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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Detaylı Bibliyografya
Asıl Yazarlar: Allocati, Nerino, Masulli, Michele, Pietracupa, Marilena, Favaloro, Bartolo, Federici, Luca, Di Ilio, Carmine
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Portland Press Ltd. 2004
Konular:
Research Article
Online Erişim: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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