Sukcinilglutamat-semialdehid dehidrogenaza
Sukcinilglutamat-semialdehid dehidrogenaza (EC 1.2.1.71, sukcinilglutaminska semialdehidna dehidrogenaza, N-sukcinilglutamat 5-semialdehidna dehidrogenaza, SGSD, AruD, AstD) je enzim sa sistematskim imenom N-sukcinil-L-glutamat 5-semialdehid:NAD+ oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Sukcinilglutamat-semialdehid dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.2.1.71 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- N-sukcinil-L-glutamat 5-semialdehid + NAD+ +H2O N-sukcinil-L-glutamat + NADH + 2 H+
Ovaj enzim je četvrti u putu argininske sukciniltransferaze (AST) katabolizma arginina. Tim metaboličkim putem se konvertuje ugljenični skeleton arginina u glutamat, uz istovremenu produkciju amonijaka i konverziju sukcinil-KoA u sukcinat i KoA. Pet enzima koji učestvuju u ovom putu su: EC 2.3.1.109 (arginin N-sukciniltransferaza), EC 3.5.3.23 (N-sukcinilarginin dihidrolaza), EC 2.6.1.11 (acetilornitin transaminaza), EC 1.2.1.71 (sukcinilglutamat-semialdehid dehidrogenaza) i EC 3.5.1.96 (sukcinilglutamat desukcinilaza).
Reference
uredi- ↑ Vander Wauven, C., Jann, A., Haas, D., Leisinger, T. and Stalon, V. (1988). „N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa”. Arch. Microbiol. 150: 400-404. PMID 3144259.
- ↑ Vander Wauven, C. and Stalon, V. (1985). „Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia”. J. Bacteriol. 164: 882-886. PMID 2865249.
- ↑ Tricot, C., Vander Wauven, C., Wattiez, R., Falmagne, P. and Stalon, V. (1994). „Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine”. Eur. J. Biochem. 224: 853-861. 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: 7280-7290. PMID 9393691.
- ↑ Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. (1998). „Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli”. J. Bacteriol. 180: 4278-4286. PMID 9696779.
- ↑ Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. (1986). „Biosynthesis and metabolism of arginine in bacteria”. Microbiol. Rev. 50: 314-352. PMID 3534538.
- ↑ Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. (1987). „Erratum report: Biosynthesis and metabolism of arginine in bacteria”. Microbiol. Rev. 51: 178-178.
Literatura
uredi- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.