View source for (R)-2-hydroxy-fatty-acid dehydrogenase

{{enzyme
| Name = 3-oxoacyl-[acyl-carrier-protein] reductase
| EC_number = 1.1.1.100
| CAS_number = 37250-34-3
| IUBMB_EC_number = 1/1/1/100
| GO_code = 0004316
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''3-oxoacyl-[acyl-carrier-protein] reductase''' ({{EC number|1.1.1.100}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP<sup>+</sup> <math>\rightleftharpoons</math> 3-oxoacyl-[acyl-carrier-protein] + NADPH + H<sup>+</sup>

[[Image:FattyAcid-MB-Reduction1.png]]

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[acyl carrier protein|(3R)-3-hydroxyacyl-[acyl-carrier-protein]]] and [[nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[acyl carrier protein|3-oxoacyl-[acyl-carrier-protein]]], [[nicotinamide adenine dinucleotide phosphate|NADPH]], and [[hydrogen ion|H<sup>+</sup>]].

This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor. The systematic name of this enzyme class is '''(3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP<sup>+</sup> 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 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|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==
{{reflist|1}}
* {{cite journal | author = Prescott DJ, Vagelos PR | year = 1972 | title = Acyl carrier protein | journal = Adv. Enzymol. Relat. Areas. Mol. Biol. | volume = 36 | pages = 269&ndash;311 | pmid = 4561013 }}
* {{cite journal | author = 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&ndash;91 | pmid = 6756317 | issue = 1 | doi=10.1016/0003-9861(82)90323-X}}
* {{cite journal | author = 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&ndash;97 | pmid = 4381013 | issue = 2 | doi=10.1016/0005-2760(66)90001-4}}

{{Alcohol oxidoreductases}}
{{Lipid metabolism enzymes}}

[[Category:EC 1.1.1]]
[[Category:NADPH-dependent enzymes]]
[[Category:Enzymes of known structure]]


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