Abstract:
:The cofactor of several flavoenzymes is autocatalytically bound to the polypeptide via a histidyl(N3)-(8alpha)-FAD linkage which makes the generation of apoenzyme difficult. We introduced an alternative covalent protein-FAD bond at the active site of 6-hydroxy-D-nicotine oxidase (6HDNO) by replacing the FAD-binding histidine with cysteine. The resulting mutant enzyme was expressed with noncovalently attached cofactor. Incubation with 8-(methylsulfonyl)FAD, and less efficiently with 8-chloro-FAD, resulted in the spontaneous replacement of the noncovalently bound FAD by the flavin derivative and the formation of an 8-(N-acetylcysteinyl)FAD linkage. The flavinylated 6HDNO.cys exhibited close to wild-type activity levels. This strategy may be generally applicable to the attachment of artificially designed flavin derivatives to the active site of covalently flavinylated enzymes.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Stoltz M,Henninger HP,Brandsch Rdoi
10.1016/0014-5793(96)00438-3subject
Has Abstractpub_date
1996-05-20 00:00:00pages
194-6issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00438-3journal_volume
386pub_type
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