Succinylglutamate-semialdehyde dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a succinylglutamate-semialdehyde dehydrogenase (EC 1.2.1.71) is an enzyme that catalyzes the chemical reaction

N-succinyl-L-glutamate 5-semialdehyde + NAD⁺ + H₂O N-succinyl-L-glutamate + NADH + 2 H⁺

The 3 substrates of this enzyme are N-succinyl-L-glutamate 5-semialdehyde, NAD⁺, and H₂O, whereas its 3 products are N-succinyl-L-glutamate, NADH, and H⁺.

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.

[edit] References

• IUBMB entry for 1.2.1.71
• BRENDA references for 1.2.1.71 (Recommended.)
• PubMed references for 1.2.1.71
• PubMed Central references for 1.2.1.71
• Google Scholar references for 1.2.1.71
• Vander Wauven C, Jann A, Haas D, Leisinger T, Stalon V (1988). "N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa". Arch. Microbiol. 150: 400–4. PMID 3144259. 
• Vander Wauven C, Stalon V (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol. 164: 882–6. PMID 2865249. 
• Tricot C, Vander Wauven C, Wattiez R, Falmagne P, Stalon V (1994). "Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine". Eur. J. Biochem. 224: 853–61. PMID 7523119. 
• Itoh Y (1997). "Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa". J. Bacteriol. 179: 7280–90. PMID 9393691. 
• Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180: 4278–86. PMID 9696779. 
• Cunin R, Glansdorff N, Pierard A, Stalon V (1986). "Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 50: 314–52. PMID 3534538. 
• Cunin R, Glansdorff N, Pierard A and Stalon V (1987). "Erratum report: Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 51: 178. 

[edit] External links

• IUBMB entry for 1.2.1.71

• KEGG entry for 1.2.1.71

• BRENDA entry for 1.2.1.71

• NiceZyme view of 1.2.1.71

• EC2PDB: PDB structures for 1.2.1.71

• PRIAM entry for 1.2.1.71

• PUMA2 entry for 1.2.1.71

• IntEnz: Integrated Enzyme entry for 1.2.1.71

• MetaCyc entry for 1.2.1.71

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0043824: succinylglutamate-semialdehyde dehydrogenase

• AMIGO entry for GO code 0043824: succinylglutamate-semialdehyde dehydrogenase