1.14.13.114: 6-hydroxynicotinate 3-monooxygenase
This is an abbreviated version!
For detailed information about 6-hydroxynicotinate 3-monooxygenase, go to the full flat file.
Reaction
Synonyms
6-hydroxynicotinic acid 3-monooxygenase, 6HNA monooxygenase, BB1770, BbNicC, NicC, PpNicC
ECTree
1.14.13.114 6-hydroxynicotinate 3-monooxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.13.114 - 6-hydroxynicotinate 3-monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H211A
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
H302A
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
H47A
site-directed mutagenesis, inactive mutant, unable to bind FAD
H47E
site-directed mutagenesis, the mutant can bind FAD, but shows very low activity compared to wild-type. The mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
H47F
site-directed mutagenesis, inactive mutant, unable to bind FAD
Y215F
site-directed mutagenesis, the mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
Y225F
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
H211A
-
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
-
H47A
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
H47F
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
Y215F
-
site-directed mutagenesis, the mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
-
H211A
-
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
-
H47A
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
H47F
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
Y215F
-
site-directed mutagenesis, the mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
-
H211A
-
site-directed mutagenesis, the mutant shows moderate uncoupling of their rates of NAD+ and 2,5-DHP product formation, suggesting that the variant has lost some efficiency in hydroxylating the substrate
-
H47A
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
H47F
-
site-directed mutagenesis, inactive mutant, unable to bind FAD
-
Y215F
-
site-directed mutagenesis, the mutant shows significant consequences in its hydroxylating activity, with NADH oxidization proceeding much more rapidly than 6-HNA is decarboxylated and hydroxylated
-
