Abstract:
:Replacing the essential Cys-149 by a selenocysteine into the active site of phosphorylating glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus leads to a selenoGAPDH that mimics a selenoperoxidase activity. Saturation kinetics were observed with cumenyl and tert-butyl hydroperoxides, with a better catalytic efficiency for the aromatic compound. The enzymatic mechanism fits a sequential model where the formation of a ternary complex between the holoselenoenzyme, the 3-carboxy 4-nitrobenzenethiol used as the reductant and the hydroperoxide precedes product release. The fact that the selenoGAPDH is NAD-saturated supports a binding of hydroperoxide and reductant in the substrate binding site. The catalytic efficiency is similar to selenosubtilisins but remains low compared to selenoglutathione peroxidase. This is discussed in relation to what is known from the X-ray crystal structures of selenoglutathione peroxidase and GAPDHs.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Boschi-Muller S,Muller S,Van Dorsselaer A,Böck A,Branlant Gdoi
10.1016/s0014-5793(98)01377-5subject
Has Abstractpub_date
1998-11-20 00:00:00pages
241-5issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01377-5journal_volume
439pub_type
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