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Enzyme Kinetic Parameters
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Ligand 6-hydroxypseudooxynicotine

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Basic Ligand Information

Molecular Structure

Picture of 6-hydroxypseudooxynicotine (click for magnification)

Molecular Formula

BRENDA Name

InChIKey

C₁₀H₁₄N₂O₂

6-hydroxypseudooxynicotine

UMLOUOBDBGOHHR-UHFFFAOYSA-N

Synonyms:

1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one, 1-(6-hydroxypyrid-3-yl)-4-(methylamino)butan-1-one, 1-(6-hydroxypyridin-3-yl)-4-(methylamino)-butan-1-one, 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one, 6-hydroxy-pseudooxynicotine

Pathway Source

Pathways

KEGG

Microbial metabolism in diverse environments, Nicotinate and nicotinamide metabolism

MetaCyc

nicotine degradation I (pyridine pathway), nicotine degradation III (VPP pathway)

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.99.14

6-hydroxypseudooxynicotine + EtfAB + H2O = 6-hydroxy-3-succinoylsemialdehyde-pyridine + methylamine + reduced EtfAB

763956

In Vivo Product in Enzyme-catalyzed Reactions (7 results)

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EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.5

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

392433, 392434, 392435, 392436, 392437, 392438, 392440, 392430, 392431, 392432, 392439

3nh3, 3D-view

1.5.3.5

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

392433, 392434, 392435, 392436, 392437, 392438, 392440, 392430, 392431, 392432, 392439

3nho, 3D-view

1.5.3.5

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

392433, 392434, 392435, 392436, 392437, 392438, 392440, 392430, 392431, 392432, 392439

3nk0, 3D-view

1.5.3.5

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

3nh3, 3D-view

1.5.3.5

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

3nho, 3D-view

1.5.3.5

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

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

0, 392430, 392433

Substrate in Enzyme-catalyzed Reactions (4 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.99.14

1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor

392537

1.5.99.14

1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + phenazine methosulfate + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced phenazine methosulfate

765432

1.5.99.14

6-hydroxypseudooxynicotine + 2,6-dichlorophenolindophenol + H2O = 6-hydroxy-3-succinoylsemialdehyde-pyridine + methylamine + reduced 2,6-dichlorophenolindophenol

741698, 763956

1.5.99.14

6-hydroxypseudooxynicotine + EtfAB + H2O = 6-hydroxy-3-succinoylsemialdehyde-pyridine + methylamine + reduced EtfAB

763956

1.5.99.14

4 entries

Product in Enzyme-catalyzed Reactions (11 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.5

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

392433, 392434, 392435, 392436, 392437, 392438, 392440, 0, 392430, 392431, 392432, 392439

3nh3, 3D-view

1.5.3.5

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

392433, 392434, 392435, 392436, 392437, 392438, 392440, 0, 392430, 392431, 392432, 392439

3nho, 3D-view

1.5.3.5

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

392433, 392434, 392435, 392436, 392437, 392438, 392440, 0, 392430, 392431, 392432, 392439

3nk0, 3D-view

1.5.3.5

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

3nh3, 3D-view

1.5.3.5

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

3nho, 3D-view

1.5.3.5

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

3nk0, 3D-view

1.5.3.5

(S)-6-hydroxynicotine + H2O + O2 = 6-hydroxy-pseudooxynicotine + H2O2

3nh3, 3D-view

1.5.3.5

(S)-6-hydroxynicotine + H2O + O2 = 6-hydroxy-pseudooxynicotine + H2O2

3nho, 3D-view

1.5.3.5

(S)-6-hydroxynicotine + H2O + O2 = 6-hydroxy-pseudooxynicotine + H2O2

3nk0, 3D-view

1.5.3.6

(R)-6-hydroxynicotine + H2O + electron acceptor = 1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + electron donor

392461

1.5.3.6

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

0, 392430, 392433, 392436

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.6

392461

3D Structure of Enzyme-Ligand-Complex (PDB) (18 results)

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EC NUMBER

ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (10 results)

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EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.5.99.14

2.3

mutant F269A, pH 8.0, 30°C

765432

1.5.99.14

5.13

wild-type, PBS, pH 6.4, 30°C

765432

1.5.99.14

6.3

mutant R383A, pH 8.0, 30°C

765432

1.5.99.14

8.92

wild-type, Tris/HCl, pH 8.5, 30°C

765432

1.5.99.14

9.03

wild-type, PBS, pH 8.0, 30°C

765432

1.5.99.14

9.03

wild-type, pH 8.0, 30°C

765432

1.5.99.14

9.09

wild-type, Tris/HCl, pH 6.8, 30°C

765432

1.5.99.14

9.28

wild-type, Tris/HCl, pH 7.4, 30°C

765432

1.5.99.14

9.47

wild-type, Tris/HCl, pH 8.0, 30°C

765432

1.5.99.14

10.58

wild-type, PBS, pH 7.4, 30°C

765432

1.5.99.14

10 entries

K_M Value (10 results)

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EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.99.14

0.0125

wild-type, PBS, pH 8.0, 30°C

765432

1.5.99.14

0.0125

wild-type, pH 8.0, 30°C

765432

1.5.99.14

0.0151

wild-type, Tris/HCl, pH 8.5, 30°C

765432

1.5.99.14

0.0159

wild-type, Tris/HCl, pH 8.0, 30°C

765432

1.5.99.14

0.0214

mutant R383A, pH 8.0, 30°C

765432

1.5.99.14

0.0223

wild-type, Tris/HCl, pH 7.4, 30°C

765432

1.5.99.14

0.0234

wild-type, PBS, pH 7.4, 30°C

765432

1.5.99.14

0.026

mutant F269A, pH 8.0, 30°C

765432

1.5.99.14

0.0377

wild-type, Tris/HCl, pH 6.8, 30°C

765432

1.5.99.14

0.065

wild-type, PBS, pH 6.4, 30°C

765432

1.5.99.14

10 entries

K_i Value (1 result)

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EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.3.6

0.05

392461

References & Links

Literature References (16)

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BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

392430

9878353

Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans

1998

Schenk, S.; Hoelz, A.; Krauss, B.; Decker, K.

J. Mol. Biol.

284

1323-1339

392431

7815950

Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans

1994

Grether-Beck, S.; Igloi, G.L.; Pust, S.; Schilz, E.; Decker, K.; Brandsch, R.

Mol. Microbiol.

929-936

392432

2540800

13C, 15N, and 31P NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans

1989

Pust, S.; Vervoort, J.; Decker, K.; Bacher, A.; Muller, F.

Biochemistry

516-521

392433

3622516

6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase

1987

Brandsch, R.; Hinkkanen, A.E.; Mauch, L.; Nagursky, H.; Decker, K.

Eur. J. Biochem.

167

315-320

392434

4019415

Localization of the enantiozymes of 6-hydroxy-nicotine oxidase in Arthrobacter oxidans by electron immunochemistry

1985

Swafford, J.R.; Reeves, H.C.; Brandsch, R.

J. Bacteriol.

163

792-795

392435

6618442

Purification of the flavoproteins 6-hydroxy-D- and 6-hydroxy-L-nicotine oxidase using hydrophobic affinity chromatography

1983

Hinkkanen, A.; Lilius, E.M.; Nowack, J.; Maas, R.; Decker, K.

Hoppe-Seyler's Z. Physiol. Chem.

364

801-806

392436

4405081

D- and L-6-hydroxynicotine oxidase, enantioenzymes of Arthrobacter oxidans

1972

Decker, K.; Dai, V.D.; Möhler, H.; Bruhmuller, M.

Z. Naturforsch. B

1072-1073

392437

Mechanisms of flavoprotein catalysis

1968

Palmer, G.; Massey, V.

Biol. Oxidations (Singer, T. P. , ed. )

263-300

392438

5646150

Purification and properties of L-6-hydroxynicotine oxidase

1968

Dai, V.D.; Decker, K.; Sund, H.

Eur. J. Biochem.

95-102

392439

4965794

Mechanism and specifcity of L- and D-6-hydroxynicotine oxidase

1967

Decker, K.; Dai, V.D.

Eur. J. Biochem.

132-138

392440

5849820

Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans

1965

Decker, K.; Bleeg, H.

Biochim. Biophys. Acta

105

313-324

392461

4628374

Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase

1972

Bruhmuller, M.; Möhler, H.; Decker, K.

Eur. J. Biochem.

143-151

392537

Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase

1988

Freudenberg, W.; Koenig, K.; Andreesen, J.R.

FEMS Microbiol. Lett.

13-18

741698

26729714

Nicotine dehydrogenase complexed with 6-hydroxypseudooxynicotine oxidase involved in the hybrid nicotine-degrading pathway in Agrobacterium tumefaciens S33

2016

Li, H.; Xie, K.; Yu, W.; Hu, L.; Huang, H.; Xie, H.; Wang, S.

Appl. Environ. Microbiol.

1745-1755

763956

30926728

6-Hydroxypseudooxynicotine dehydrogenase delivers electrons to electron transfer flavoprotein during nicotine degradation by Agrobacterium tumefaciens S33

2019

Wang, R.; Yi, J.; Shang, J.; Yu, W.; Li, Z.; Huang, H.; Xie, H.; Wang, S.

Appl. Environ. Microbiol.

e00454

765432

34299660

Structural, mechanistic, and functional insights into an Arthrobacter nicotinovorans molybdenum hydroxylase involved in nicotine degradation

2021

Wang, L.; Mu, X.; Li, W.; Xu, Q.; Xu, P.; Zhang, L.; Zhang, Y.; Wu, G.

Molecules

4387