Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site
10.1042/BSR20150183
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2020
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sg-nus-scholar.10635-1796322024-03-26T08:55:33Z Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site Wongsantichon, J Robinson, R.C Ketterman, A.J CHEMICAL & BIOMOLECULAR ENGINEERING glutathione glutathione transferase glutathione transferase E6 histidine serine unclassified drug Drosophila protein glutathione glutathione transferase GSTE6 protein, Drosophila amino acid sequence Article binding affinity controlled study crystal structure Drosophila melanogaster enzyme specificity molecular interaction nonhuman protein folding protein quaternary structure protein subunit residue analysis sequence alignment sequence analysis structure activity relation structure analysis animal binding site chemistry enzyme active site enzymology genetics metabolism protein conformation protein motif X ray crystallography Amino Acid Motifs Amino Acid Sequence Animals Binding Sites Catalytic Domain Crystallography, X-Ray Drosophila melanogaster Drosophila Proteins Glutathione Glutathione Transferase Protein Conformation 10.1042/BSR20150183 Bioscience Reports 35 6 e00272 2020-10-23T08:07:00Z 2020-10-23T08:07:00Z 2015 Article Wongsantichon, J, Robinson, R.C, Ketterman, A.J (2015). Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site. Bioscience Reports 35 (6) : e00272. ScholarBank@NUS Repository. https://doi.org/10.1042/BSR20150183 0144-8463 https://scholarbank.nus.edu.sg/handle/10635/179632 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Portland Press Ltd Unpaywall 20201031 |
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Singapore Singapore |
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glutathione glutathione transferase glutathione transferase E6 histidine serine unclassified drug Drosophila protein glutathione glutathione transferase GSTE6 protein, Drosophila amino acid sequence Article binding affinity controlled study crystal structure Drosophila melanogaster enzyme specificity molecular interaction nonhuman protein folding protein quaternary structure protein subunit residue analysis sequence alignment sequence analysis structure activity relation structure analysis animal binding site chemistry enzyme active site enzymology genetics metabolism protein conformation protein motif X ray crystallography Amino Acid Motifs Amino Acid Sequence Animals Binding Sites Catalytic Domain Crystallography, X-Ray Drosophila melanogaster Drosophila Proteins Glutathione Glutathione Transferase Protein Conformation |
| spellingShingle |
glutathione glutathione transferase glutathione transferase E6 histidine serine unclassified drug Drosophila protein glutathione glutathione transferase GSTE6 protein, Drosophila amino acid sequence Article binding affinity controlled study crystal structure Drosophila melanogaster enzyme specificity molecular interaction nonhuman protein folding protein quaternary structure protein subunit residue analysis sequence alignment sequence analysis structure activity relation structure analysis animal binding site chemistry enzyme active site enzymology genetics metabolism protein conformation protein motif X ray crystallography Amino Acid Motifs Amino Acid Sequence Animals Binding Sites Catalytic Domain Crystallography, X-Ray Drosophila melanogaster Drosophila Proteins Glutathione Glutathione Transferase Protein Conformation Wongsantichon, J Robinson, R.C Ketterman, A.J Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site |
| description |
10.1042/BSR20150183 |
| author2 |
CHEMICAL & BIOMOLECULAR ENGINEERING |
| author_facet |
CHEMICAL & BIOMOLECULAR ENGINEERING Wongsantichon, J Robinson, R.C Ketterman, A.J |
| format |
Article |
| author |
Wongsantichon, J Robinson, R.C Ketterman, A.J |
| author_sort |
Wongsantichon, J |
| title |
Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site |
| title_short |
Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site |
| title_full |
Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site |
| title_fullStr |
Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site |
| title_full_unstemmed |
Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site |
| title_sort |
epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site |
| publisher |
Portland Press Ltd |
| publishDate |
2020 |
| url |
https://scholarbank.nus.edu.sg/handle/10635/179632 |
| _version_ |
1795301252889837568 |