“3-oxoacyl-(acyl-carrier-protein) reductase”的意思、由来-开放百科全书

词条

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

释义

Structural studies
References

{{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 catalyzes the chemical reaction

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP⁺ 3-oxoacyl-[acyl-carrier-protein] + NADPH + H⁺

Thus, the two substrates of this enzyme are (3R)-3-hydroxyacyl-[acyl-carrier-protein] and NADP⁺, whereas its 3 products are 3-oxoacyl-[acyl-carrier-protein], NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as 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 journal |vauthors=Prescott DJ, Vagelos PR | year = 1972 | title = Acyl carrier protein | journal = Adv. Enzymol. Relat. Areas Mol. Biol. | volume = 36 | pages = 269–311 | pmid = 4561013 | doi=10.1002/9780470122815.ch8}}
{{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}}

{{Alcohol oxidoreductases}}{{Lipid metabolism enzymes}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{1.1.1-enzyme-stub}}

3 : EC 1.1.1|NADPH-dependent enzymes|Enzymes of known structure

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