The enzyme catalyzes the Mg2+-dependent transfert of the P-pant moiety from CoA to Ser36, producing holo-acyl carrier protein (PMID10997907).
![Image of apo-[acyl-carrier protein]](/thornton-srv/databases/MACiE/images/C03688.gif)
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| CA 130 A | CA | magnesium | magnesium/manganese | mononuclear | Coordinates substrate Electrostatic stabiliser Increases acidity |
*It refers to the MACiE reference pdb: 1f7l
| Metal/s Properties in Resting State | ||||||
| CA 130 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| References |
| -Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure. 2000 Aug 15;8(8):883-95.(MEDLINE:10997907) |
| - Some information have been also deduced from the MACiE mechanism model |