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Ligand (S)-6-hydroxynicotine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Natural Substrate (12 entries)

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

3k7q, 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

3ng7, 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

3ngc, 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

3nh3, 3D-view

1.5.3.5

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

718677, 712752, 741943, 741686, 741691

3k7q, 3D-view

1.5.3.5

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

718677, 712752, 741943, 741686, 741691

3ng7, 3D-view

1.5.3.5

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

718677, 712752, 741943, 741686, 741691

3ngc, 3D-view

1.5.3.5

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

718677, 712752, 741943, 741686, 741691

3nh3, 3D-view

1.5.3.5

6-hydroxy-L-nicotine + H2O + O2 = 6-hydroxy-N-methylmyosmine + NH3 + H2O2

726378

3k7q, 3D-view

1.5.3.5

6-hydroxy-L-nicotine + H2O + O2 = 6-hydroxy-N-methylmyosmine + NH3 + H2O2

726378

3ng7, 3D-view

1.5.3.5

6-hydroxy-L-nicotine + H2O + O2 = 6-hydroxy-N-methylmyosmine + NH3 + H2O2

726378

3ngc, 3D-view

1.5.3.5

6-hydroxy-L-nicotine + H2O + O2 = 6-hydroxy-N-methylmyosmine + NH3 + H2O2

726378

3nh3, 3D-view

1.5.3.5

12 entries

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

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.99.4

L-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced acceptor

0

-

Substrate in Enzyme-catalyzed Reactions (16 results)

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Show Substrate (16 entries)

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, 764029, 392430, 392431, 392432, 392439

3k7q, 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, 764029, 392430, 392431, 392432, 392439

3ng7, 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, 764029, 392430, 392431, 392432, 392439

3ngc, 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, 764029, 392430, 392431, 392432, 392439

3nh3, 3D-view

1.5.3.5

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

718677, 741943, 741691, 764750, 712752, 741686

3k7q, 3D-view

1.5.3.5

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

718677, 741943, 741691, 764750, 712752, 741686

3ng7, 3D-view

1.5.3.5

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

718677, 741943, 741691, 764750, 712752, 741686

3ngc, 3D-view

1.5.3.5

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

718677, 741943, 741691, 764750, 712752, 741686

3nh3, 3D-view

1.5.3.5

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

700058

3k7q, 3D-view

1.5.3.5

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

700058

3ng7, 3D-view

1.5.3.5

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

700058

3ngc, 3D-view

1.5.3.5

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

700058

3nh3, 3D-view

1.5.3.5

6-hydroxy-L-nicotine + H2O + O2 = 6-hydroxy-N-methylmyosmine + NH3 + H2O2

726378

3k7q, 3D-view

1.5.3.5

6-hydroxy-L-nicotine + H2O + O2 = 6-hydroxy-N-methylmyosmine + NH3 + H2O2

726378

3ng7, 3D-view

1.5.3.5

6-hydroxy-L-nicotine + H2O + O2 = 6-hydroxy-N-methylmyosmine + NH3 + H2O2

726378

3ngc, 3D-view

1.5.3.5

6-hydroxy-L-nicotine + H2O + O2 = 6-hydroxy-N-methylmyosmine + NH3 + H2O2

726378

3nh3, 3D-view

1.5.3.5

16 entries

Product in Enzyme-catalyzed Reactions (7 results)

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Show Product (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.99.4

(S)-nicotine + 2,6-dichlorophenolindophenol + H2O = (S)-6-hydroxynicotine + reduced 2,6-dichlorophenolindophenol

0

-

1.5.99.4

(S)-nicotine + brilliant cresyl blue + H2O = (S)-6-hydroxynicotine + reduced brilliant cresyl blue

0

-

1.5.99.4

(S)-nicotine + menadione + H2O = (S)-6-hydroxynicotine + menadiol

0

-

1.5.99.4

(S)-nicotine + methylene blue + H2O = (S)-6-hydroxynicotine + reduced methylene blue

0

-

1.5.99.4

(S)-nicotine + pseudoazurin + H2O = (S)-6-hydroxynicotine + reduced pseudoazurin

0

-

1.5.99.4

(S)-nicotine + vitamin K5 + H2O = (S)-6-hydroxynicotine + reduced vitamin K5

0

-

1.5.99.4

L-nicotine + acceptor + H2O = (S)-6-hydroxynicotine + reduced acceptor

0

-

1.5.99.4

7 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.6

-

392439, 392461

-

1.5.3.6

at 0.12 M 50% inhibition

392440

-

1.5.3.6

competitive inhibitor

392430

-

1.5.3.6

3 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (12 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (12 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.5.3.5

3k7q, 3D-view

1.5.3.5

3ng7, 3D-view

1.5.3.5

3ngc, 3D-view

1.5.3.5

3nh3, 3D-view

1.5.3.5

3k7q, 3D-view

1.5.3.5

3ng7, 3D-view

1.5.3.5

3ngc, 3D-view

1.5.3.5

3nh3, 3D-view

1.5.3.5

3k7q, 3D-view

1.5.3.5

3ng7, 3D-view

1.5.3.5

3ngc, 3D-view

1.5.3.5

3nh3, 3D-view

1.5.3.5

12 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (10 results)

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Show Turnover Number (10 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.5.3.5

0.26

-

pH 7.0, 25°C, mutant enzyme K287M

741943

1.5.3.5

2.5

-

mutant R274A/Y311W/C417W, pH 7.4, 22°C

764029

1.5.3.5

4.8

-

pH 7.0, 25°C, mutant enzyme N166A

741943

1.5.3.5

7.3

-

pH 7.0, 40°C

741686

1.5.3.5

9

-

mutant Y311W, pH 7.4, 22°C

764029

1.5.3.5

20.9

-

pH 7.0, 25°C, mutant enzyme Y311F

741943

1.5.3.5

25.8

-

pH 8.0, 25°C

741691

1.5.3.5

29.3

-

-

392436, 392438

1.5.3.5

56

-

wild-type, pH 7.4, 22°C

764029

1.5.3.5

78

-

pH 7.0, 25°C, wild-type enzyme

741943

1.5.3.5

10 entries

K_M Value (11 results)

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Show KM Value (11 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.3.5

0.011

-

pH 7.0, 25°C, mutant enzyme K287M

741943

1.5.3.5

0.019

-

pH 7.0, 40°C

741686

1.5.3.5

0.02

-

pH and temperature not specified in the publication

712752

1.5.3.5

0.02

-

-

392436, 392440

1.5.3.5

0.06

-

wild-type, pH 7.4, 22°C

764029

1.5.3.5

0.13

-

pH 7.0, 25°C, wild-type enzyme

741943

1.5.3.5

0.2

-

pH 7.0, 25°C, mutant enzyme Y311F

741943

1.5.3.5

0.34

-

pH 7.0, 25°C, mutant enzyme N166A

741943

1.5.3.5

2.7

-

mutant R274A/Y311W/C417W, pH 7.4, 22°C

764029

1.5.3.5

3.4

-

mutant Y311W, pH 7.4, 22°C

764029

1.5.3.5

24.6

-

pH 8.0, 25°C

741691

1.5.3.5

11 entries

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.3.6

0.02

-

-

392430

1.5.3.6

1.5

-

-

392461

1.5.3.6

2 entries

References & Links

Literature References (21)

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Show Reference (21 entries)

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.

13

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

28

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

27

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.

4

95-102

392439

4965794

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

1967

Decker, K.; Dai, V.D.

Eur. J. Biochem.

3

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.

29

143-151

700058

19443550

Uptake of L-nicotine and of 6-hydroxy-L-nicotine by Arthrobacter nicotinovorans and by Escherichia coli is mediated by facilitated diffusion and not by passive diffusion or active transport

2009

Ganas, P.; Brandsch, R.

Microbiology

155

1866-1877

712752

20006620

Crystal structure analysis of free and substrate-bound 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans

2010

Kachalova, G.S.; Bourenkov, G.P.; Mengesdorf, T.; Schenk, S.; Maun, H.R.; Burghammer, M.; Riekel, C.; Decker, K.; Bartunik, H.D.

J. Mol. Biol.

396

785-799

718677

22466953

Identification of nicotine biotransformation intermediates by Agrobacterium tumefaciens strain S33 suggests a novel nicotine degradation pathway

2012

Wang, S.; Huang, H.; Xie, K.; Xu, P.

Appl. Microbiol. Biotechnol.

95

1567-1578

726378

21383134

Crystallographic snapshots of the complete reaction cycle of nicotine degradation by an amine oxidase of the monoamine oxidase (MAO) family

2011

Kachalova, G.; Decker, K.; Holt, A.; Bartunik, H.D.

Proc. Natl. Acad. Sci. USA

108

4800-4805

741686

25002425

A novel (S)-6-hydroxynicotine oxidase gene from Shinella sp. strain HZN7

2014

Qiu, J.; Wei, Y.; Ma, Y.; Wen, R.; Wen, Y.; Liu, W.

Appl. Environ. Microbiol.

80

5552-5560

741691

25344232

Molecular mechanism of nicotine degradation by a newly isolated strain, Ochrobactrum sp. strain SJY1

2015

Yu, H.; Tang, H.; Zhu, X.; Li, Y.; Xu, P.

Appl. Environ. Microbiol.

81

272-281

741943

28080034

Mechanism of flavoprotein L-6-hydroxynicotine oxidase pH and solvent isotope effects and identification of key active site residues

2017

Fitzpatrick, P.F.; Chadegani, F.; Zhang, S.; Dougherty, V.

Biochemistry

56

869-875

764029

32750321

An active site mutation in 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans changes the substrate specificity in favor of (S)-nicotine

2020

Deay, D.I.; Colvert, K.; Gao, F.; Seibold, S.; Goyal, P.; Aillon, D.; Petillo, P.; Richter, M.

Arch. Biochem. Biophys.

692

108520

764750

28337179

Characterization of a novel nicotine degradation gene cluster ndp in Sphingomonas melonis TY and its evolutionary analysis

2017

Wang, H.; Zhi, X.; Qiu, J.; Shi, L.; Lu, Z.

Front. Microbiol.

8

337

Links to other databases for (S)-6-hydroxynicotine

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Show Links (1 entry)

ChEBI

PubChem