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PDBsum entry 1v2a
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Identification, Characterization and structure of a new delta class glutathione transferase isoenzyme.
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Authors
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R.Udomsinprasert,
S.Pongjaroenkit,
J.Wongsantichon,
A.J.Oakley,
L.A.Prapanthadara,
M.C.Wilce,
A.J.Ketterman.
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Ref.
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Biochem J, 2005,
388,
763-771.
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PubMed id
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Abstract
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The insect GST (glutathione transferase) supergene family encodes a varied group
of proteins belonging to at least six individual classes. Interest in insect
GSTs has focused on their role in conferring insecticide resistance. Previously
from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta
class GSTs have been characterized for structural as well as enzyme activities.
We have obtained a new Delta class GST gene and isoenzyme from A. dirus, which
we name adGSTD5-5. The adGSTD5-5 isoenzyme was identified and was only
detectably expressed in A. dirus adult females. A putative promoter analysis
suggests that this GST has an involvement in oogenesis. The enzyme displayed
little activity for classical GST substrates, although it possessed the greatest
activity for DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for
Delta GSTs. However, GST activity was inhibited or enhanced in the presence of
various fatty acids, suggesting that the enzyme may be modulated by fatty acids.
We obtained a crystal structure for adGSTD5-5 and compared it with other Delta
GSTs, which showed that adGSTD5-5 possesses an elongated and more polar
active-site topology.
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