Site-directed mutagenesis of histidine 106 and lysine 107 residues in the Proteus mirabilis glutathione transferase B1-1

Nerino Allocati, Michele Masulli, Enrico Casalone, Galina Polekhina, Jamie Rossjohn, Michael W. Parker, Carmine Di Ilio

Research output: Contribution to journalArticleResearchpeer-review

Abstract

The crystal structure of PmGST B1-1 suggested that one or more residues in the C-terminal domain of the enzyme might stabilise the activated form of glutathione for conjugation reaction. In order to test this hypothesis we have emulated His 106 and Lys 107 of PmGST B1-1 to investigate their possible role in the enzyme's catalytic activity. The data are consistent with His 106 and Lys 107 being involved in interacting with glutathione in the site active but these residues do not contribute significantly to catalysis.

Original languageEnglish
Pages (from-to)182-184
Number of pages3
JournalChemico-Biological Interactions
Volume133
Issue number1-3
Publication statusPublished - 28 Feb 2001
Externally publishedYes

Keywords

  • Glutathione transferase
  • Proteus mirabilis
  • Site-directed mutagenesis

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