print visible entries

print all entries

Ligand pyridine N-oxide

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Substrate (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.7.2.3

pyridine N-oxide + electron donor = pyridine + oxidized electron donor + H2O

392773, 392776

-

1.8.5.3

dimethylsulfide + H2O + pyridine N-oxide = dimethylsulfoxide + pyridine

711886

-

1.8.5.3

pyridine N-oxide + reduced benzyl viologen + H2O = pyridine + oxidized benzyl viologen

712959

-

1.8.5.3

2 entries

Product in Enzyme-catalyzed Reactions (2 results)

top print hide

Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.2.1

pyridine + H2O2 = pyridine N-oxide + H2O

0

-

1.14.13.25

pyridine + NAD(P)H + O2 = pyridine N-oxide + NAD(P)+ + H2O

438920

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

top print hide

Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.17.7.4

-

715301

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

4.1.99.2

2yct, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (20 results)

top print hide

Show Turnover Number (20 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.7.2.3

42.2

-

tungsten-restored enzyme

392776

1.7.2.3

44.7

-

molybdenum-restored enzyme

392776

1.7.2.3

53.5

-

-

392773

1.8.5.3

3

6

mutant Q179I, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

10

-

mutant A178Q, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

33

-

mutant W357Y, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

41

-

mutant W357F, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

95

-

mutant R149C, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

96

-

mutant T148S, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

99

-

mutant G167N, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

99

-

mutant W191G, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

100

-

mutant W357C, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

110

-

mutant M147L, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

120

-

mutant R217Q, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

190

-

mutant G190D, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

190

-

mutant M147I, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

200

-

wild-type, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

243

-

pH 7.0, 30°C

712959

1.8.5.3

260

-

mutant G190V, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

940

-

mutant A181T, pH not specified in the publication, temperature not specified in the publication

711886

1.7.2.3

3 entries

1.8.5.3

17 entries

K_M Value (20 results)

top print hide

Show KM Value (20 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.7.2.3

0.0108

-

tungsten-restored enzyme

392776

1.7.2.3

1.86

-

-

392773

1.7.2.3

2.25

-

molybdenum-restored enzyme

392776

1.8.5.3

0.001

-

mutant A178Q, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.024

-

mutant T148S, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.028

-

mutant W357Y, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.034

-

mutant Q179I, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.048

-

mutant W191G, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.048

-

mutant W357F, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.076

-

mutant G167N, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.094

-

pH 7.0, 30°C

712959

1.8.5.3

0.095

-

mutant W357C, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.1

-

wild-type, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.11

-

mutant M147L, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.12

-

mutant G190V, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.12

-

mutant R149C, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.14

-

mutant G190D, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.18

-

mutant M147I, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

0.24

-

mutant A181T, pH not specified in the publication, temperature not specified in the publication

711886

1.8.5.3

3.8

-

mutant R217Q, pH not specified in the publication, temperature not specified in the publication

711886

1.7.2.3

3 entries

1.8.5.3

17 entries

References & Links

Literature References (6)

top print hide

Show Reference (6 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

392773

8639717

High substrate specificity and induction characteristics of trimethylamine N-oxide reductase of Escherichia coli

1996

Iobbi-Nivol, C.; Pommier, J.; Simala-Grant, J.; Mejean, V.; Giordano, G.

Biochim. Biophys. Acta

1294

77-82

392776

10216869

Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli

1999

Buc, J.; Santini, C.; Giordani, R.; Czjzek, M.; Wu, L.; Giordano, G.

Mol. Microbiol.

32

159-168

438920

411486

The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds

1977

Colby, J.; Stirling, D.I.; Dalton, H.

Biochem. J.

165

395-402

711886

9492325

Modulation of the substrate specificity of Escherichia coli dimethylsulfoxide reductase

1998

Simala-Grant, J.L.; Weiner, J.H.

Eur. J. Biochem.

251

510-515

712959

8969520

Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase

1996

Simala-Grant, J.; Weiner, J.

Microbiology

142

3231-3239

715301

21486034

Pyridine inhibitor binding to the 4Fe-4S protein A. aeolicus IspH (LytB): a HYSCORE Investigation

2011

Wang, W.; Li, J.; Wang, K.; Smirnova, T.I.; Oldfield, E.

J. Am. Chem. Soc.

133

6525-6528

Links to other databases for pyridine N-oxide

top print hide

Show Links (1 entry)

ChEBI

PubChem