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Ligand 7,8-dihydromonapterin

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 7,8-dihydromonapterin

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.1.50

7,8-dihydromonapterin + NADPH + H+ = 5,6,7,8-tetrahydromoapterin + NADP+

765008

-

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

4.1.2.25

6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde = 7,8-dihydroneopterin + 7,8-dihydromonapterin

0

1u68, 3D-view

Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Substrate (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.153

L-threo-dihydroneopterin + NADP+ = ?

286026, 286013

-

1.5.1.3

L-threo-7,8-dihydroneopterin + NADPH = ?

392230

-

1.5.1.33

7,8-dihydromonapterin + NADPH + H+ = 5,6,7,8-tetrahydromonapterin + NADP+

765008

-

1.5.1.34

quinonoid dihydro-L-threo-neopterin + NAD(P)H = tetrahydro-L-threo-neopterin + NAD(P)+

484963

-

1.5.1.50

7,8-dihydromonapterin + NADPH + H+ = 5,6,7,8-tetrahydromoapterin + NADP+

765008

-

1.5.1.50

7,8-dihydromonapterin + NADPH + H+ = 5,6,7,8-tetrahydromonapterin + NADP+

704330, 765008

-

4.1.2.25

2-amino-4-hydroxy-6-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = ?

5109, 5104

1u68, 3D-view

4.1.2.25

7,8-dihydro-L-monapterin = ?

678176

1u68, 3D-view

4.1.2.25

7,8-dihydromonapterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde

653544, 727676

1u68, 3D-view

4.1.2.25

7,8-Dihydromonapterin = ?

5109

1u68, 3D-view

1.5.1.50

2 entries

4.1.2.25

4 entries

5.1.99.7

7,8-dihydromonapterin = 7,8-dihydroneopterin

5109

-

5.1.99.8

7,8-dihydromonapterin = 7,8-dihydroneopterin

5109

-

Product in Enzyme-catalyzed Reactions (3 results)

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Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.2.25

6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde = 7,8-dihydroneopterin + 7,8-dihydromonapterin

0

1u68, 3D-view

5.1.99.7

7,8-dihydroneopterin = 7,8-dihydromonapterin

0

-

5.1.99.8

7,8-dihydroneopterin = 7,8-dihydromonapterin

0

-

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

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

EC NUMBER

ENZYME 3D STRUCTURE

4.1.2.25

1u68, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (15 results)

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Show Turnover Number (15 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.5.1.33

0.8

-

recombinant mutant R24A, pH 6.0, 25°C

765008

1.5.1.33

1.4

-

recombinant mutant Y161A, pH 6.0, 25°C

765008

1.5.1.33

2

-

recombinant mutant Y161F/Y163F, pH 6.0, 25°C

765008

1.5.1.33

2.3

-

recombinant wild-type enzyme, pH 6.0, 25°C

765008

1.5.1.33

4.2

-

recombinant mutant Y163F, pH 6.0, 25°C

765008

1.5.1.33

5 entries

1.5.1.50

1.9

-

recombinant enzyme, pH 6.0, 25°C

765008

4.1.2.25

0.0000023

-

mutant enzyme E21A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.0000051

-

mutant enzyme K100A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.0000053

-

mutant enzyme K98A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.0000057

-

mutant enzyme K100Q, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.000006

-

mutant enzyme E73A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.0000065

-

mutant enzyme E22A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.006

-

pH 7.0, 22°C

727676

4.1.2.25

0.01

-

wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.089

-

wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

9 entries

K_M Value (22 results)

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Show KM Value (22 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.1.33

0.0713

-

recombinant wild-type enzyme, pH 6.0, 25°C

765008

1.5.1.33

0.1694

-

recombinant mutant R24A, pH 6.0, 25°C

765008

1.5.1.33

0.2127

-

recombinant mutant Y163F, pH 6.0, 25°C

765008

1.5.1.33

0.3332

-

recombinant mutant Y161F/Y163F, pH 6.0, 25°C

765008

1.5.1.33

0.505

-

recombinant mutant Y161A, pH 6.0, 25°C

765008

1.5.1.33

5 entries

1.5.1.34

1.45

-

-

484963

1.5.1.50

0.147

-

pH 6.0, 22°C

704330

1.5.1.50

0.17

-

recombinant enzyme, pH 6.0, 25°C

765008

4.1.2.25

0.00017

-

pH 7.0, 22°C

727676

4.1.2.25

0.00076

-

mutant enzyme E21A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.0029

-

mutant enzyme K98A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.004

-

mutant enzyme E22A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.0055

-

wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.0095

-

mutant enzyme K100A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

0.016

-

cleavage

5109

4.1.2.25

0.019

-

epimerization

5109

4.1.2.25

0.036

-

cleavage

5109

4.1.2.25

0.057

-

epimerization

5109

4.1.2.25

8

-

wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

4.1.2.25

9.8

-

mutant enzyme E73A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)

678176

1.5.1.50

2 entries

4.1.2.25

12 entries

5.1.99.7

0.066

-

pH 6.2, 37°C, recombinant enzyme

5109

5.1.99.8

0.066

-

pH 8.0, 55°C

5109

References & Links

Literature References (11)

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Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5104

4912541

The biosynthesis of folic acid. XI. Purification and properties of dihydroneopterin aldolase

1970

Mathis, J.B.; Brown, G.M.

J. Biol. Chem.

245

3015-3025

5109

9651328

Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase

1998

Hau¯mann, C.; Rohdich, F.; Schmidt, E.; Bacher, A.; Richter, G.

J. Biol. Chem.

273

17418-17424

286013

4401291

Sepiapterin reductase from horse liver: purification and properties of the enzyme

1971

Katoh, S.

Arch. Biochem. Biophys.

146

202-214

286026

-

Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum

1999

Cho, S.H.; Na, J.U.; Youn, H.; Hwang, C.S.; Lee, C.H.; Kang, S.O.

Biochem. J.

340

497-503

392230

-

The occurence and properties of pteridine reductase: dihydrofolate reductase in Crithidia fasciculata

1983

Oe, H.; Kohashi, M.; Iwai, K.

Agric. Biol. Chem.

47

251-258

484963

8429

Isolation and characterization of dihydropteridine reductase from Pseudomonas species

1976

Williams, C.D.; Dickens, G.; Letendre, C.H.; Guroff, G.; Haines, C.; Shiota, T.

J. Bacteriol.

127

1197-1207

653544

15107504

Folate biosynthesis in higher plants. cDNA cloning, heterologous expression, and characterization of Dihydroneopterin aldolases

2004

Goyer, A.; Illarionova, V.; Roje, S.; Fischer, M.; Bacher, A.; Hanson, A.D.

Plant Physiol.

135

103-111

678176

17176045

Mechanism of dihydroneopterin aldolase: functional roles of the conserved active site glutamate and lysine residues

2006

Wang, Y.; Li, Y.; Yan, H.

Biochemistry

45

15232-15239

704330

19897652

FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa

2010

Pribat, A.; Blaby, I.K.; Lara-Nunez, A.; Gregory, J.F.; de Crecy-Lagard, V.; Hanson, A.D.

J. Bacteriol.

192

475-482

727676

23150985

One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis

2012

Czekster, C.M.; Blanchard, J.S.

J. Am. Chem. Soc.

134

19758-19771

765008

32482721

Enzymatic and mutational analysis of the PruA pteridine reductase required for pterin-dependent control of biofilm formation in Agrobacterium tumefaciens

2020

Labine, M.; DePledge, L.; Feirer, N.; Greenwich, J.; Fuqua, C.; Allen, K.

J. Bacteriol.

202

e00098-20

Links to other databases for 7,8-dihydromonapterin

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Show Links (1 entry)

ChEBI

PubChem