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Succinylglutamate-semialdehyde dehydrogenase

FieldValue
Namesuccinylglutamate-semialdehyde dehydrogenase
EC_number1.2.1.71
GO_code0043824

The three substrates of this enzyme are N-succinyl-L-glutamic 5-semialdehyde, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are N-succinyl-L-glutamic acid, reduced NADH, and a proton.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N-succinyl-L-glutamate 5-semialdehyde:NAD+ oxidoreductase. Other names in common use include succinylglutamic semialdehyde dehydrogenase, N-succinylglutamate 5-semialdehyde dehydrogenase, SGSD, AruD, and AstD. This enzyme participates in arginine and proline metabolism.

References

References

  1. {{KEGG enzyme. 1.2.1.71
  2. (1988). "N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa". Arch. Microbiol..
  3. (1994). "Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine". Eur. J. Biochem..
  4. Itoh Y. (1997). "Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa". J. Bacteriol..
  5. (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol..
  6. (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol..
  7. (1986). "Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev..
  8. (1987). "Erratum report: Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev..
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ec-1.2.1 nadh-dependent-enzymes enzymes-of-unknown-structure
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