Serine
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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]]
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