This image is a scaled-down version of the actual pathway image. It does not contain any links to the protein information pages.
|
|
Description |
Legionella pneumophila is a motile, rod-shaped, Gram-negative, aerobic,
bacterium, considered to be a facultative parasite. L. pneumophila is
the causative agent of the Legionnaires disease, a potential fatal pneumonia.
L. pneumophila Lens is an epidemic strain and was responsible for a
major outbreak of disease in France. Glutathione metabolism in L.
pneumophila occurs within cells in two closely linked, enzymatically
controlled reactions that utilize ATP and draw on nonessential amino acids as
substrates. Glutathione is a tripeptide, composed of glutamate, cysteine and
glycine, and has numerous important functions within the bacterial cell. This
tripeptide is specifically a thiol compound, present in the highest
concentration in all types of cells (Ref.1 & 9).
During Glutathione
metabolism, the L-Amino acid (Laevorotatory Amino acids) [...] |
|
|
References:
1. Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity.Cazalet C, Rusniok C, Bruggemann H, Zidane N, Magnier A, Ma L, Tichit M, Jarraud S, Bouchier C, Vandenesch F, Kunst F, Etienne J, Glaser P, Buchrieser C.:Nat Genet. 2004 Nov; 36(11):1165-73. Epub 2004 Oct 3.2. Cloning and expression of a single-chain catalytic antibody that acts as a glutathione peroxidase mimic with high catalytic efficiency.Ren X, Gao S, You D, Huang H, Liu Z, Mu Y, Liu J, Zhang Y, Yan G, Luo G, Yang T, Shen J.Biochem J. 2001 Oct 15; 359(Pt 2):369-74
|
|
|
|
|