Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase.
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, SFGH...
Main Authors: | Cummins, I, McAuley, K, Fordham-Skelton, A, Schwoerer, R, Steel, P, Davis, B, Edwards, R |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2006
|
Similar Items
-
Crystal Structure and Functional Characterization of an S-Formylglutathione Hydrolase (<i>Bu</i>SFGH) from <i>Burkholderiaceae</i> sp.
by: Jisub Hwang, et al.
Published: (2023-04-01) -
A front-face 'SNi synthase' engineered from a retaining 'double-SN2' hydrolase.
by: Iglesias-Fernández, J, et al.
Published: (2017) -
Serine esterases are required for pollen tube penetration of the stigma in Brassica
by: Hiscock, S, et al.
Published: (2002) -
Serine ADP-ribosylation reversal by the hydrolase ARH3
by: Fontana, P, et al.
Published: (2017) -
Serine ADP-ribosylation reversal by the hydrolase ARH3
by: Pietro Fontana, et al.
Published: (2017-06-01)