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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

Authors


Cummins, I More by this author
McAuley, K More by this author
Fordham-Skelton, A More by this author
Schwoerer, R More by this author
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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

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