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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  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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