|
type |
Journal Article |
authors |
Mamaeva, D.V.; Morozovam, E.A.; Nikulinm, A.D.; Revtovichm, S.V.; Nikonovm, S.V.; Garberm, M.B.; Demidkina, T.V. |
title |
Structure of Citrobacter freundiiL-methionine gamma-lyase |
journal |
Acta Crystallograph Sect F Struct Biol Cryst Commun. |
Activity |
4.4.1.11 |
sel |
selected |
ui |
16511092 |
year |
(2005) |
volume |
61 |
number |
6 |
pages |
546-9 |
| |
abstract |
L-Methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes gamma-elimination of L-methionine. The crystal structure of MGL from Citrobacter freundii has been determined at 1.9 A resolution. The spatial fold of the protein is similar to those of MGLs from Pseudomonas putida and Trichomonas vaginalis. The comparison of these structures revealed that there are differences in PLP-binding residues and positioning of the surrounding flexible loops. |
last changed |
2008/06/09 17:52 |
|