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1.5.3.5: (S)-6-hydroxynicotine oxidase

This is an abbreviated version!
For detailed information about (S)-6-hydroxynicotine oxidase, go to the full flat file.

Word Map on EC 1.5.3.5

Reaction

(S)-6-hydroxynicotine
+
H2O
 +
O2
=
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one
 +
H2O2

Synonyms

6-HLNO, 6-hydroxy-L-nicotine oxidase, 6-hydroxy-L-nicotine:oxygen oxidoreductase, 6HLNO, flavoprotein nicotine oxidoreductase, L-6-hydroxynicotine oxidase, LHNO, MAO, NdpB, NicA2, NOX, VppB

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.3 With oxygen as acceptor
                1.5.3.5 (S)-6-hydroxynicotine oxidase

Engineering

Engineering on EC 1.5.3.5 - (S)-6-hydroxynicotine oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D166Q
mutation slightly reduces the KM for nicotine, it also reduced enzyme turnover by 5fold with nicotine
K287M
-
mutation results in an about 10-fold decreases in kcat/Km and k(red) for (S)-6-hydroxynicotine and a 6000-fold decrease in the kcat/Km value for oxygen
N166A
-
mutation results in an about 30fold decrease in kcat/Km and k(red) for (S)-6-hydroxynicotine, respectively, with larger effects on the kcat/Km value for (S)-6-hydroxynornicotine. The shapes of the pH profiles are not altered
R274A/Y311W/C417W
combination of mutations predicted to enhance enzyme stability, and mutation Y311W. The triple mutant displays an increased kcat value for nicotine resulting in a comparatively robust oxidation of (S)-nicotine, at the same time reducing the specificity for (S)-OH-nicotine by more than 100fold and increasing that for (S)-nicotine by more than fold
Y311F
-
mutation results in an about 30fold decrease in kcat/Km and k(red) for (S)-6-hydroxynicotine, respectively, with larger effects on the kcat/Km value for (S)-6-hydroxynornicotine. The shapes of the pH profiles are not altered
Y311W
active site residue Tyr311 forms a hydrogen bond with the hydroxyl group of (S)-6-OH-nicotine within the catalytic pocket. Replacement by a tryptophan residue reduces the kcat for (S)-6-OH-nicotine by more than 6fold
N462H
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
N462Y/W427Y
mutant enzyme shows increased catalytic activity
W427V
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
N462H
-
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
-
N462Y/W427Y
-
mutant enzyme shows increased catalytic activity
-
W427V
-
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
-
additional information