Просмотр кода страницы Английская Википедия:(acyl-carrier-protein) S-acetyltransferase

{{Английская Википедия/Панель перехода}}
{{Short description|Class of enzymes}}
{{infobox enzyme
| Name       = [acyl-carrier-protein] S-acetyltransferase
| EC_number  = 2.3.1.38
| CAS_number = 37257-16-2
| GO_code    = 0004313
| image      =
| width      = 
| caption    =  
}}
In [[enzymology]], a '''[acyl-carrier-protein] S-acetyltransferase''' ({{EC number|2.3.1.38}}) is an [[enzyme]] that [[catalysis|catalyzes]] the reversible [[chemical reaction]]

:acetyl-CoA + [acyl-carrier-protein] <math>\rightleftharpoons</math> CoA + acetyl-[acyl-carrier-protein]

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[acetyl-CoA]] and [[acyl carrier protein]], whereas its two [[product (chemistry)|products]] are [[coenzyme A|CoA]] and acetyl-acyl-carrier-protein.

This enzyme belongs to the family of [[transferase]]s, specifically those [[acyltransferase]]s transferring groups other than aminoacyl groups.  The [[List of enzymes|systematic name]] of this enzyme class is '''acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase'''. Other names in common use include '''acetyl coenzyme A-acyl-carrier-protein transacylase''', '''Acetyl CoA:ACP transacylase''', '''[acyl-carrier-protein]acetyltransferase''', '''[ACP]acetyltransferase''', and '''ACAT'''.  This enzyme participates in [[fatty acid biosynthesis]].

==Structural studies==

As of late 2007, only one [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|2PFF}}.

==References==
{{reflist|30em}}
* {{cite book |vauthors=Prescott DJ, Vagelos PR | title = Advances in Enzymology and Related Areas of Molecular Biology | date = 1972 | chapter = Acyl carrier protein | volume = 36 | pages = 269&ndash;311  | pmid = 4561013 | doi=10.1002/9780470122815.ch8| series = Advances in Enzymology - and Related Areas of Molecular Biology | isbn = 9780470122815 }}
* {{cite journal |vauthors=Vance DE, Mitsuhashi O, Bloch K | date = 1973 | title = Purification and properties of the fatty acid synthetase from Mycobacterium phlei | journal = J. Biol. Chem.  | volume = 248 | pages = 2303&ndash;9  | pmid = 4698221 | issue = 7 }}
* {{cite journal |vauthors=Williamson IP, Wakil SJ | date = 1966 | title = Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases | journal = J. Biol. Chem.  | volume = 241 | pages = 2326&ndash;32  | pmid = 5330116 | issue = 10 }}
* {{cite journal |vauthors=Lowe PN, Rhodes S | date = 1988 | title = Purification and characterization of acyl-carrier-protein acetyltransferase from Escherichia coli | journal = Biochem. J.  | volume = 250 | pages = 789&ndash;96  | pmid = 3291856 | issue = 3 | doi = 10.1042/bj2500789 | pmc = 1148925 }}
* {{cite journal |vauthors=Tsay JT, Oh W, Larson TJ, Jackowski S, Rock CO | date = 1992 | title = Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12 | journal = J. Biol. Chem.  | volume = 267 | pages = 6807&ndash;14  | pmid = 1551888 | issue = 10 }}
* {{cite journal |vauthors=Rangan VS, Smith S | date = 1997 | title = Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue | journal = J. Biol. Chem.  | volume = 272 | pages = 11975&ndash;8  | pmid = 9115261 | doi = 10.1074/jbc.272.18.11975 | issue = 18 | doi-access = free }}

{{Acyltransferases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}

[[Category:EC 2.3.1]]
[[Category:Enzymes of known structure]]


{{2.3-enzyme-stub}}
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[[Категория:Английская Википедия]]
[[Категория:Википедия]]
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