Journal article
Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase.
- Abstract:
-
S-Formylglutathione hydrolases (SFGHs) are highly conserved thioesterases present in prokaryotes and eukaryotes, and form part of the formaldehyde detoxification pathway, as well as functioning as xenobiotic-hydrolysing carboxyesterases. As defined by their sensitivity to covalent modification, SFGHs behave as cysteine hydrolases, being inactivated by thiol alkylating agents, while being insensitive to inhibition by organophosphates such as paraoxon. As such, the enzyme has been classified as...
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- Publication status:
- Published
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- Publisher copy:
- 10.1016/j.jmb.2006.03.048
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Authors
Bibliographic Details
- Journal:
- Journal of molecular biology
- Volume:
- 359
- Issue:
- 2
- Pages:
- 422-432
- Publication date:
- 2006-06-01
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- Source identifiers:
-
39982
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:39982
- UUID:
-
uuid:b7e57199-be19-4e2a-bc4d-c5be602fdff4
- Local pid:
- pubs:39982
- Deposit date:
- 2012-12-19
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- Copyright date:
- 2006
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