Serine 63551 219239317 2008-06-14T07:02:28Z AlnoktaBOT 3096998 robot Modifying: [[id:Serin]] {{NatOrganicBox | image= [[Image:L-serine-skeletal.png|160px|Skeletal formula of serine]]<br>[[Image:L-serine-3D-sticks.png|140px|Stick model of the serine molecule]] | name=(''S'')-2-amino-3-hydroxypropanoic acid | PubChem = 617 | CAS = 56-45-1 | SMILES = OCC(N)C(=O)O | C=3 | H=7 | N=1 | O=3 | mass=105.09 g/mol }} '''Serine''' (abbreviated as '''Ser''' or '''S''')<ref>{{cite web | author=IUPAC-IUBMB Joint Commission on Biochemical Nomenclature | title=Nomenclature and Symbolism for Amino Acids and Peptides | work=Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc | url=http://www.chem.qmul.ac.uk/iupac/AminoAcid/ | accessdate=2007-05-17}}</ref> is an [[organic compound]] with the [[chemical formula|formula]] [[hydrogen|H]][[oxygen|O]]<sub>2</sub>[[carbon|C]]CH([[nitrogen|N]]H<sub>2</sub>)CH<sub>2</sub>OH. It is one of the 20 naturally occurring [[proteins|proteinogenic]] [[amino acid]]s. Its [[codon]]s are UCU, UCC, UCA, UCG, AGU and AGC. Only the L-[[stereoisomer]] appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other [[metabolites]], including [[glycine]]. Serine was first obtained from [[silk]] protein, a particularly rich source, in 1865. Its name is derived from the [[Latin]] for silk, ''sericum''. Serine's structure was established in 1902. The hydroxyl group attached makes it a polar amino acid. ==Biosynthesis== The synthesis of serine starts with the [[oxidation]] of [[3-phosphoglycerate]] forming [[3-phosphohydroxypyruvate]] and [[NADH]]. [[Reductive amination]] of this ketone followed by hydrolysis affords serine. [[Serine hydroxymethyltransferase]] catalyzes the reversible, simultaneous conversions of L-serine to [[glycine]] (retro-aldol cleavage) and [[5,6,7,8-tetrahydrofolate]] to [[5,10-methylenetetrahydrofolate]] (hydrolysis).<ref>Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. ISBN 1-57259-153-6.</ref> ==Function== ===Metabolic=== Serine is important in [[metabolism]] in that it participates in the [[biosynthesis]] of [[purines]] and [[pyrimidines]]. It is also the precursor to several amino acids, including [[glycine]], [[cysteine]], [[tryptophan]] (in bacteria). It is also the precursor to numerous of other metabolites, including [[sphingolipid]]s. Serine is also a precursor to [[folate]], which is the principal donor of one carbon fragments in biosynthesis. ===Structural=== Serine plays an important role in the catalytic function of many [[enzyme]]s. It has been shown to occur in the active sites of [[chymotrypsin]], [[trypsin]], and many other enzymes. The so-called [[nerve gas]]es and many substances used in [[insecticide]]s have been shown to act by combining with a residue of serine in the active site of [[acetylcholine esterase]], inhibiting the enzyme completely. The unmetabolized acetylcholine cannot be recycled into the nerve for signaling. This results in depletion of [[acetylcholine]] at the neuromuscular junction, resulting in the inability to control muscles, which results in [[asphyxia|asphyxiation]], and death. As a constituent (residue) of proteins, its [[side chain]] can undergo O-linked [[glycosylation]]. This might be important in explaining some of the devastating consequences of [[diabetes]]. It is one of three amino acid residues that are commonly [[phosphorylation|phosphorylated]] by [[kinases]] during [[signal transduction|cell signaling]] in [[eukaryote]]s. Phosphorylated serine residues are often referred to as [[phosphoserine]]. [[Serine protease]]s are a common type of protease. ===Signaling=== D-serine, synthesized by [[serine racemase]] from L-serine, serves as a neuronal signaling molecule by activating [[NMDA receptor]]s in the brain.<ref>D-Serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor http://www.pnas.org/cgi/content/full/97/9/4926</ref> ==Chemical Synthesis== Serine is prepared from methyl acrylate.<ref>Carter, H. E.; West, H. D. “dl-Serine” Organic Syntheses, Collected Volume 3, p.774 (1955). http://www.orgsyn.org/orgsyn/pdfs/CV3P0774.pdf</ref> ==See also== * Serine aggregation properties in [[Serine octamer cluster]]s * [http://www.compchemwiki.org/index.php?title=Serine Computational Chemistry Wiki] == References == <references/> {{AminoAcids}} [[Category:Proteinogenic amino acids]] [[Category:Glucogenic amino acids]] [[ar:سيرين]] [[ca:Serina]] [[cs:Serin]] [[da:Serin]] [[de:Serin]] [[et:Seriin]] [[es:Serina]] [[eo:Serino]] [[fr:Sérine]] [[ko:세린]] [[hr:Serin]] [[id:Serin]] [[it:Serina (chimica)]] [[he:סרין]] [[lv:Serīns]] [[lb:Serin]] [[lt:Serinas]] [[hu:Szerin]] [[nl:Serine]] [[ja:セリン]] [[no:Serin]] [[pl:Seryna]] [[pt:Serina]] [[ru:Серин]] [[fi:Seriini]] [[sv:Serin]] [[ta:செர்ரீன்]] [[tr:Serin]] [[uk:Серин]] [[zh:絲氨酸]]