = |
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| Solubility = soluble |
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| BoilingPt = |
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| Solubility = 54.5 g/100 mL |
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| SolubleOther = soluble in ]. Insoluble in ], ] |
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| LogP = -3.05 |
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| pKa = {{ubl |
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| 3.55 (carboxyl; H<sub>2</sub>O) |
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| 10.24 (amino; H<sub>2</sub>O)<ref name="CRC97">{{cite book | editor= Haynes, William M. | year = 2016 | title = CRC Handbook of Chemistry and Physics | edition = 97th | publisher = ] | isbn = 978-1498754286 | pages=5–88 | title-link = CRC Handbook of Chemistry and Physics }}</ref> |
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| Section3 = {{Chembox Hazards |
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|Section3={{Chembox Hazards |
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| ExternalSDS = |
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| MainHazards = |
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| FlashPt = |
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| MainHazards = Irritant |
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| NFPA-H = 2 | NFPA-F = 1 | NFPA-R = 0 |
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| Autoignition = |
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| FlashPtC = |
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| AutoignitionPt = |
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| LD50 = 1000 mg/kg (rat, oral) |
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'''β-Alanine''' (or '''''beta''-alanine''') is a naturally occurring ], which are ] in which the ] group is at the β-position from the carboxylate group (i.e., two atoms away, see Figure 1). The ] name for β-alanine would be '''3-aminopropanoic acid'''. Unlike its normal counterpart, ], β-alanine has no chiral center. |
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'''β-Alanine''' ('''''beta''-alanine''') is a naturally occurring ], which is an ] in which the ] group is attached to the ] (i.e. the carbon two carbon atoms away from the ] group) instead of the more usual α-carbon for ] (α-alanine). The ] name for β-alanine is '''3-aminopropanoic acid'''. Unlike its counterpart α-alanine, β-alanine has no ]. |
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==Biosynthesis and industrial route== |
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β-Alanine is not used in the ] of any major ]s or ]s. It is formed ] by the degradation of ] and ]. It is a component of the naturally occurring ] carnosine and ] and also of ] (vitamin B<sub>5</sub>) which itself is a component of ]. Under normal conditions, β-alanine is ] into ]. |
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In terms of its ], it is formed by the degradation of ] and ]. ] is the ] ] which hydrolyses within the body to form β-alanine.<ref>{{cite journal|last1=Wright|first1=Margaret Robson|title=Arrhenius parameters for the acid hydrolysis of esters in aqueous solution. Part I. Glycine ethyl ester, β-alanine ethyl ester, acetylcholine, and methylbetaine methyl ester|journal=Journal of the Chemical Society B: Physical Organic|date=1969|pages=707–710|doi=10.1039/J29690000707}}</ref> It is produced industrially by the reaction of ammonia with ].<ref name=Ullmann>{{Ullmann|doi=10.1002/14356007.a13_507|title=Hydroxycarboxylic Acids, Aliphatic|year=2005|last1=Miltenberger|first1=Karlheinz|isbn=3527306730}}</ref> |
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Sources for β-alanine includes ] of cytosine and uracil. |
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β-Alanine is the rate-limiting precursor of ], which is to say carnosine levels are limited by the amount of available β-alanine. Supplementation with β-alanine has been shown to increase the concentration of carnosine in muscles, decrease fatigue in athletes and increase total muscular work done.<ref>{{cite journal|author=Derave W, Ozdemir MS, Harris R, Pottier A, Reyngoudt H, Koppo K, Wise JA, Achten E. |title=Beta-alanine supplementation augments muscle carnosine content and attenuates fatigue during repeated isokinetic contraction bouts in trained sprinters |journal=J Appl Physiol |date=August 9, 2007 |pmid = 17690198 |doi=10.1152/japplphysiol.00397.2007 |volume=103|issue=5 |pages=1736 }}</ref><ref name="Hill2007">{{cite journal|author=Hill CA, Harris RC, Kim HJ, Harris BD, Sale C, Boobis LH, Kim CK, Wise JA. |title=Influence of beta-alanine supplementation on skeletal muscle carnosine concentrations and high intensity cycling capacity |journal= Amino Acids |year=2007 |issue=2 |volume=32 |pages=225–33 |pmid =16868650 |doi=10.1007/s00726-006-0364-4 }}</ref> |
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==Biochemical function== |
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β-Alanine residues are rare. It is a component of the ] carnosine and ] and also of ] (vitamin B<sub>5</sub>), which itself is a component of ]. β-alanine is ] into ]. |
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=== Precursor of carnosine === |
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Typically studies have used supplementing strategies of multiple doses of 400 mg or 800 mg, administered at regular intervals for up to eight hours, over periods ranging from 4 to 10 weeks.<ref name="Hill2007"/><ref name="Harris2006">{{Cite journal | doi = 10.1007/s00726-006-0299-9 | last1 = Harris | first1 = RC | last2 = Tallon | first2 = MJ | last3 = Dunnett | first3 = M | last4 = Boobis | first4 = L | last5 = Coakley | first5 = J | last6 = Kim | first6 = HJ | last7 = Fallowfield | first7 = JL | last8 = Hill | first8 = CA | last9 = Sale | first9 = C ''et al.'' | year = 2006 | title = The absorption of orally supplied β-alanine and its effect on muscle carnosine synthesis in human vastus lateralis | url = | journal = Amino Acids | volume = 30 | issue = 3| pages = 279–289 | pmid = 16554972 }}</ref> After a 10 week supplementing strategy, the reported increase in intramuscular carnosine content was an average of 80.1% (range 18 to 205%).<ref name="Hill2007"/> |
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β-Alanine is the rate-limiting precursor of ], which is to say carnosine levels are limited by the amount of available β-alanine, not histidine.<ref name="pharmacistanswers.com">{{cite web|url=http://pharmacistanswers.com/beta-alanine-supplementation-for-exercise-performance.html|title=Beta-Alanine Supplementation For Exercise Performance|access-date=21 September 2018|archive-date=20 June 2017|archive-url=https://web.archive.org/web/20170620082252/http://www.pharmacistanswers.com/beta-alanine-supplementation-for-exercise-performance.html|url-status=dead}}</ref> Supplementation with β-alanine has been shown to increase the concentration of carnosine in muscles, decrease fatigue in athletes, and increase total muscular work done.<ref>{{cite journal|vauthors=Derave W, Ozdemir MS, Harris R, Pottier A, Reyngoudt H, Koppo K, Wise JA, Achten E |title=Beta-alanine supplementation augments muscle carnosine content and attenuates fatigue during repeated isokinetic contraction bouts in trained sprinters |journal=J Appl Physiol |date=August 9, 2007 |pmid = 17690198 |doi=10.1152/japplphysiol.00397.2007 |volume=103|issue=5 |pages=1736–43 |s2cid=6990201 }}</ref><ref name="Hill2007">{{cite journal|vauthors=Hill CA, Harris RC, Kim HJ, Harris BD, Sale C, Boobis LH, Kim CK, Wise JA |title=Influence of beta-alanine supplementation on skeletal muscle carnosine concentrations and high intensity cycling capacity |journal= Amino Acids |year=2007 |issue=2 |volume=32 |pages=225–33 |pmid =16868650 |doi=10.1007/s00726-006-0364-4 |s2cid=23988054 }}</ref> Simply supplementing with carnosine is not as effective as supplementing with β-alanine alone since carnosine, when taken orally, is broken down during digestion to its components, histidine and β-alanine. Hence, by weight, only about 40% of the dose is available as β-alanine.<ref name="pharmacistanswers.com"/> |
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<small>L</small>-], with a pKa of 6.1 is a relatively weak buffer over the physiological intramuscular pH range. However, when bound to other amino acids this increases nearer to 6.8-7.0. In particular, when bound to β-alanine the pKa value is 6.83,<ref>{{Cite journal | last1 = Bate-Smith | first1 = EC | year = 1938 | title = The buffering of muscle in rigor: protein, phosphate and carnosine | url = | journal = Journal of Physiology | volume = 92 | issue = 3| pages = 336–343 | pmid = 16994977 | pmc = 1395289 }}</ref> making this a very efficient intramuscular buffer. Furthermore, because of the position of the beta amino group, β-alanine dipeptides are not incorporated proteins and thus can be stored at relatively high concentrations (millimolar). Occurring at 17-25 mmol/kg (dry muscle),<ref>{{Cite journal | doi = 10.1007/BF00376439 | last1 = Mannion | first1 = AF | last2 = Jakeman | first2 = PM | last3 = Dunnett | first3 = M | last4 = Harris | first4 = RC | last5 = Willan | first5 = PLT | year = 1992 | title = Carnosine and anserine concentrations in the quadriceps femoris muscle of healthy humans | url = | journal = Eur. J. Appl. Physiol | volume = 64 | issue = | pages = 47–50 }}</ref> carnosine (β-alanyl-<small>L</small>-histidine) is an important intramuscular buffer, constituting 10-20% of the total buffering capacity in type I and II muscle fibres. |
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Because β-alanine dipeptides are not incorporated into proteins, they can be stored at relatively high concentrations. Occurring at 17–25 mmol/kg (dry muscle),<ref>{{Cite journal | doi = 10.1007/BF00376439 | pmid = 1735411 | last1 = Mannion | first1 = AF | last2 = Jakeman | first2 = PM | last3 = Dunnett | first3 = M | last4 = Harris | first4 = RC | last5 = Willan | first5 = PLT | year = 1992 | title = Carnosine and anserine concentrations in the quadriceps femoris muscle of healthy humans | journal = Eur. J. Appl. Physiol | volume = 64 | issue = 1| pages = 47–50 | s2cid = 24590951 }}</ref> carnosine (β-alanyl-<small>L</small>-histidine) is an important intramuscular buffer, constituting 10-20% of the total buffering capacity in type I and II muscle fibres. In carnosine, the pK<sub>a</sub> of the imidazolium group is 6.83, which is ideal for buffering.<ref>{{Cite journal | last1 = Bate-Smith | first1 = EC | year = 1938 | title = The buffering of muscle in rigor: protein, phosphate and carnosine | journal = Journal of Physiology | volume = 92 | issue = 3| pages = 336–343 | pmid = 16994977 | pmc = 1395289 | doi = 10.1113/jphysiol.1938.sp003605 }}</ref> |
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β-Alanine, provided in solution or as powder in gelatine capsules, however, causes ] when ingested in amounts above 10 mg per kg body weight (bwt).<ref name="Harris2006"/> This is variable between individuals. Symptoms may be experienced by some individuals as mild even at 10 mg per kg bwt, in a majority as significant at 20 mg per kg bwt, and severe at 40 mg per kg bwt.<ref name="Harris2006"/> However, an equivalent amount (equimolar) to 40 mg per kg bwt, ingested in the form of histidine containing dipeptides in chicken broth extract, did not cause paraesthesia.<ref name="Harris2006"/> |
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=== Receptors === |
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It is probable that the ], a form of neuropathic pain, results from high peak blood-plasma concentrations of β-alanine since greater quantities, ingested in the form of the β-alanine / histidine (or methylhistidine) containing dipeptides (i.e. carnosine and anserine) in meat, do not cause the same symptoms. In this case the β-alanine absorption profile is flattened but sustained for a longer period of time,<ref name="Harris2006"/> whereas, the β-alanine samples in the studies were administered as gelatine capsules containing powder. This resulted in plasma concentrations rising rapidly, peaking within 30 to 45 minutes, and being eliminated after 90 to 120 minutes. The paraesthesia caused is no indication of efficacy since the published studies undertaken so far have utilised doses of 400 mg or 800 mg at a time to avoid the paraesthesia. Furthermore, excretion of β-alanine in urine accounted for 0.60%(+/-0.09), 1.50%(+/-0.40) and 3.64%(+/-0.47) of the administered doses of 10, 20, or 40 mg per kg body weight,<ref name="Harris2006"/> indicating greater losses occurring with increasing dosage. |
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Even though much weaker than ] (and, thus, with a debated role as a physiological transmitter), β-alanine is an agonist next in activity to the cognate ligand glycine itself, for ]-sensitive inhibitory ]s (GlyRs) (the agonist order: glycine ≫ β-alanine > taurine ≫ alanine, <small>L</small>-serine > proline).<ref>''Encyclopedia of Life Sciences'' Amino Acid Neurotransmitters. Jeremy M Henley, 2001 John Wiley & Sons, Ltd. {{doi|10.1038/npg.els.0000010}}, Article Online Posting Date: April 19, 2001</ref> |
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β-alanine has five known receptor sites, including ], ] a co-agonist site (with glycine) on ], the aforementioned GlyR site, and blockade of GAT protein-mediated glial GABA uptake, making it a putative "small molecule neurotransmitter."<ref>{{cite journal |vauthors=Tiedje KE, Stevens K, Barnes S, Weaver DF |title=Beta-alanine as a small molecule neurotransmitter |journal=Neurochem Int |volume=57 |issue=3 |pages=177–88 |date=October 2010 |pmid=20540981 |doi=10.1016/j.neuint.2010.06.001 |s2cid=7814845 |url=}}</ref> |
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Even though much weaker than ] (and thus with a debated role as a physiological transmitter), β-alanine is an agonist next in activity to the cognate ligant glycine itself, for ]-sensitive inhibitory ]s (GlyRs) (the agonist order: glycine >> β-alanine > taurine >> alanine, <small>L</small>-serine > proline).<ref>''Encyclopedia of Life Sciences'' Amino Acid Neurotransmitters. Jeremy M Henley, 2001 John Wiley & Sons, Ltd. {{DOI|10.1038/npg.els.0000010}}, Article Online Posting Date: April 19, 2001</ref> |
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== Athletic performance enhancement == |
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A high potency ], called ], is derived from beta-alanine.<ref name="chemidplus">{{ChemID|102-66-9|Aspartic acid-beta-4-nitroanilide}}</ref> |
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There is evidence that β-alanine supplementation can increase exercise and cognitive performance,<ref name=quesnale>{{cite journal |vauthors=Quesnele JJ, Laframboise MA, Wong JJ, Kim P, Wells GD |title=The effects of beta-alanine supplementation on performance: a systematic review of the literature |journal=Int J Sport Nutr Exerc Metab |volume=24 |issue=1 |pages=14–27 |year=2014 |pmid=23918656 |doi=10.1123/ijsnem.2013-0007 |type=Systematic review}}</ref><ref name=hoffman>{{cite journal |vauthors=Hoffman JR, Stout JR, Harris RC, Moran DS |title=β-Alanine supplementation and military performance |journal=Amino Acids |volume=47 |issue=12 |pages=2463–74 |year=2015 |pmid=26206727 |pmc=4633445 |doi=10.1007/s00726-015-2051-9 }}</ref><ref name=hobson>{{cite journal |last1=Hobson |first1=R. M. |last2=Saunders |first2=B. |last3=Ball |first3=G. |last4=Harris |first4=R. C. |last5=Sale |first5=C. |title=Effects of β-alanine supplementation on exercise performance: a meta-analysis |journal=Amino Acids|date=9 December 2016 |volume=43 |issue=1 |pages=25–37|doi=10.1007/s00726-011-1200-z|pmc=3374095|issn=0939-4451|pmid=22270875}}</ref><ref name="issn2015"/> for some sporting modalities,<ref>{{cite journal |title=Ergogenic Effects of β-Alanine Supplementation on Different Sports Modalities: Strong Evidence or Only Incipient Findings? |first1=Gabriel M P |last1=Brisola |first2=Alessandro M |last2=Zagatto |journal=] |year=2019 |volume=33 |issue=1 |pages=253–282 |pmid= 30431532 |doi= 10.1519/JSC.0000000000002925 |s2cid=53441737 }}</ref> and exercises within a 0.5–10 min time frame.<ref>{{cite journal |title=β-alanine supplementation to improve exercise capacity and performance: a systematic review and meta-analysis FREE |author1=Bryan Saunders |author2=Kirsty Elliott-Sale |author3=Guilherme G Artioli1 |author4=Paul A Swinton |author5=Eimear Dolan |author6=Hamilton Roschel |author7=Craig Sale |author8=Bruno Gualano|journal=British Journal of Sports Medicine |year=2017 |volume=51 |issue=8 |pages=658–669 |pmid=27797728 |doi=10.1136/bjsports-2016-096396 |s2cid=25496458 |doi-access=free|hdl=10059/1913 |hdl-access=free }}</ref> β-alanine is converted within muscle cells into ], which acts as a buffer for the ] produced during high-intensity exercises, and helps delay the onset of neuromuscular fatigue.<ref name=hobson /><ref>{{cite journal |journal=Med Sci Sports Exerc |date=June 2010 |volume=42 |issue=6 |pages=1162–73 |title=Role of beta-alanine supplementation on muscle carnosine and exercise performance |author1=Guilherme Giannini Artioli |author2=Bruno Gualano |author3=Abbie Smith |author4=Jeffrey Stout |author5=Antonio Herbert Lancha Jr. |doi=10.1249/MSS.0b013e3181c74e38 |pmid=20479615|doi-access=free }}</ref> |
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Ingestion of β-alanine can cause ], reported as a tingling sensation, in a dose-dependent fashion.<ref name="issn2015">{{cite journal |vauthors=Trexler ET, Smith-Ryan AE, Stout JR, Hoffman JR, Wilborn CD, Sale C, Kreider RB, Jäger R, Earnest CP, Bannock L, Campbell B, Kalman D, Ziegenfuss TN, Antonio J |title=International society of sports nutrition position stand: Beta-Alanine |journal=J Int Soc Sports Nutr |volume=12 |pages=30 |year=2015 |pmid=26175657 |pmc=4501114 |doi=10.1186/s12970-015-0090-y |doi-access=free |type=Review}}</ref> Aside from this, no important adverse effect of β-alanine has been reported, however, there is also no information on the effects of its long-term usage or its safety in combination with other supplements, and caution on its use has been advised.<ref name=quesnale /><ref name=hoffman /> Furthermore, many studies have failed to test for the purity of the supplements used and check for the presence of banned substances.<ref name=hobson /> |
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== Metabolism == |
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β-Alanine can undergo a ] reaction with ] to form malonate-semialdehyde and <small>L</small>-alanine. The malonate semialdehyde can then be converted into ] via ]. Malonate is then converted into ] and enter ].<ref name=":0">{{Cite web|url=http://www.genome.jp/kegg-bin/show_pathway?scale=1.0&query=1.2.1.15&map=map00410&scale=&auto_image=&show_description=hide&multi_query=|title=KEGG PATHWAY: beta-Alanine metabolism - Reference pathway|website=www.genome.jp|access-date=2016-10-04}}</ref> |
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Alternatively, β-alanine can be diverted into ] and ] biosynthesis.<ref name=":0" /> |
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==References== |
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==References== |
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==External links== |
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==External links== |
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* {{Webarchive|url=https://web.archive.org/web/20090302170913/http://www.genome.ad.jp/kegg/pathway/map/map00410.html |date=2009-03-02 }} |
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{{Nucleotide metabolism intermediates}} |
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{{Nucleotide metabolism intermediates}} |
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{{GABA metabolism and transport modulators}} |
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{{Glycine receptor modulators}} |
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{{DEFAULTSORT:Alanine, Beta-}} |
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