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• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
  • Links

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Ligand azurin

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.17.9.1

4-cresol + azurin + H2O = 4-hydroxybenzaldehyde + reduced azurin

437869, 437871

-

1.20.99.1

arsenite + azurin + H2O = arsenate + reduced azurin

658961

-

1.7.2.1

reduced azurin + O2 = oxidized azurin + H2O

644786, 395063

-

1.7.2.1

nitrite + reduced azurin I = NO + oxidized azurin I

671644

-

1.7.2.1

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.17.9.1

4-cresol + azurin + H2O = 4-hydroxybenzaldehyde + reduced azurin

-

-

1.20.99.1

arsenite + azurin + H2O = arsenate + reduced azurin

-

-

1.7.2.1

nitrite + reduced azurin I = NO + oxidized azurin I

-

-

Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Substrate (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.5

azurin + H2O2 = oxidized azurin + ?

394610, 394612

-

1.17.9.1

4-cresol + azurin + H2O = 4-hydroxybenzaldehyde + reduced azurin

437869, 437871

-

1.20.9.1

arsenite + H2O + azurin(ox) = arsenate + azurin(red)

690420, 692109

-

1.20.9.1

arsenite + H2O + azurin(oxidized) = arsenate + azurin(reduced)

287857, 287858

-

1.20.9.1

arsenate + azurin(red) = arsenite + H2O + azurin(ox)

287859

-

1.20.9.1

3 entries

1.20.99.1

arsenite + azurin + H2O = arsenate + reduced azurin

658961

-

1.4.9.2

ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin

396593, 715426

-

1.7.2.1

nitrite + reduced azurin = NO + H2O + oxidized azurin

657476

-

1.7.2.1

nitrite + reduced azurin = NO + oxidized azurin

658638

-

1.7.2.1

NO2- + reduced azurin = NO + oxidized azurin

644786

-

1.7.2.1

reduced azurin + O2 = oxidized azurin + H2O

644786, 395063

-

1.7.2.1

nitrite + reduced azurin I = NO + azurin I

696239

-

1.7.2.1

nitrite + reduced azurin I = NO + oxidized azurin I

671644

-

1.7.2.1

6 entries

Product in Enzyme-catalyzed Reactions (8 results)

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Show Product (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.17.9.1

4-cresol + azurin + H2O = 4-hydroxybenzaldehyde + reduced azurin

-

-

1.17.9.2

(+)-pinoresinol + 2 oxidized azurin + H2O = (+)-6-hydroxypinoresinol + 2 reduced azurin + 2 H+

-

-

1.20.9.1

arsenate + azurin(red) = arsenite + H2O + azurin(ox)

-

-

1.20.9.1

arsenite + H2O + azurin(ox) = arsenate + azurin(red)

-

-

1.20.9.1

arsenite + H2O + azurin(oxidized) = arsenate + azurin(reduced)

287857, 287858

-

1.20.9.1

3 entries

1.20.99.1

arsenite + azurin + H2O = arsenate + reduced azurin

-

-

1.4.9.2

ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin

-

-

1.7.2.1

nitrite + reduced azurin I = NO + oxidized azurin I

-

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.20.9.1

27

-

-

287857

1.4.9.2

64

-

in 0.01 M potassium phosphate buffer

396593

1.4.9.2

91

-

in 0.25 M potassium phosphate buffer

396593

1.7.2.1

1

-

recombinant Y10F mutant enzyme, at pH 6.2 and 27°C

395070

1.7.2.1

1.12

-

recombinant wild-type enzyme, at pH 6.2 and 27°C

395070

1.7.2.1

3.2

-

-

395067

1.4.9.2

2 entries

1.7.2.1

3 entries

K_M Value (6 results)

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Show KM Value (6 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.20.9.1

0.008

-

-

287857

1.4.9.2

0.044

-

in 0.25 M potassium phosphate buffer

396593

1.4.9.2

0.137

-

in 0.01 M potassium phosphate buffer

396593

1.7.2.1

0.00084

-

recombinant Y10F mutant enzyme, at pH 6.2 and 27°C

395070

1.7.2.1

0.035

-

recombinant wild-type and Y10F mutant enzyme, at pH 6.2 and 27°C

395070

1.7.2.1

0.049

-

-

395067

1.4.9.2

2 entries

1.7.2.1

3 entries

References & Links

Literature References (20)

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Show Reference (20 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

287857

1331097

The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase

1992

Anderson, G.L.; Williams, J.; Hille, R.

J. Biol. Chem.

267

23674-23682

287858

11250197

Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A

2001

Ellis, P.J.; Conrads, T.; Hille, R.; Kuhn, P.

Structure

9

125-132

287859

9738904

Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis

1998

Krafft, T.; Macy, J.M.

Eur. J. Biochem.

255

647-653

394610

6307263

Pseudomonas cytochrome C-551 peroxidase. A purification procedure and study of CO-binding kinetics

1983

Foote, N.; Thompson, A.C.; Barber, D.; Greenwood, C.

Biochem. J.

209

701-707

394612

226080

Isolation and properties of cytochrome c peroxidase from Pseudomonas denitrificans

1979

Coulson, A.F.W.; Oliver, R.I.C.

Biochem. J.

181

159-169

395063

7893816

Pseudomonas aeruginosa nitrite reductase (or cytochrome oxidase): an overview

1994

Silvestrini, M.C.; Falcinelli, S.; Ciabatti, I.; Cutruzzola, F.; Brunori, M.

Biochimie

76

641-654

395067

-

Kinetics of electron transfer in Pseudomonas aeruginosa cytochrome cd1-nitrite reductase

1996

Schichman, S.A.; Meyer, T.E.; Gray, H.B.

Inorg. Chim. Acta

243

25-31

395070

9256253

Mutagenesis of nitrite reductase from Pseudomonas aeruginosa: tyrosine-10 in the c heme domain is not involved in catalysis

1997

Cutruzzola, f.; Arese, M.; Grasso, S.; Bellelli, A.; Brunori, M.

FEBS Lett.

412

365-369

396593

7547967

Electron transfer reactions between aromatic amine dehydrogenase and azurin

1995

Hyun, Y.L.; Davidson, V.L.

Biochemistry

34

12249-12254

437869

-

Azurin from Pseudomonas putida: an electron acceptor for p-cresol methylhydroxylase

1984

Causer, M.J.; Hopper, D.J.; McIntire, W.S.; Singer, T.P.

Biochem. Soc. Trans.

12

1131-1132

437871

3920077

Periplasmic location of p-cresol methylhydroxylase in Pseudomonas putida

1985

Hopper, D.J.; Jones, M.R.; Causer, M.J.

FEBS Lett.

182

485-488

644786

11139389

Catalytic and spectroscopic analysis of blue copper-containing nitrite reductase mutants altered in the environment of the type 2 copper centre: implications for substrate interaction

2001

Prudencio, M.; Eady, R.R.; Sawers, G.

Biochem. J.

353

259-266

657476

15583395

Crystallization and preliminary x-ray crystallographic studies of dissimilatory nitrite reductase isolated from Hyphomicrobium denitrificans A3151

2004

Xie, Y.; Inoue, T.; Seike, N.; Matsumura, H.; Kanbayashi, K.; Itoh, K.; Kataoka, K.; Yamaguchi, K.; Suzuki, S.; Kai, Y.; Deligeer

Acta Crystallogr. Sect. D

D60

2383-2386

658638

15182351

Copper-containing nitrite reductase from Pseudomonas chlororaphis DSM 50135

2004

Pinho, D.; Besson, S.; Brondino, C.D.; de Castro, B.; Moura, I.

Eur. J. Biochem.

271

2361-2369

658961

12236735

The active site of arsenite oxidase from Alcaligenes faecalis

2002

Conrads, T.; Hemann, C.; George, G.N.; Pickering, I.J.; Prince, R.C.; Hille, R.

J. Am. Chem. Soc.

124

11276-11277

671644

16832626

Coordinate synthesis of azurin I and copper nitrite reductase in Alcaligenes xylosoxidans during denitrification

2006

Harris, R.L.; Eady, R.R.; Hasnain, S.S.; Sawers, R.G.

Arch. Microbiol.

186

241-249

690420

17874847

Biosensor for arsenite using arsenite oxidase and multiwalled carbon nanotube modified electrodes

2007

Male, K.B.; Hrapovic, S.; Santini, J.M.; Luong, J.H.

Anal. Chem.

79

7831-7837

692109

17359265

Detection, diversity and expression of aerobic bacterial arsenite oxidase genes

2007

Inskeep, W.P.; Macur, R.E.; Hamamura, N.; Warelow, T.P.; Ward, S.A.; Santini, J.M.

Environ. Microbiol.

9

934-943

696239

19053252

Identification of the proton channel to the active site type 2 Cu center of nitrite reductase: structural and enzymatic properties of the His254Phe and Asn90Ser mutants

2008

Hough, M.A.; Eady, R.R.; Hasnain, S.S.

Biochemistry

47

13547-13553

715426

7876189

Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes

1995

Edwards, S.L.; Davidson, V.L.; Hyun, Y.L.; Wingfield, P.T.

J. Biol. Chem.

270

4293-4298

Links to other databases for azurin

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Show Links (1 entry)

ChEBI

PubChem

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