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• • Molecular Structure
  • Sum Formula
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  • Synonyms
  • InChIKey
  • Pathways
• 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 D-mannonate

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for D-mannonate

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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

1.1.1.57

D-mannonate + NAD+ = D-fructuronate + NADH

287128, 287129, 287131, 287132, 287133, 287130

-

4.2.1.8

D-mannonate = ?

5902, 5899, 5903

3dbn, 3D-view

4.2.1.8

D-mannonate = ?

5902, 5899, 5903

4eay, 3D-view

4.2.1.8

D-mannonate = ?

5902, 5899, 5903

4kpl, 3D-view

4.2.1.8

3 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

1.1.1.131

D-mannuronate + NADPH = D-mannonate + NADP+

5902

-

Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Substrate (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

D-mannonate + NADH + H+ = ?

745695

-

1.1.1.45

D-mannonic acid + NAD+ = ?

286905

-

1.1.1.57

D-mannonate + NAD+ = D-fructuronate + NADH

287128, 287129, 287130, 287131, 287132, 287133

-

1.1.1.57

D-mannonate + NADP+ = D-fructuronate + NADPH

287129

-

1.1.1.57

2 entries

4.2.1.39

D-mannonate = ?

5696, 5688, 691429

-

4.2.1.68

D-mannonate = 2-dehydro-3-deoxy-D-mannonate + H2O

747890

-

4.2.1.8

D-Mannonate = 2-Dehydro-3-deoxy-D-gluconate + H2O

5899, 5900, 5901, 5903, 5902, 704307, 730286, 747075

3dbn, 3D-view

4.2.1.8

D-Mannonate = 2-Dehydro-3-deoxy-D-gluconate + H2O

5899, 5900, 5901, 5903, 5902, 704307, 730286, 747075

4eay, 3D-view

4.2.1.8

D-Mannonate = 2-Dehydro-3-deoxy-D-gluconate + H2O

5899, 5900, 5901, 5903, 5902, 704307, 730286, 747075

4kpl, 3D-view

4.2.1.8

D-mannonate = ?

5902, 5899, 5903

3dbn, 3D-view

4.2.1.8

D-mannonate = ?

5902, 5899, 5903

4eay, 3D-view

4.2.1.8

D-mannonate = ?

5902, 5899, 5903

4kpl, 3D-view

4.2.1.8

6 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.131

D-mannuronate + NADPH = D-mannonate + NADP+

5902

-

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.57

non-competitive

287131

-

1.1.1.58

inhibitory for forward and reverse reaction

287140

-

2.7.1.197

-

736548

-

3D Structure of Enzyme-Ligand-Complex (PDB) (9 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (9 entries)

EC NUMBER

ENZYME 3D STRUCTURE

4.2.1.8

3dbn, 3D-view

4.2.1.8

4eay, 3D-view

4.2.1.8

4kpl, 3D-view

4.2.1.8

3dbn, 3D-view

4.2.1.8

4eay, 3D-view

4.2.1.8

4kpl, 3D-view

4.2.1.8

3dbn, 3D-view

4.2.1.8

4eay, 3D-view

4.2.1.8

4kpl, 3D-view

4.2.1.8

9 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (12 results)

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Show Turnover Number (12 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.1

0.53

-

at pH 7.9 and 25°C

745695

4.2.1.8

0.09

-

mutant enzyme H311A, at pH 7.5 and 37°C

704307

4.2.1.8

0.1

-

mutant N103A/D109A, pH 7.5, 37°C

730286

4.2.1.8

0.23

-

mutant E185D, pH 7.5, 37°C

730286

4.2.1.8

0.29

-

mutant E186D, pH 7.5, 37°C

730286

4.2.1.8

0.81

-

wild-type, pH 7.5, 37°C

730286

4.2.1.8

0.94

-

mutant E185G, pH 7.5, 37°C

730286

4.2.1.8

1.1

-

mutant E186G, pH 7.5, 37°C

730286

4.2.1.8

1.29

-

mutant H32G, pH 7.5, 37°C

730286

4.2.1.8

1.4

-

mutant N36G, pH 7.5, 37°C

730286

4.2.1.8

1.6

-

pH 7.9, 25°C

747075

4.2.1.8

5.88

-

wild type enzyme, at pH 7.5 and 37°C

704307

4.2.1.8

11 entries

K_M Value (15 results)

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Show KM Value (15 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.1

14

-

at pH 7.9 and 25°C

745695

1.1.1.57

0.78

-

-

287129

1.1.1.57

1.7

-

-

287130

1.1.1.57

1.8

-

-

287133

4.2.1.8

1.9

-

mutant enzyme H311A, at pH 7.5 and 37°C

704307

4.2.1.8

2.31

-

mutant E185D, pH 7.5, 37°C

730286

4.2.1.8

3

-

wild type enzyme, at pH 7.5

704307

4.2.1.8

3.6

-

mutant E186D, pH 7.5, 37°C

730286

4.2.1.8

4.08

-

mutant N103A/D109A, pH 7.5, 37°C

730286

4.2.1.8

4.55

-

mutant E185G, pH 7.5, 37°C

730286

4.2.1.8

4.67

-

mutant N36G, pH 7.5, 37°C

730286

4.2.1.8

4.79

-

wild-type, pH 7.5, 37°C

730286

4.2.1.8

5.21

-

mutant H32G, pH 7.5, 37°C

730286

4.2.1.8

5.3

-

mutant E186G, pH 7.5, 37°C

730286

4.2.1.8

20

-

-

5899, 5900

1.1.1.57

3 entries

4.2.1.8

11 entries

References & Links

Literature References (22)

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Show Reference (22 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5688

5383859

The occurence of a modified Entner-Doudoroff pathway in Clostridium aceticum

1969

Andreesen, J.R.; Gottschalk, G.

Arch. Microbiol.

69

160-170

5696

-

Some properties of D-gluconate dehydratase from Penicillium citrinum

1986

Hassan, M.M.; Hosseny, E.N.; Elzainy, T.A.; Allam, A.M.

Egypt. J. Bot.

29/30

211-220

5899

4581499

Purification et proprietes de la D-mannonate hydrolase d'Escherichia coli'

1973

Robert-Baudouy, J.M.; Stoeber, F.R.

Biochim. Biophys. Acta

309

473-485

5900

6759855

D-Mannonate and D-altronate dehydratases of Escherichia coli K12

1982

Robert-Baudouy, J.; Jimeno-Abendano, J.; Stoeber, F.

Methods Enzymol.

90

288-294

5901

3038546

The role of iron in the activation of mannonic and altronic acid hydratases, two Fe-requiring hydro-lyases

1987

Dreyer, J.L.

Eur. J. Biochem.

166

623-630

5902

4388117

Aldohexuronic acid catabolism by a soil Aeromonas

1969

Farmer, J.J.; Eagon, R.G.

J. Bacteriol.

97

97-106

5903

13584413

A new pathway of uronic acid metabolism

1958

Ashwell, G.; Wahba, A.J.; Hickman, J.

Biochim. Biophys. Acta

30

186-187

286905

-

Purification and properties of beta-L-hydroxy acid dehydrogenase

1961

Smiley, J.D.; Ashwell, G.

J. Biol. Chem.

236

357-364

287128

14401695

Uronic acid metabolism in bacteria. II Purification and properties of D-altronic acid and D-mannonic acid dehydrogenase in Escherichia coli

1960

Hickman, J.; Ashwell, G.

J. Biol. Chem.

235

1566-1570

287129

6755169

D-Mannonate and D-altronate-NAD dehydrogenases from Escherichia coli

1982

Portalier, R.; Stoeber, F.

Methods Enzymol.

89

210-218

287130

4564054

Colorimetric determinations of aldonate oxidoreductases of Escherichia coli K 12: applications

1972

Portalier, R.C.; Stoeber, F.R.

Biochim. Biophys. Acta

289

19-27

287131

195622

Hit-and-run mechanism for D-glucuronate reduction catalyzed by D-mannonate:NAD oxidoreductase of Escherichia coli

1977

Mandrand-Berthelot, M.A.; Lagarde, A.E.

Biochim. Biophys. Acta

483

6-23

287132

4351435

D-Mannonate: NAD-oxidoreductase from Escherichia coli K12. Kinetic studies of the enzymatic mechanism

1972

Portalier, R.C.

Eur. J. Biochem.

30

220-233

287133

4402996

D-Mannonate: NAD oxidoreductase from Escherichia coli K12. Purification, properties and specificity

1972

Portalier, R.C.; Stoeber, F.R.

Eur. J. Biochem.

26

290-300

287140

4351434

D-Altronate: NAD-oxidoreductase from Escherichia coli K12. Kinetic studies

1972

Portalier, R.C.

Eur. J. Biochem.

30

211-219

691429

-

Identification and characterization of the bacterial D-gluconate dehydratase in Achromobacter xylosoxidans

2008

Kim, S.; Lee, S.B.

Biotechnol. Bioprocess Eng.

13

436-444

704307

19617363

Crystal structures of Streptococcus suis mannonate dehydratase (ManD) and its complex with substrate: genetic and biochemical evidence for a catalytic mechanism

2009

Zhang, Q.; Gao, F.; Peng, H.; Cheng, H.; Liu, Y.; Tang, J.; Thompson, J.; Wei, G.; Zhang, J.; Du, Y.; Yan, J.; Gao, G.F.

J. Bacteriol.

191

5832-5837

730286

22796868

Structural insights into decreased enzymatic activity induced by an insert sequence in mannonate dehydratase from Gram negative bacterium

2012

Qiu, X.; Tao, Y.; Zhu, Y.; Yuan, Y.; Zhang, Y.; Liu, H.; Gao, Y.; Teng, M.; Niu, L.

J. Struct. Biol.

180

327-334

736548

6427236

Substrate and phospholipid specificity of the purified mannitol permease of Escherichia coli

1983

Jacobson, G.; Tanney, L.; Kelly, D.; Palman, K.; Corn, S.

J. Cell. Biochem.

23

231-240

745695

29697194

Substrate scope of a dehydrogenase from Sphingomonas species A1 and its potential application in the synthesis of rare sugars and sugar derivatives

2018

Beer, B.; Pick, A.; Doering, M.; Lommes, P.; Sieber, V.

Microb. Biotechnol.

11

747-758

747075

25145794

Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily pathways for the catabolism of L-gulonate and L-idonate

2014

Wichelecki, D.J.; Vendiola, J.A.; Jones, A.M.; Al-Obaidi, N.; Almo, S.C.; Gerlt, J.A.

Biochemistry

53

5692-5699

747890

24382357

Categorisation of sugar acid dehydratases in Aspergillus niger

2014

Motter, F.A.; Kuivanen, J.; Keraenen, H.; Hilditch, S.; Penttilae, M.; Richard, P.

Fungal Genet. Biol.

64

67-72

Links to other databases for D-mannonate

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Show Links (1 entry)

ChEBI

PubChem

-