The enzyme catalyzes the reduction of C4-C5 double bond of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. It uses FAD, FMN and an iron-sulfur cluster to perform the reaction (PMID12840019).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| FS4 700 A | FE1,FE2,FE3,FE4 | iron | iron | Fe4S4 | Electron relay |
*It refers to the MACiE reference pdb: 1ps9
| Metal/s Properties in Resting State | ||||||
| FS4 700 A | Resting state enzyme (-) | |||||
| Oxidation State | 9999 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 4 | |||||
| Notes | - | |||||
| N.B.The coordination number and the geometry refer to each single iron in the iron-sulfur cluster whereas the oxidation state is the formal oxidation state of the whole cluster. | ||||||
| References |
| -Hubbard PA, Liang X, Schulz H, Kim JJ The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase. J Biol Chem. 2003 Sep 26;278(39):37553-60. Epub 2003 Jul 2.(MEDLINE:12840019) |
| - Some information have been also deduced from the MACiE mechanism model |