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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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| Autors principals: | , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Portland Press Ltd.
2004
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| Matèries: | |
| Accés en línia: | 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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