Contribution of the two conserved tryptophan residues to the catalytic and structural properties of Proteus mirabilis glutathione S-transferase B1-1

PmGSTB1-1 (Proteus mirabilis glutathione S-transferase B1-1) has two tryptophan residues at positions 97 and 164 in each monomer. Structural data for this bacterial enzyme indicated that Trp(97) is positioned in the helix α4, whereas Trp(164) is located at the bottom of the helix α6 in the xenobioti...

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Bibliografische gegevens
Hoofdauteurs: Allocati, Nerino, Masulli, Michele, Pietracupa, Marilena, Favaloro, Bartolo, Federici, Luca, Di Ilio, Carmine
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Portland Press Ltd. 2004
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Research Article
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1134671/
https://ncbi.nlm.nih.gov/pubmed/15320869
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20040890
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