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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

Crystallization

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

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
forms hexagonal crystals in ammonium sulfate solution
-
His-tagged and untagged free enzyme and complex of dithionite-reduced 6HLNO with the natural substrate 6-hydroxy-L-nicotine X-ray diffraction structure determination and analysis at 1.95 A and 2.05 A resolution, respectively, combined isomorphous/multiple-wavelength anomalous dispersion phasing
to 1.95 A resolution. A diacylglycerophospholipid molecule is non-covalently bound to each protomer of 6HLNO. The fatty acid chains occupy hydrophobic channels that penetrate deep into the interior of the substrate-binding domain of each subunit. The solvent-exposed glycerophosphate moiety is located at the subunit-subunit interface. In the crystal structure of a complex of dithionite-reduced 6HLNO with the natural substrate 6-hydroxy-L-nicotine at 2.05 A resolution, the location of the substrate in a tight cavity suggests that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions. A comparison of the substrate-binding modes of 6HLNO and 6-hydroxy-D-nicotine oxidase, EC 1.5.3.6, based on models of complexes with the D-substrate, suggests that the two enzymes orient the enantiomeric substrates in mirror symmetry with respect to the plane of the flavin
hanging-drop vapor diffusion method, X-ray crystal structures of the N462V and N462Y/W427Y variants complexed with (S)-nicotine (at 2.7 and 2.3 A resolution, respectively) reveal no significant active-site rearrangements