IntEnz

EC 1.2.1.71 - Succinylglutamate-semialdehyde dehydrogenase

IntEnz Enzyme Nomenclature
EC 1.2.1.71

Names

Reaction

• 10812 [IUBMB]
  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  N-succinyl-L-glutamate 5-semialdehyde

  N-succinyl-L-glutamate 5-semialdehyde

  Name origin: UniProt - CHECKED (C)

  CHEBI:58520

  Formula: C9H11NO6
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

  +

  NAD⁺

  NAD(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:57540

  Formula: C21H26N7O14P2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  =

  2

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  N-succinyl-L-glutamate

  N-succinyl-L-glutamate

  Name origin: UniProt - CHECKED (C)

  CHEBI:58763

  Formula: C9H10NO7
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  +

  NADH

  NADH

  Name origin: UniProt - CHECKED (C)

  CHEBI:57945

  Formula: C21H27N7O14P2
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Comments:

This is the fourth enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.11 (acetylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [3,6].

Links to other databases

References

1. Vander Wauven, C., Jann, A., Haas, D., Leisinger, T. and Stalon, V.
   N²-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa.
   Arch. Microbiol. 150: 400-404 (1988). [PMID: 3144259]
2. Vander Wauven, C. and Stalon, V.
   Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia.
   J. Bacteriol. 164: 882-886 (1985). [PMID: 2865249]
3. Tricot, C., Vander Wauven, C., Wattiez, R., Falmagne, P. and Stalon, V.
   Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine.
   Eur. J. Biochem. 224: 853-861 (1994). [PMID: 7523119]
4. Itoh, Y.
   Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.
   J. Bacteriol. 179: 7280-7290 (1997). [PMID: 9393691]
5. Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J.
   Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.
   J. Bacteriol. 180: 4278-4286 (1998). [PMID: 9696779]
6. Cunin, R., Glansdorff, N., Piérard, A. and Stalon, V.
   Biosynthesis and metabolism of arginine in bacteria.
   Microbiol. Rev. 50: 314-352 (1986). [PMID: 3534538]
7. Cunin, R., Glansdorff, N., Piérard, A. and Stalon, V.
   Erratum report. Biosynthesis and metabolism of arginine in bacteria.
   Microbiol. Rev. 51: 178 (1987).

[EC 1.2.1.71 created 2006]