3-oxoacyl-(acyl-carrier-protein) reductase

{{infobox enzyme

| Name = 3-oxoacyl-[acyl-carrier-protein] reductase

| EC_number = 1.1.1.100

| CAS_number = 37250-34-3

| GO_code = 0004316

| image = 3rsh.jpg

| width = 270

| caption = 3-oxoacyl-[acyl-carrier-protein] reductase homotetramer, Vibrio cholerae

}}

In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase ({{EC number|1.1.1.100}}) is an enzyme that catalyzes the chemical reaction

:3-oxoacyl-[acyl-carrier-protein](ACP) + NADPH + H⁺ $\rightleftharpoons$ (3R)-3-hydroxyacyl-[acyl-carrier-protein](ACP) + NADP⁺

:File:3-oxoacyl-ACP reductase reaction.svg

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group as hydride donor with NAD⁺ or NADP⁺ as hydride acceptor. The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP⁺ oxidoreductase. Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP) reductase, beta-ketoacyl reductase, beta-ketoacyl thioester reductase, beta-ketoacyl-ACP reductase, beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl acyl carrier protein reductase, 3-ketoacyl ACP reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, and 3-oxoacyl-[ACP]reductase. This enzyme participates in fatty acid biosynthesis and polyunsaturated fatty acid biosynthesis.

Structural studies

As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1I01}}, {{PDB link|1O5I}}, {{PDB link|1Q7B}}, {{PDB link|1Q7C}}, {{PDB link|1ULS}}, {{PDB link|1UZL}}, {{PDB link|1UZM}}, {{PDB link|1UZN}}, {{PDB link|2A4K}}, {{PDB link|2B4Q}}, {{PDB link|2C07}}, {{PDB link|2FR0}}, {{PDB link|2FR1}}, {{PDB link|2NM0}}, {{PDB link|2NTN}}, {{PDB link|2P68}}, {{PDB link|2PFF}}, {{PDB link|2PH3}}, {{PDB link|2PNF}}, {{PDB link|2UVD}}, and {{PDB link|2Z5L}}.

References

{{cite book |vauthors=Prescott DJ, Vagelos PR | title = Advances in Enzymology and Related Areas of Molecular Biology | chapter = Acyl Carrier Protein | year = 1972 | series = Advances in Enzymology - and Related Areas of Molecular Biology | volume = 36 | pages = 269–311 | pmid = 4561013 | doi=10.1002/9780470122815.ch8| isbn = 9780470122815 }}
{{cite journal |vauthors=Shimakata T, Stumpf PK | year = 1982 | title = Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves | journal = Arch. Biochem. Biophys. | volume = 218 | pages = 77–91 | pmid = 6756317 | issue = 1 | doi=10.1016/0003-9861(82)90323-X}}
{{cite journal |vauthors=Toomey RE, Wakil SJ | year = 1966 | title = Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli | journal = Biochim. Biophys. Acta | volume = 116 | pages = 189–97 | pmid = 4381013 | issue = 2 | doi=10.1016/0005-2760(66)90001-4}}

Category:EC 1.1.1

Category:NADPH-dependent enzymes

Category:Enzymes of known structure