- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/j.jmb.2006.03.048
-
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- Journal:
- Journal of molecular biology
- Volume:
- 359
- Issue:
- 2
- Pages:
- 422-432
- Publication date:
- 2006-06-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:b7e57199-be19-4e2a-bc4d-c5be602fdff4
- Source identifiers:
-
39982
- Local pid:
- pubs:39982
- Language:
- English
- Keywords:
- Copyright date:
- 2006
Journal article
Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase.
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