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Literature summary for 1.5.3.5 extracted from

  • Kachalova, G.S.; Bourenkov, G.P.; Mengesdorf, T.; Schenk, S.; Maun, H.R.; Burghammer, M.; Riekel, C.; Decker, K.; Bartunik, H.D.
    Crystal structure analysis of free and substrate-bound 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans (2010), J. Mol. Biol., 396, 785-799.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Paenarthrobacter nicotinovorans

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Paenarthrobacter nicotinovorans
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 Paenarthrobacter nicotinovorans

Inhibitors

Inhibitors Comment Organism Structure
(R)-6-hydroxynicotine
-
Paenarthrobacter nicotinovorans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
(S)-6-hydroxynicotine pH and temperature not specified in the publication Paenarthrobacter nicotinovorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-6-hydroxynicotine + H2O + O2 Paenarthrobacter nicotinovorans absolute stereospecificity on the L-form 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Paenarthrobacter nicotinovorans Q93NH4
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein a diacylglycerophospholipid molecule is non-covalently bound to each enzyme protomer. 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 Paenarthrobacter nicotinovorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-6-hydroxynicotine + H2O + O2 absolute stereospecificity on the L-form Paenarthrobacter nicotinovorans 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
?
(S)-6-hydroxynicotine + H2O + O2 absolute stereospecificity on the L-form Paenarthrobacter nicotinovorans 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 intermediate product 6-hydroxy-N-methylmyosmine, which hydrolyzes to 6-hydroxy-pseudooxynicotine ?

Subunits

Subunits Comment Organism
dimer the active enzyme exists as a stable dimer in solution Paenarthrobacter nicotinovorans

Synonyms

Synonyms Comment Organism
6-hydroxy-L-nicotine oxidase
-
Paenarthrobacter nicotinovorans
6HLNO
-
Paenarthrobacter nicotinovorans

Cofactor

Cofactor Comment Organism Structure
FAD binding domain structure, overview. The flavin may have a role in oxygen activation involving replacement of the water molecule by oxygen and superoxide formation Paenarthrobacter nicotinovorans

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.1
-
(R)-6-hydroxynicotine pH and temperature not specified in the publication Paenarthrobacter nicotinovorans

General Information

General Information Comment Organism
additional information the flavin may have a role in oxygen activation involving replacement of the water molecule by oxygen and superoxide formation. The orientation of the bound substrate relative to the isoalloxazine ring of the FAD cofactor is suitable for hydride transfer dehydrogenation at the carbon atom that forms the chiral center of the substrate molecule, substrate-binding mode, overview. In the dithionite-reduced 6HLNO, the natural substrate 6-hydroxy-L-nicotine is located in a tight cavity suggesting that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions Paenarthrobacter nicotinovorans