| succinylglutamate-semialdehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.71 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
References
- Vander Wauven C, Jann A, Haas D, Leisinger T, Stalon V (1988). "N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa". Arch. Microbiol. 150 (4): 400–4. doi: 10.1007/BF00408314. PMID 3144259.
- Vander Wauven C, Stalon V (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol. 164 (2): 882–6. PMC 214334. 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 (3): 853–61. doi: 10.1111/j.1432-1033.1994.00853.x. 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 (23): 7280–90. doi: 10.1128/jb.179.23.7280-7290.1997. PMC 179677. PMID 9393691.
- Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180 (16): 4278–86. PMC 107427. PMID 9696779.
- Cunin R, Glansdorff N, Pierard A, Stalon V (1986). "Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 50 (3): 314–52. PMC 373073. PMID 3534538.
- Cunin R, Glansdorff N, Pierard A, Stalon V (1987). "Erratum report: Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 51 (1): 178. PMC 373097. PMID 16350242.
| succinylglutamate-semialdehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.71 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
References
- Vander Wauven C, Jann A, Haas D, Leisinger T, Stalon V (1988). "N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa". Arch. Microbiol. 150 (4): 400–4. doi: 10.1007/BF00408314. PMID 3144259.
- Vander Wauven C, Stalon V (1985). "Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia". J. Bacteriol. 164 (2): 882–6. PMC 214334. 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 (3): 853–61. doi: 10.1111/j.1432-1033.1994.00853.x. 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 (23): 7280–90. doi: 10.1128/jb.179.23.7280-7290.1997. PMC 179677. PMID 9393691.
- Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli". J. Bacteriol. 180 (16): 4278–86. PMC 107427. PMID 9696779.
- Cunin R, Glansdorff N, Pierard A, Stalon V (1986). "Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 50 (3): 314–52. PMC 373073. PMID 3534538.
- Cunin R, Glansdorff N, Pierard A, Stalon V (1987). "Erratum report: Biosynthesis and metabolism of arginine in bacteria". Microbiol. Rev. 51 (1): 178. PMC 373097. PMID 16350242.