Difference between revisions of "Serine" - New World Encyclopedia
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| + | ! {{chembox header}}| '''Serine''' | ||
| + | |- | ||
| + | | align="center" colspan="2" | [[Image:L-serine-skeletal.png|110px|Chemical structure of Serine]] [[Image:L-serine-3D-sticks.png|110px|Chemical structure of {{PAGENAME}}]] | ||
| + | |- | ||
| + | | style="width: 30%;" | [[IUPAC nomenclature|Systematic name]] | ||
| + | | (''S'')-2-amino-3-hydroxypropanoic acid | ||
| + | |- | ||
| + | | Abbreviations | ||
| + | | '''Ser<br/>S''' | ||
| + | |- | ||
| + | | [[Chemical formula]] | ||
| + | | C<sub>3</sub>H<sub>7</sub>NO<sub>3</sub> | ||
| + | |- | ||
| + | | [[Molecular mass]] | ||
| + | | 105.09 g mol<sup>-1</sup> | ||
| + | |- | ||
| + | | [[Melting point]] | ||
| + | | 228 °C | ||
| + | |- | ||
| + | | [[Density]] | ||
| + | | 1.537 g cm<sup>-3</sup> | ||
| + | |- | ||
| + | | [[Isoelectric point]] | ||
| + | | 5.68 | ||
| + | |- | ||
| + | | [[Acid dissociation constant|p''K''<sub>a</sub>]] | ||
| + | | 2.13<br/>9.05 | ||
| + | |- | ||
| + | | [[CAS registry number|CAS number]] | ||
| + | | [56-45-1] | ||
| + | |- | ||
| + | | [[PubChem]] | ||
| + | | [http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi?cid=5951 5951] | ||
| + | |- | ||
| + | | [[EINECS number]] | ||
| + | | 200-274-3 | ||
| + | |- | ||
| + | | {{chembox SMILES||value=N[C@@H](CO)C(O)=O}} | ||
| + | |- | ||
| + | | {{chembox header}} | <small>[[wikipedia:Chemical infobox|Disclaimer and references]]</small> | ||
| + | |- | ||
| + | |} | ||
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| + | '''Serine''' ([[International Phonetic Alphabet|IPA]] {{IPA|[ˈsɛɹin]}}) is the [[organic compound]] with the [[chemical formula|formula]] HO<sub>2</sub>CCH(NH<sub>2</sub>)CH<sub>2</sub>OH. It is one of the 20 [[amino acid]]s commonly found in animal [[protein]]s. Its three letter code is ser, its one letter code is S, and its codons are AGU and AGC.<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> Only the L-[[stereoisomer]] appears in mammalian protein. 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. Without the [[esterase]] activity that usually destroys [[acetylcholine]] as soon as it performs its function, dangerously high levels of this [[neurotransmitter]] build up, quickly resulting in [[convulsion]]s 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. | ||
| + | |||
| + | ==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 | ||
| + | |||
| + | ==References== | ||
| + | <references/> | ||
| + | |||
| + | == External links == | ||
| + | * [http://www.compchemwiki.org/index.php?title=Serine Computational Chemistry Wiki] | ||
| + | {{ChemicalSources}} | ||
| + | |||
| + | {{AminoAcids}} | ||
| + | |||
| + | [[Category:Proteinogenic amino acids]] | ||
| + | [[Category:Glucogenic amino acids]] | ||
| + | {{credit|137243769}} | ||
| + | [[Category:Life sciences]] | ||
Revision as of 15:38, 15 June 2007
| Serine | |
|---|---|
 
| |
| Systematic name | (S)-2-amino-3-hydroxypropanoic acid |
| Abbreviations | Ser S |
| Chemical formula | C3H7NO3 |
| Molecular mass | 105.09 g mol-1 |
| Melting point | 228 °C |
| Density | 1.537 g cm-3 |
| Isoelectric point | 5.68 |
| pKa | 2.13 9.05 |
| CAS number | [56-45-1] |
| PubChem | 5951 |
| EINECS number | 200-274-3 |
| SMILES | N[C@@H](CO)C(O)=O |
| Disclaimer and references | |
Serine (IPA [ˈsɛɹin]) is the organic compound with the formula HO2CCH(NH2)CH2OH. It is one of the 20 amino acids commonly found in animal proteins. Its three letter code is ser, its one letter code is S, and its codons are AGU and AGC.[1] Only the L-stereoisomer appears in mammalian protein. 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).[2]
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 sphingolipids. 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 enzymes. It has been shown to occur in the active sites of chymotrypsin, trypsin, and many other enzymes. The so-called nerve gases and many substances used in insecticides have been shown to act by combining with a residue of serine in the active site of acetylcholine esterase, inhibiting the enzyme completely. Without the esterase activity that usually destroys acetylcholine as soon as it performs its function, dangerously high levels of this neurotransmitter build up, quickly resulting in convulsions 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 phosphorylated by kinases during cell signaling in eukaryotes. Phosphorylated serine residues are often referred to as phosphoserine. Serine proteases 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 receptors in the brain.
Chemical Synthesis
Serine is prepared from methyl acrylate.[3]
See also
- Serine aggregation properties in Serine octamer clusters
ReferencesISBN links support NWE through referral fees
- ↑ IUPAC-IUBMB Joint Commission on Biochemical Nomenclature. Nomenclature and Symbolism for Amino Acids and Peptides. Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc. Retrieved 2007-05-17.
- ↑ Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. ISBN 1-57259-153-6.
- ↑ Carter, H. E.; West, H. D. “dl-Serine” Organic Syntheses, Collected Volume 3, p.774 (1955). http://www.orgsyn.org/orgsyn/pdfs/CV3P0774.pdf
External links
Template:ChemicalSources
| Major families of biochemicals | ||
| Peptides | Amino acids | Nucleic acids | Carbohydrates | Nucleotide sugars | Lipids | Terpenes | Carotenoids | Tetrapyrroles | Enzyme cofactors | Steroids | Flavonoids | Alkaloids | Polyketides | Glycosides | ||
| Analogues of nucleic acids: | The 20 Common Amino Acids | Analogues of nucleic acids: |
| Alanine (dp) | Arginine (dp) | Asparagine (dp) | Aspartic acid (dp) | Cysteine (dp) | Glutamic acid (dp) | Glutamine (dp) | Glycine (dp) | Histidine (dp) | Isoleucine (dp) | Leucine (dp) | Lysine (dp) | Methionine (dp) | Phenylalanine (dp) | Proline (dp) | Serine (dp) | Threonine (dp) | Tryptophan (dp) | Tyrosine (dp) | Valine (dp) | ||
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