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Ligand iminosuccinate

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for iminosuccinate

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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

2.5.1.72

glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate

738460, 737716, 738452

-

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

1.4.3.16

L-aspartate + O2 = alpha-iminosuccinate + H2O2

0

-

1.4.3.16

L-aspartate + fumarate = iminosuccinate + succinate

0

-

1.4.3.16

L-aspartate + O2 = iminosuccinate + H2O2

0

-

1.4.3.16

3 entries

Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Substrate (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.72

dihydroxyacetone phosphate + iminoaspartate = ? + H2O + phosphate

686712, 685193

-

2.5.1.72

glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate

738460, 737716, 738452

-

2.5.1.72

2 entries

Product in Enzyme-catalyzed Reactions (6 results)

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Show Product (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.16

L-aspartate + O2 = alpha-iminosuccinate + H2O2

0

-

1.4.3.16

L-aspartate + fumarate = iminoaspartate + succinate

0

-

1.4.3.16

L-aspartate + O2 = iminoaspartate + H2O2

0

-

1.4.3.16

DL-aspartate + O2 = iminosuccinate + H2O2

0

-

1.4.3.16

L-aspartate + fumarate = iminosuccinate + succinate

0

-

1.4.3.16

L-aspartate + O2 = iminosuccinate + H2O2

0

-

1.4.3.16

6 entries

Enzyme Kinetic Parameters

References & Links

Literature References (5)

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Show Reference (5 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

685193

18803397

Characterization of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes

2008

Saunders, A.H.; Griffiths, A.E.; Lee, K.H.; Cicchillo, R.M.; Tu, L.; Stromberg, J.A.; Krebs, C.; Booker, S.J.

Biochemistry

47

10999-11012

686712

18959769

Characterization of L-aspartate oxidase and quinolinate synthase from Bacillus subtilis

2008

Marinoni, I.; Nonnis, S.; Monteferrante, C.; Heathcote, P.; Haertig, E.; Boettger, L.H.; Trautwein, A.X.; Negri, A.; Albertini, A.M.; Tedeschi, G.

FEBS J.

275

5090-5107

737716

26455817

Dual activity of quinolinate synthase: triose phosphate isomerase and dehydration activities play together to form quinolinate

2015

Reichmann, D.; Coute, Y.; Ollagnier de Choudens, S.

Biochemistry

54

6443-6446

738452

24650327

The crystal structure of Fe4S4 quinolinate synthase unravels an enzymatic dehydration mechanism that uses tyrosine and a hydrolase-type triad

2014

Cherrier, M.V.; Chan, A.; Darnault, C.; Reichmann, D.; Amara, P.; Ollagnier de Choudens, S.; Fontecilla-Camps, J.C.

J. Am. Chem. Soc.

136

5253-5256

738460

27224840

Structure of quinolinate synthase from Pyrococcus horikoshii in the presence of its product, quinolinic acid

2016

Esakova, O.A.; Silakov, A.; Grove, T.L.; Saunders, A.H.; McLaughlin, M.I.; Yennawar, N.H.; Booker, S.J.

J. Am. Chem. Soc.

138

7224-7227

Links to other databases for iminosuccinate

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Show Links (1 entry)

ChEBI

PubChem