Valine - wikipedia Valine Valine Names IUPAC name Valine Other names 2 - Amino - 3 - methylbutanoic acid Identifiers CAS Number 516 - 06 - 3 72 - 18 - 4 ( L - isomer ) 640 - 68 - 6 ( D - isomer ) 3D model ( JSmol ) Interactive image ChEBI CHEBI : 57762 ChEMBL ChEMBL43068 ChemSpider 6050 DrugBank DB00161 ECHA InfoCard 100.000. 703 EC Number 208 - 220 - 0 IUPHAR / BPS 4794 KEGG D00039 PubChem CID 1182 UNII 4CA13A832H InChI InChI = 1S / C5H11NO2 / c1 - 3 ( 2 ) 4 ( 6 ) 5 ( 7 ) 8 / h3 - 4H, 6H2, 1 - 2H3, ( H, 7, 8 ) / t4 - / m0 / s1 Key : KZSNJWFQEVHDMF - BYPYZUCNSA - N InChI = 1 / C5H11NO2 / c1 - 3 ( 2 ) 4 ( 6 ) 5 ( 7 ) 8 / h3 - 4H, 6H2, 1 - 2H3, ( H, 7, 8 ) / t4 - / m0 / s1 Key : KZSNJWFQEVHDMF - BYPYZUCNBW SMILES CC ( C ) ( C @ @ H ) ( C ( = O ) O ) N Properties Chemical formula C H NO Molar mass 117.15 g mol Density 1.316 g / cm Melting point 298 ° C ( 568 ° F ; 571 K ) ( decomposition ) Solubility in water soluble Acidity ( pK ) 2.32 ( carboxyl ), 9.62 ( amino ) Magnetic susceptibility ( χ ) - 74.3 10 cm / mol Supplementary data page Structure and properties Refractive index ( n ), Dielectric constant ( ε ), etc. Thermodynamic data Phase behaviour solid -- liquid -- gas Spectral data UV, IR, NMR, MS Except where otherwise noted, data are given for materials in their standard state ( at 25 ° C ( 77 ° F ), 100 kPa ). Y verify ( what is ? ) Infobox references Valine ( symbol Val or V ) is an α - amino acid that is used in the biosynthesis of proteins. It contains an α - amino group ( which is in the protonated − NH form under biological conditions ), an α - carboxylic acid group ( which is in the deprotonated − COO form under biological conditions ), and a side chain isopropyl group, making it a non-polar aliphatic amino acid. It is essential in humans, meaning the body can not synthesize it : it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, beans and legumes. In the genetic code it is encoded by all codons starting with GU, namely GUU, GUC, GUA, and GUG. Like leucine and isoleucine, valine is a branched - chain amino acid. In sickle - cell disease, a single glutamic acid in β - globin is replaced with valine. Because valine is hydrophobic, whereas glutamic acid is hydrophilic, this change makes the hemoglobin prone to abnormal aggregation. Contents 1 History and etymology 2 Nomenclature 3 Metabolism 3.1 Source and biosynthesis 3.2 Degradation 4 Synthesis 5 Medical Significance 5.1 Insulin resistance 5.2 Hematopoietic stem cells 6 See also 7 References 8 External links History and etymology Valine was first isolated from casein in 1901 by Hermann Emil Fischer. The name valine comes from valeric acid, which in turn is named after the plant valerian due to the presence of the acid in the roots of the plant. Nomenclature According to IUPAC, carbon atoms forming valine are numbered sequentially starting from 1 denoting the carboxyl carbon, whereas 4 and 4 ' denote the two terminal methyl carbons. Metabolism Source and biosynthesis Valine, like other branched - chain amino acids, is synthesized by plants, but not by animals. It is therefore an essential amino acid in animals, and needs to be present in the diet. Adult humans require about 4 mg / kg body weight daily. It is synthesized in plants and bacteria via several steps starting from pyruvic acid. The initial part of the pathway also leads to leucine. The intermediate α - ketoisovalerate undergoes reductive amination with glutamate. Enzymes involved in this biosynthesis include : Acetolactate synthase ( also known as acetohydroxy acid synthase ) Acetohydroxy acid isomeroreductase Dihydroxyacid dehydratase Valine aminotransferase Degradation Like other branched - chain amino acids, the catabolism of valine starts with the removal of the amino group by transamination, giving alpha - ketoisovalerate, an alpha - keto acid, which is converted to isobutyryl - CoA through oxidative decarboxylation by the branched - chain α - ketoacid dehydrogenase complex. This is further oxidised and rearranged to succinyl - CoA, which can enter the citric acid cycle. Synthesis Racemic valine can be synthesized by bromination of isovaleric acid followed by amination of the α - bromo derivative HO CCH CH ( CH ) + Br → HO CCHBrCH ( CH ) + HBr HO CCHBrCH ( CH ) + 2 NH → HO CCH ( NH ) CH ( CH ) + NH Br Medical significance Insulin resistance Valine, like other branched - chain amino acids, is associated with insulin resistance : higher levels of valine are observed in the blood of diabetic mice, rats, and humans. Mice fed a valine deprivation diet for one day have improved insulin sensitivity, and feeding of a valine deprivation diet for one week significantly decreases blood glucose levels. In diet - induced obese and insulin resistant mice, a diet with decreased levels of valine and the other branched - chain amino acids results in reduced adiposity and improved insulin sensitivity. The valine catabolite 3 - hydroxyisobutyrate promotes skeletal muscle insulin resistance in mice by stimulating fatty acid uptake into muscle and lipid accumulation. In humans, a protein restricted diet lowers blood levels of valine and decreases fasting blood glucose levels. Hematopoietic stem cells Dietary valine is essential for hematopoietic stem cell ( HSC ) self - renewal, as demonstrated by experiments in mice. Dietary valine restriction selectively depletes long - term repopulating HSC in mouse bone marrow. Successful stem cell transplantation was achieved in mice without irradiation after 3 weeks on a valine restricted diet. Long term survival of the transplanted mice was achieved when valine was returned to the diet gradually over a 2 - week period to avoid refeeding syndrome. See also Valinol References Jump up ^ Dawson, R.M.C., et al., Data for Biochemical Research, Oxford, Clarendon Press, 1959. Jump up ^ Weast, Robert C., ed. ( 1981 ). CRC Handbook of Chemistry and Physics ( 62nd ed. ). Boca Raton, FL : CRC Press. p. C - 569. ISBN 0 - 8493 - 0462 - 8. Jump up ^ `` 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. Jump up ^ `` valine ''. Encyclopædia Britannica Online. Retrieved 2015 - 12 - 06. Jump up ^ `` valine ''. Merriam - Webster Online Dictionary. Retrieved 2015 - 12 - 06. Jump up ^ `` valeric acid ''. Merriam - Webster Online Dictionary. Retrieved 2015 - 12 - 06. Jump up ^ Jones, J.H., ed. ( 1985 ). Amino Acids, Peptides and Proteins. Specialist Periodical Reports. 16. London : Royal Society of Chemistry. p. 389. ISBN 978 - 0 - 85186 - 144 - 9. Jump up ^ Basuchaudhuri, Pranab ( 2016 ). Nitrogen metabolism in rice. Boca Raton, Florida : CRC Press. p. 159. ISBN 9781498746687. OCLC 945482059. Jump up ^ Institute of Medicine ( 2002 ). `` Protein and Amino Acids ''. Dietary Reference Intakes for Energy, Carbohydrates, Fiber, Fat, Fatty Acids, Cholesterol, Protein, and Amino Acids. Washington, DC : The National Academies Press. pp. 589 -- 768. Jump up ^ Lehninger, Albert L. ; Nelson, David L. ; Cox, Michael M. ( 2000 ). Principles of Biochemistry ( 3rd ed. ). New York : W. H. Freeman. ISBN 1 - 57259 - 153 - 6... Jump up ^ Mathews, Christopher K., ( 2000 ). Biochemistry. Van Holde, K.E., Ahern, Kevin G. ( 3rd ed. ). San Francisco, Calif. : Benjamin Cummings. p. 776. ISBN 0805330666. OCLC 42290721. Jump up ^ Marvel, C.S. ( 1940 ). `` dl - Valine ''. Organic Syntheses. 20 : 106. ; Collective Volume, 3, p. 848. Jump up ^ Lynch, Christopher J. ; Adams, Sean H. ( 2014 - 12 - 01 ). `` Branched - chain amino acids in metabolic signalling and insulin resistance ''. Nature Reviews. Endocrinology. 10 ( 12 ) : 723 -- 736. doi : 10.1038 / nrendo. 2014.171. ISSN 1759 - 5037. PMC 4424797. PMID 25287287. Jump up ^ Xiao, Fei ; Yu, Junjie ; Guo, Yajie ; Deng, Jiali ; Li, Kai ; Du, Ying ; Chen, Shanghai ; Zhu, Jianmin ; Sheng, Hongguang ( 2014 - 06 - 01 ). `` Effects of individual branched - chain amino acids deprivation on insulin sensitivity and glucose metabolism in mice ''. Metabolism : Clinical and Experimental. 63 ( 6 ) : 841 -- 850. doi : 10.1016 / j. metabol. 2014.03. 006. ISSN 1532 - 8600. PMID 24684822. Jump up ^ Cummings, Nicole E. ; Williams, Elizabeth M. ; Kasza, Ildiko ; Konon, Elizabeth N. ; Schaid, Michael D. ; Schmidt, Brian A. ; Poudel, Chetan ; Sherman, Dawn S. ; Yu, Deyang ( 2017 - 12 - 19 ). `` Restoration of metabolic health by decreased consumption of branched - chain amino acids ''. The Journal of Physiology. doi : 10.1113 / JP275075. ISSN 1469 - 7793. PMID 29266268. Jump up ^ Jang, Cholsoon ; Oh, Sungwhan F. ; Wada, Shogo ; Rowe, Glenn C. ; Liu, Laura ; Chan, Mun Chun ; Rhee, James ; Hoshino, Atsushi ; Kim, Boa ( 2016 - 04 - 01 ). `` A branched - chain amino acid metabolite drives vascular fatty acid transport and causes insulin resistance ''. Nature Medicine. 22 ( 4 ) : 421 -- 426. doi : 10.1038 / nm. 4057. ISSN 1546 - 170X. PMC 4949205. PMID 26950361. Jump up ^ Fontana, Luigi ; Cummings, Nicole E. ; Arriola Apelo, Sebastian I. ; Neuman, Joshua C. ; Kasza, Ildiko ; Schmidt, Brian A. ; Cava, Edda ; Spelta, Francesco ; Tosti, Valeria ( 2016 - 06 - 21 ). `` Decreased Consumption of Branched - Chain Amino Acids Improves Metabolic Health ''. Cell Reports. 16 : 520 -- 30. doi : 10.1016 / j. celrep. 2016.05. 092. ISSN 2211 - 1247. PMC 4947548. PMID 27346343. Jump up ^ Taya, Yuki ; Ota, Yasunori ; Wilkinson, Adam C. ; Kanazawa, Ayano ; Watarai, Hiroshi ; Kasai, Masataka ; Nakauchi, Hiromitsu ; Yamazaki, Satoshi ( 2016 - 12 - 02 ). `` Depleting dietary valine permits nonmyeloablative mouse hematopoietic stem cell transplantation ''. Science. 354 ( 6316 ) : 1152 -- 1155. doi : 10.1126 / science. aag3145. External links Valine MS Spectrum Isoleucine and valine biosynthesis Valine 's relationship to prions Encoded ( proteinogenic ) amino acids General topics Protein Peptide Genetic code By properties Aliphatic Branched - chain amino acids ( Valine Isoleucine Leucine ) Methionine Alanine Proline Glycine Aromatic Phenylalanine Tyrosine Tryptophan Histidine Polar, uncharged Asparagine Glutamine Serine Threonine Positive charge ( pK ) Lysine ( ≈ 10.8 ) Arginine ( ≈ 12.5 ) Histidine ( ≈ 6.1 ) Negative charge ( pK ) Aspartic acid ( ≈ 3.9 ) Glutamic acid ( ≈ 4.1 ) Cysteine ( ≈ 8.3 ) Tyrosine ( ≈ 10.1 ) Amino acids types : Encoded ( proteins ) Essential Non-proteinogenic Ketogenic Glucogenic Imino acids D - amino acids Dehydroamino acids Amino acid metabolism metabolic intermediates K → acetyl - CoA lysine → Saccharopine Allysine α - Aminoadipic acid α - Ketoadipate Glutaryl - CoA Glutaconyl - CoA Crotonyl - CoA β - Hydroxybutyryl - CoA leucine → 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 tryptophan → alanine → N ' - Formylkynurenine Kynurenine Anthranilic acid 3 - Hydroxykynurenine 3 - Hydroxyanthranilic acid 2 - Amino - 3 - carboxymuconic semialdehyde 2 - Aminomuconic semialdehyde 2 - Aminomuconic acid Glutaryl - CoA G → pyruvate → citrate glycine → serine → 3 - Phosphoglyceric acid glycine → creatine : Glycocyamine Phosphocreatine Creatinine G → glutamate → α - ketoglutarate histidine → Urocanic acid Imidazol - 4 - one - 5 - propionic acid Formiminoglutamic acid Glutamate - 1 - semialdehyde proline → 1 - Pyrroline - 5 - carboxylic acid arginine → Agmatine Ornithine Citrulline Cadaverine Putrescine other cysteine + glutamate → glutathione : γ - Glutamylcysteine G → propionyl - CoA → succinyl - CoA valine → α - Ketoisovaleric acid Isobutyryl - CoA Methacrylyl - CoA 3 - Hydroxyisobutyryl - CoA 3 - Hydroxyisobutyric acid 2 - Methyl - 3 - oxopropanoic acid isoleucine → 2, 3 - Dihydroxy - 3 - methylpentanoic acid 2 - Methylbutyryl - CoA Tiglyl - CoA 2 - Methylacetoacetyl - CoA methionine → generation of homocysteine : S - Adenosyl methionine S - Adenosyl - L - homocysteine Homocysteine conversion to cysteine : Cystathionine alpha - Ketobutyric acid + Cysteine threonine → α - Ketobutyric acid propionyl - CoA → Methylmalonyl - CoA G → fumarate phenylalanine → tyrosine → 4 - Hydroxyphenylpyruvic acid Homogentisic acid 4 - Maleylacetoacetic acid G → oxaloacetate see urea cycle Other Cysteine metabolism Cysteine sulfinic acid Retrieved from `` https://en.wikipedia.org/w/index.php?title=Valine&oldid=836252341 '' Categories : Branched - chain amino acids Proteinogenic amino acids Glucogenic amino acids Essential amino acids Isobutyrates Isopropyl compounds Hidden categories : Chemical articles with multiple compound IDs Multiple chemicals in an infobox that need indexing Chemical articles with multiple CAS registry numbers ECHA InfoCard ID from Wikidata Chemical articles having a data page Articles containing unverified chemical infoboxes Use dmy dates from March 2018 Talk Contents About Wikipedia Afrikaans تۆرکجه Bân - lâm - gú Беларуская Беларуская ( тарашкевіца ) ‎ Български Català Čeština Dansk Deutsch Eesti Ελληνικά Español Esperanto Euskara فارسی Français Galego 한국어 Հայերեն Hrvatski Bahasa Indonesia Italiano עברית Қазақша Kurdî Кыргызча Latviešu Lëtzebuergesch Lietuvių Magyar Македонски Nederlands 日本 語 Norsk Norsk nynorsk Occitan Oʻzbekcha / ўзбекча Polski Português Română Русский Scots Slovenčina Slovenščina Српски / srpski Srpskohrvatski / српскохрватски Suomi Svenska தமிழ் ไทย Türkçe Українська Tiếng Việt West - Vlams 粵語 中文 49 more Edit links This page was last edited on 13 April 2018, at 16 : 26. Text is available under the Creative Commons Attribution - ShareAlike License ; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia ® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization. About Wikipedia

Question: the side chain for valine is classified as a
Answer: isopropyl group