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In chemistry, acylation is a broad class of chemical reactions in which an acyl group (R−C=O) is added to a substrate. The compound providing the acyl group is called the acylating agent. The substrate to be acylated and the product include the following:

A particularly common type of acylation is acetylation, the addition of the acetyl group. Closely related to acylation is formylation, which employ sources of "HCO⁺ in place of "RCO⁺".

Examples

Because they form a strong electrophile when treated with Lewis acids, acyl halides are commonly used as acylating agents. For example, Friedel–Crafts acylation uses acetyl chloride (CH₃COCl) as the agent and aluminum chloride (AlCl₃) as a catalyst to add an acetyl group to benzene:^[2]

This reaction is an example of electrophilic aromatic substitution.

Acyl halides and acid anhydrides of carboxylic acids are also common acylating agents. In some cases, active esters exhibit comparable reactivity. All react with amines to form amides and with alcohols to form esters by nucleophilic acyl substitution.

Acylation can be used to prevent rearrangement reactions that would normally occur in alkylation. To do this an acylation reaction is performed, then the carbonyl is removed by Clemmensen reduction or a similar process.^[3]

Acylation in biology

Protein acylation is the post-translational modification of proteins via the attachment of functional groups through acyl linkages. Protein acylation has been observed as a mechanism controlling biological signaling.^[4] One prominent type is fatty acylation, the addition of fatty acids to particular amino acids (e.g. myristoylation, palmitoylation or palmitoleoylation).^[5] Different types of fatty acids engage in global protein acylation.^[6] Palmitoleoylation is an acylation type where the monounsaturated fatty acid palmitoleic acid is covalently attached to serine or threonine residues of proteins.^[7]^[8] Palmitoleoylation appears to play a significant role in the trafficking, targeting, and function of Wnt proteins.^[9]^[10]

References

^ 裴, 坚. 基础有机化学 [Basic Organic Chemistry] (4th ed.). p. 508. ISBN 978-7-301-27212-1.
^ Brown, William H.; Iverson, Brent L.; Anslyn, Eric V.; Foote, Christopher S. (2017). Organic Chemistry (8th ed.). Boston, MA: Cengage Learning. p. 1002. ISBN 978-1-305-58035-0. OCLC 974377227.
^ Vollhardt, Peter; Neil E. Schore (2014). Organic Chemistry: Structure and Function (7th ed.). New York, NY: W.H. Freeman and Company. pp. 714–715. ISBN 978-1-4641-2027-5.
^ Towler, D A; Gordon, J I; Adams, S P; Glaser, L (1988). "The Biology and Enzymology of Eukaryotic Protein Acylation". Annual Review of Biochemistry. 57 (1): 69–97. doi:10.1146/annurev.bi.57.070188.000441. PMID 3052287.
^ Resh, M. D. (1999). "Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1451 (1): 1–16. doi:10.1016/S0167-4889(99)00075-0. PMID 10446384.
^ Mohammadzadeh, Fatemeh; Hosseini, Vahid; Mehdizadeh, Amir; Dani, Christian; Darabi, Masoud (2019). "A method for the gross analysis of global protein acylation by gas–liquid chromatography". IUBMB Life. 71 (3): 340–346. doi:10.1002/iub.1975. ISSN 1521-6551. PMID 30501005.
^ Hannoush, Rami N. (October 2015). "Synthetic protein lipidation". Current Opinion in Chemical Biology. 28: 39–46. doi:10.1016/j.cbpa.2015.05.025. ISSN 1879-0402. PMID 26080277.
^ Pelegri, Francisco; Danilchik, Michael; Sutherland, Ann (2016-12-13). Vertebrate development : maternal to zygotic control. Cham, Switzerland. ISBN 9783319460956. OCLC 966313034.{{cite book}}: CS1 maint: location missing publisher (link)
^ Hosseini, Vahid; Dani, Christian; Geranmayeh, Mohammad Hossein; Mohammadzadeh, Fatemeh; Nazari Soltan Ahmad, Saeed; Darabi, Masoud (2018-10-20). "Wnt lipidation: Roles in trafficking, modulation, and function". Journal of Cellular Physiology. 234 (6): 8040–8054. doi:10.1002/jcp.27570. ISSN 1097-4652. PMID 30341908. S2CID 53009014.
^ Nile, Aaron H.; Hannoush, Rami N. (February 2016). "Fatty acylation of Wnt proteins". Nature Chemical Biology. 12 (2): 60–69. doi:10.1038/nchembio.2005. ISSN 1552-4469. PMID 26784846.

[1] 裴, 坚. 基础有机化学 [Basic Organic Chemistry] (4th ed.). p. 508. ISBN 978-7-301-27212-1.

[2] Brown, William H.; Iverson, Brent L.; Anslyn, Eric V.; Foote, Christopher S. (2017). Organic Chemistry (8th ed.). Boston, MA: Cengage Learning. p. 1002. ISBN 978-1-305-58035-0. OCLC 974377227.

[3] Vollhardt, Peter; Neil E. Schore (2014). Organic Chemistry: Structure and Function (7th ed.). New York, NY: W.H. Freeman and Company. pp. 714–715. ISBN 978-1-4641-2027-5.

[4] Towler, D A; Gordon, J I; Adams, S P; Glaser, L (1988). "The Biology and Enzymology of Eukaryotic Protein Acylation". Annual Review of Biochemistry. 57 (1): 69–97. doi:10.1146/annurev.bi.57.070188.000441. PMID 3052287.

[5] Resh, M. D. (1999). "Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1451 (1): 1–16. doi:10.1016/S0167-4889(99)00075-0. PMID 10446384.

[6] Mohammadzadeh, Fatemeh; Hosseini, Vahid; Mehdizadeh, Amir; Dani, Christian; Darabi, Masoud (2019). "A method for the gross analysis of global protein acylation by gas–liquid chromatography". IUBMB Life. 71 (3): 340–346. doi:10.1002/iub.1975. ISSN 1521-6551. PMID 30501005.

[7] Hannoush, Rami N. (October 2015). "Synthetic protein lipidation". Current Opinion in Chemical Biology. 28: 39–46. doi:10.1016/j.cbpa.2015.05.025. ISSN 1879-0402. PMID 26080277.

[8] Pelegri, Francisco; Danilchik, Michael; Sutherland, Ann (2016-12-13). Vertebrate development : maternal to zygotic control. Cham, Switzerland. ISBN 9783319460956. OCLC 966313034.{{cite book}}: CS1 maint: location missing publisher (link)

[9] Hosseini, Vahid; Dani, Christian; Geranmayeh, Mohammad Hossein; Mohammadzadeh, Fatemeh; Nazari Soltan Ahmad, Saeed; Darabi, Masoud (2018-10-20). "Wnt lipidation: Roles in trafficking, modulation, and function". Journal of Cellular Physiology. 234 (6): 8040–8054. doi:10.1002/jcp.27570. ISSN 1097-4652. PMID 30341908. S2CID 53009014.

[10] Nile, Aaron H.; Hannoush, Rami N. (February 2016). "Fatty acylation of Wnt proteins". Nature Chemical Biology. 12 (2): 60–69. doi:10.1038/nchembio.2005. ISSN 1552-4469. PMID 26784846.

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@@ Line 1: / Line 1: @@
+{{short description|1=Chemical reaction which adds an acyl group (R–C=O) to a compound}}
-In [[chemistry]], '''acylation''' (or alkanoylation) is the process of adding an [[acyl]] group to a compound. The compound providing the acyl group is called the '''acylating agent'''.
+{{see also|Acyl group}}
-Because they form a strong [[electrophile]] when treated with some metal [[catalyst]]s, [[acyl halide]]s are commonly used as acylating agents. For example, [[Friedel-Crafts reaction|Friedel-Crafts acylation]] uses [[acetyl chloride]] (ethanoyl chloride), [[Acetyl chloride|CH<sub>3</sub>COCl]], as the agent and aluminum chloride (AlCl<sub>3</sub>) as a catalyst to add an ethanoyl ([[acetyl]]) group to [[benzene]]:
+In [[chemistry]], '''acylation''' is a broad class of [[chemical reaction]]s in which an [[acyl]] group ({{chem2|R\sC\dO}}) is added to a substrate. The compound providing the acyl group is called the '''acylating agent'''.  The substrate to be acylated and the product include the following:
+*[[Alcohol (chemistry)|alcohols]], [[ester]]s
+*[[Amine|amines]], [[amide]]s
+*[[Aromatic compound|arenes]] or [[Alkene|alkenes]],<ref>{{Cite book |last=裴 |first=坚 |title=基础有机化学 |isbn=978-7-301-27212-1 |edition=4th |pages=508 |trans-title=Basic Organic Chemistry}}</ref> [[ketone]]s
+A particularly common type of acylation is [[acetylation]], the addition of the acetyl group. Closely related to acylation is [[formylation]], which employ sources of "HCO<sup>+</sup> in place of "RCO<sup>+</sup>".
+==Examples==
+Because they form a strong [[electrophile]] when treated with [[Lewis acid]]s, [[acyl halide]]s are commonly used as acylating agents. For example, [[Friedel–Crafts reaction|Friedel–Crafts acylation]] uses [[acetyl chloride]] ({{chem2|CH3COCl}}) as the agent and [[Aluminium chloride|aluminum chloride]] ({{chem2|AlCl3}}) as a catalyst to add an [[acetyl]] group to [[benzene]]:<ref>{{Cite book |last1=Brown |first1=William H. |url=https://www.worldcat.org/oclc/974377227 |title=Organic Chemistry |last2=Iverson |first2=Brent L. |last3=Anslyn |first3=Eric V. |last4=Foote |first4=Christopher S. |publisher=Cengage Learning |year=2017 |isbn=978-1-305-58035-0 |edition=8th |location=Boston, MA |pages=1002 |language=en |oclc=974377227}}</ref>
 [[File:Benzen acylowany.svg|600px|center|Friedel-Crafts acylation of benzene by ethanoyl chloride]]
-The mechanism of this reaction is [[electrophilic aromatic substitution]].
+This reaction is an example of [[electrophilic aromatic substitution]].
-[[Acyl halide]]s and [[anhydride]]s of [[carboxylic acid]]s are also commonly used acylating agents.  In some cases, [[active ester]]s exhibit comparable reactivity.  All react with [[amine]]s to form [[amide]]s and [[alcohol]]s to form [[ester]]s by [[nucleophilic acyl substitution]].
+[[Acyl halide]]s and [[acid anhydride]]s of [[carboxylic acid]]s are also common acylating agents.  In some cases, [[active ester]]s exhibit comparable reactivity. All react with [[amine]]s to form [[amide]]s and with [[Alcohol (chemistry)|alcohol]]s to form [[ester]]s by [[nucleophilic acyl substitution]].
-Acylation can be used to prevent [[rearrangement reactions]] that would normally occur in [[alkylation]]. To do this an acylation reaction is performed, then the carbonyl is removed by [[Clemmensen reduction]] or a similar process.<ref>{{cite book|last1=Vollhardt|first1=Peter|last2=Schore|first2=Neil|authorlink2=Neil E. Schore|title=Organic Chemistry: Structure and Function.|date=2014|publisher=W.H. Freeman and Company|location=New York, NY|isbn=978-1-4641-2027-5|pages=714–715|edition=7th}}</ref>
+Acylation can be used to prevent [[rearrangement reactions]] that would normally occur in [[alkylation]]. To do this an acylation reaction is performed, then the carbonyl is removed by [[Clemmensen reduction]] or a similar process.<ref>{{cite book |last1=Vollhardt |first1=Peter |title=Organic Chemistry: Structure and Function. |author2=[[Neil E. Schore]] |date=2014 |publisher=[[W.H. Freeman and Company]] |isbn=978-1-4641-2027-5 |edition=7th |location=New York, NY |pages=714–715}}</ref>
 ==Acylation in biology==
 {{see also|protein lipidation}}
-Protein acylation is the [[post-translational modification]] of proteins via the attachment of [[functional group]]s through acyl linkages. Protein acylation has been observed as a mechanism controlling biological signaling.<ref>{{Cite journal | doi = 10.1146/annurev.bi.57.070188.000441 | pmid = 3052287 | last1 = Towler | first1 = D A | last2 = Gordon | first2 = J I | last3 = Adams | first3 = S P | last4 = Glaser | first4 = L | title = The Biology and Enzymology of Eukaryotic Protein Acylation | journal = Annual Review of Biochemistry | volume = 57 | issue = 1 | pages = 69–97 | year = 1988}}</ref> One prominent type is fatty acylation, the addition of fatty acids to particular amino acids (e.g. [[myristoylation]], [[palmitoylation]] or [[palmitoleoylation]]).<ref>{{Cite journal
+Protein acylation is the [[post-translational modification]] of [[Protein|proteins]] via the attachment of [[functional group]]s through acyl linkages. Protein acylation has been observed as a mechanism controlling biological signaling.<ref>{{Cite journal |last1=Towler |first1=D A |last2=Gordon |first2=J I |last3=Adams |first3=S P |last4=Glaser |first4=L |year=1988 |title=The Biology and Enzymology of Eukaryotic Protein Acylation |journal=[[Annual Review of Biochemistry]] |volume=57 |issue=1 |pages=69–97 |doi=10.1146/annurev.bi.57.070188.000441 |pmid=3052287}}</ref> One prominent type is fatty acylation, the addition of [[Fatty acid|fatty acids]] to particular [[Amino acid|amino acids]] (e.g. [[myristoylation]], [[palmitoylation]] or [[palmitoleoylation]]).<ref>{{Cite journal |last1=Resh |first1=M. D. |year=1999 |title=Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins |journal=[[Biochimica et Biophysica Acta (BBA) - Molecular Cell Research]] |volume=1451 |issue=1 |pages=1–16 |doi=10.1016/S0167-4889(99)00075-0 |pmid=10446384 |doi-access=free}}</ref> Different types of fatty acids engage in global protein acylation.<ref>{{Cite journal |last1=Mohammadzadeh |first1=Fatemeh |last2=Hosseini |first2=Vahid |last3=Mehdizadeh |first3=Amir |last4=Dani |first4=Christian |last5=Darabi |first5=Masoud |year=2019 |title=A method for the gross analysis of global protein acylation by gas–liquid chromatography |journal=[[IUBMB Life]] |volume=71 |issue=3 |pages=340–346 |doi=10.1002/iub.1975 |issn=1521-6551 |pmid=30501005 |doi-access=free}}</ref> Palmitoleoylation is an acylation type where the [[monounsaturated]] fatty acid [[palmitoleic acid]] is [[covalently]] attached to [[serine]] or [[threonine]] [[Protein residue|residues of proteins]].<ref>{{Cite journal |last=Hannoush |first=Rami N. |date=October 2015 |title=Synthetic protein lipidation |journal=[[Current Opinion in Chemical Biology]] |volume=28 |pages=39–46 |doi=10.1016/j.cbpa.2015.05.025 |issn=1879-0402 |pmid=26080277}}</ref><ref>{{Cite book|title=Vertebrate development : maternal to zygotic control|isbn=9783319460956|location=Cham, Switzerland|oclc=966313034|last1 = Pelegri|first1 = Francisco|last2=Danilchik|first2=Michael|last3=Sutherland|first3=Ann|date=2016-12-13}}</ref> Palmitoleoylation appears to play a significant role in the trafficking, targeting, and function of [[Wnt signaling pathway|Wnt proteins]].<ref>{{Cite journal |last1=Hosseini |first1=Vahid |last2=Dani |first2=Christian |last3=Geranmayeh |first3=Mohammad Hossein |last4=Mohammadzadeh |first4=Fatemeh |last5=Nazari Soltan Ahmad |first5=Saeed |last6=Darabi |first6=Masoud |date=2018-10-20 |title=Wnt lipidation: Roles in trafficking, modulation, and function |journal=[[Journal of Cellular Physiology]] |volume=234 |issue=6 |pages=8040–8054 |doi=10.1002/jcp.27570 |issn=1097-4652 |pmid=30341908 |s2cid=53009014}}</ref><ref>{{Cite journal |last1=Nile |first1=Aaron H. |last2=Hannoush |first2=Rami N. |date=February 2016 |title=Fatty acylation of Wnt proteins |journal=[[Nature Chemical Biology]] |volume=12 |issue=2 |pages=60–69 |doi=10.1038/nchembio.2005 |issn=1552-4469 |pmid=26784846}}</ref>
-| last1 = Resh | first1 = M. D.
-| title = Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
-| journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
-| volume = 1451
-| issue = 1
-| pages = 1–16
-| year = 1999
-| pmid = 10446384
- | doi=10.1016/S0167-4889(99)00075-0
-| doi-access = free
-}}</ref> Different types of fatty acids engage in global protein acylation.<ref>{{Cite journal |last1=Mohammadzadeh|first1=Fatemeh |last2=Hosseini|first2=Vahid |last3=Mehdizadeh|first3=Amir |last4=Dani|first4=Christian |last5=Darabi|first5=Masoud|title=A method for the gross analysis of global protein acylation by gas–liquid chromatography |journal=IUBMB Life |volume=71|issue=3 |pages=340–346 |doi=10.1002/iub.1975|pmid=30501005 |issn=1521-6551|year=2019 |doi-access=free }}</ref> Palmitoleoylation is an acylation type where the monounsaturated fatty acid [[palmitoleic acid]] is covalently attached to serine or threonine residues of proteins.<ref>{{Cite journal|last=Hannoush|first=Rami N.|date=October 2015|title=Synthetic protein lipidation|journal=Current Opinion in Chemical Biology|volume=28|pages=39–46|doi=10.1016/j.cbpa.2015.05.025|issn=1879-0402|pmid=26080277}}</ref><ref>{{Cite book|title=Vertebrate development : maternal to zygotic control|isbn=9783319460956|location=Cham, Switzerland|oclc=966313034|last1 = Pelegri|first1 = Francisco|last2=Danilchik|first2=Michael|last3=Sutherland|first3=Ann|date=2016-12-13}}</ref> Palmitoleoylation appears to play a significant role in trafficking and targeting and function of [[Wnt signaling pathway|Wnt proteins]].<ref>{{Cite journal|last1=Hosseini|first1=Vahid|last2=Dani|first2=Christian|last3=Geranmayeh|first3=Mohammad Hossein|last4=Mohammadzadeh|first4=Fatemeh|last5=Nazari Soltan Ahmad|first5=Saeed|last6=Darabi|first6=Masoud|date=2018-10-20|title=Wnt lipidation: Roles in trafficking, modulation, and function|journal=Journal of Cellular Physiology|volume=234|issue=6|pages=8040–8054|doi=10.1002/jcp.27570|issn=1097-4652|pmid=30341908}}</ref><ref>{{Cite journal|last1=Nile|first1=Aaron H.|last2=Hannoush|first2=Rami N.|date=February 2016|title=Fatty acylation of Wnt proteins|journal=Nature Chemical Biology|volume=12|issue=2|pages=60–69|doi=10.1038/nchembio.2005|issn=1552-4469|pmid=26784846}}</ref>
 ==See also==
+*[[Hydroacylation]]
 *[[Acetyl]]
 *[[Ketene]]
@@ Line 31: / Line 29: @@
 ==References==
 {{Reflist}}
+{{Organic reactions}}
 [[Category:Organic reactions]]