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B6db references: 26750487

type Journal Article
authors Revtovich S, Anufrieva N, Morozova E, Kulikova V, Nikulin A, Demidkina T
title Structure of methionine γ-lyase from Clostridium sporogenes
journal Acta Crystallograph Sect F Struct Biol Cryst Commun.
Activity 4.4.1.11
sel selected
ui 26750487
year (2016)
volume 72
number 1
pages 65-71
 
keywords Clostridium sporogenes; active site; methionine γ-lyase; pyridoxal 5′-phosphate-binding site; tetrameric contacts
abstract Methionine γ-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the γ-elimination reaction of L-methionine. The enzyme is a promising target for therapeutic intervention in some anaerobic pathogens and has attracted interest as a potential cancer treatment. The crystal structure of MGL from Clostridium sporogenes has been determined at 2.37 Å resolution. The fold of the protein is similar to those of homologous enzymes from Citrobacter freundii, Entamoeba histolytica, Pseudomonas putida and Trichomonas vaginalis. A comparison of these structures revealed differences in the conformation of two flexible regions of the N- and C-terminal domains involved in the active-site architecture.
last changed 2017/10/02 10:04

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