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

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3-oxoacyl-[acyl-carrier-protein] reductase
Identifiers
EC number 1.1.1.100
CAS number 37250-34-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

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

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ \rightleftharpoons 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 1I01, 1O5I, 1Q7B, 1Q7C, 1ULS, 1UZL, 1UZM, 1UZN, 2A4K, 2B4Q, 2C07, 2FR0, 2FR1, 2NM0, 2NTN, 2P68, 2PFF, 2PH3, 2PNF, 2UVD, and 2Z5L.

References

    • Prescott DJ, Vagelos PR (1972). "Acyl carrier protein". Adv. Enzymol. Relat. Areas. Mol. Biol. 36: 269–311. PMID 4561013. 
    • Shimakata T, Stumpf PK (1982). "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". Arch. Biochem. Biophys. 218 (1): 77–91. doi:10.1016/0003-9861(82)90323-X. PMID 6756317. 
    • Toomey RE, Wakil SJ (1966). "Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli". Biochim. Biophys. Acta 116 (2): 189–97. doi:10.1016/0005-2760(66)90001-4. PMID 4381013. 
    1.1.1: NAD/NADP acceptor
    1.1.2: cytochrome acceptor
    1.1.3: oxygen acceptor
    1.1.4: disulfide as acceptor
    1.1.5: quinone/similar acceptor
    1.1.99: other acceptors
    • B
    • enzm
    • 1.1
      • 2
      • 3
      • 4
      • 5
      • 6
      • 7
      • 8
      • 10
      • 11
      • 13
      • 14
      • 15-18
    • 2.1
      • 2
      • 3
      • 4
      • 5
      • 6
      • 7
        • 2.7.10
        • 11-12
      • 8
    • 3.1
        • 3.1.3.48
      • 2
      • 3
      • 4
        • 3.4.21
        • 22
        • 23
        • 24
      • 5
      • 6
      • 7
    • 4.1
      • 2
      • 3
      • 4
      • 5
      • 6
    • 5.1
      • 2
      • 3
      • 4
      • 99
    • 6.1-3
      • 4
      • 5-6
    Synthesis
    Malonyl-CoA synthesis
    Fatty acid desaturases
    Triacyl glycerol
    Degradation
    Acyl transport
    General
    Unsaturated
    Odd chain
    Other

    M: MET

    mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

    k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

    m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)


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