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Ligand N2-succinyl-L-ornithine

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for N2-succinyl-L-ornithine

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Roles as Enzyme Ligand

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

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.3.11

carbamoyl phosphate + N2-succinyl-L-ornithine = phosphate + N-succinyl-L-citrulline

755971, 756983

-

2.6.1.81

N2-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate

34268, 486120, 666762, 644951, 486123

4add, 3D-view

2.6.1.81

N2-succinyl-L-ornithine + 2-oxoglutarate = N2-succinyl-L-glutamate 5-semialdehyde + L-glutamate

486124

4add, 3D-view

2.6.1.81

2 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

2.3.1.109

succinyl-CoA + L-ornithine = CoA + N2-succinyl-L-ornithine

0

-

Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Substrate (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.3.11

N-succinyl-L-ornithine + carbamoyl phosphate = N-succinyl-L-citrulline + phosphate

689906, 687511

-

2.1.3.11

carbamoyl phosphate + N2-succinyl-L-ornithine = phosphate + N-succinyl-L-citrulline

755971, 756983

-

2.1.3.11

2 entries

2.6.1.11

N2-succinyl-L-ornithine + 2-oxoglutarate = N2-succinylglutamate semialdehyde + glutamate

644951

-

2.6.1.81

N2-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate

34268, 486120, 666762, 644951, 486123, 739459

4add, 3D-view

2.6.1.81

N2-succinyl-L-ornithine + 2-oxoglutarate = N2-succinyl-L-glutamate 5-semialdehyde + L-glutamate

486124

4add, 3D-view

2.6.1.81

2 entries

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.109

succinyl-CoA + L-ornithine = CoA + N2-succinyl-L-ornithine

0

-

3.5.3.23

N2-succinyl-L-arginine + H2O = N2-succinyl-L-ornithine + NH3 + CO2

0

-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (2 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.6.1.17

4add, 3D-view

2.6.1.81

4add, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.6.1.81

3

-

pH 8.0, temperature not specified in the publication

739459

K_M Value (7 results)

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Show KM Value (7 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.1.3.11

0.0016

-

mutant P90E/T242L, pH 8.3, 25°C

687511

2.1.3.11

0.195

-

mutant T242L, pH 8.3, 25°C

687511

2.1.3.11

0.238

-

wild-type, pH 8.3, 25°C

687511

2.1.3.11

3 entries

2.6.1.11

1.25

-

-

644951

2.6.1.81

0.284

-

pH 8.0, temperature not specified in the publication

739459

2.6.1.81

0.42

-

wild-type strain PAO1

486120

2.6.1.81

1.25

-

pH 8.5, 37°C, cell extract

644951

2.6.1.81

3 entries

References & Links

Literature References (11)

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Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

34268

3129535

Catabolism of arginine, citrulline and ornithine by Pseudomonas and related bacteria

1987

Stalon, V.; Vander Wauven, C.; Momin, P.; Legrain, C.

J. Gen. Microbiol.

133

2487-2495

486120

3144259

N2-Succinylornithine in ornithine catabolism of Pseudomonas aeruginosa

1988

Vander Wauven, C.; Jann, A.; Haas, D.; Leisinger, T.; Stalon, V.

Arch. Microbiol.

150

400-404

486123

9393691

Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa

1997

Itoh, Y.

J. Bacteriol.

179

7280-7290

486124

9696779

Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli

1998

Schneider, B.L.; Kiupakis, A.K.; Reitzer, L.J.

J. Bacteriol.

180

4278-4286

644951

2865249

Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia

1985

Vander Wauven, C.; Stalon, V.

J. Bacteriol.

164

882-886

666762

16593724

N-Succinylated intermediates in an arginine catabolic pathway of Pseudomonas aeruginosa

1986

Jann, A.; Stalon, V.; Wauven, C.V.; Leisinger, T.; Haas, D.

Proc. Natl. Acad. Sci. USA

83

4937-4941

687511

16704984

Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis

2006

Shi, D.; Morizono, H.; Cabrera-Luque, J.; Yu, X.; Roth, L.; Malamy, M.H.; Allewell, N.M.; Tuchman, M.

J. Biol. Chem.

281

20623-20631

689906

17600144

A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase

2007

Shi, D.; Yu, X.; Cabrera-Luque, J.; Chen, T.Y.; Roth, L.; Morizono, H.; Allewell, N.M.; Tuchman, M.

Protein Sci.

16

1689-1699

739459

23484010

Determination of the structure of the catabolic N-succinylornithine transaminase (AstC) from Escherichia coli

2013

Newman, J.; Seabrook, S.; Surjadi, R.; Williams,C.C.; Lucent, D.; Wilding, M.; Scott, C.; Peat, T.S.

PLoS One

8

e58298

755971

29920242

Comparative folding analyses of unknotted versus trefoil-knotted ornithine transcarbamylases suggest stabilizing effects of protein knots

2018

Sriramoju, M.K.; Yang, T.J.; Hsu, S.D.

Biochem. Biophys. Res. Commun.

503

822-829

756983

26274952

From genome to structure and back again a family portrait of the transcarbamylases

2015

Shi, D.; Allewell, N.M.; Tuchman, M.

Int. J. Mol. Sci.

16

18836-18864

Links to other databases for N2-succinyl-L-ornithine

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Show Links (1 entry)

ChEBI

PubChem