Asparaginska sintaza (glutamin-hidrolizujuća)
Asparaginska sintaza (glutamin-hidrolizujuća) (EC 6.3.5.4, asparaginska sintetaza (glutaminska hidroliza), glutamin-zavisna asparaginska sintetaza, asparaginska sintetaza B, AS, AS-B) je enzim sa sistematskim imenom L-aspartat:L-glutamin amido-ligaza (formira AMP).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Asparaginska sintaza (glutamin-hidrolizujuća) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Asparaginska sintetaza B, dimer, E.Coli | |||||||||
| Identifikatori | |||||||||
| EC broj | 6.3.5.4 | ||||||||
| CAS broj | 37318-72-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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- ATP + L-aspartat + L-glutamin + H2O AMP + difosfat + L-asparagin + L-glutamat (sveukupna reakcija)
- (1a) L-glutamin + H2O L-glutamat + NH3
- (1b) ATP + L-aspartat + NH3 AMP + difosfat + L-asparagin
Enzim iz Escherichia coli ima dva aktivna mesta.
Reference
uredi- ↑ Patterson, M.K., Jr. and Orr, G.R. (1968). „Asparagine biosynthesis by the Novikoff hepatoma. Isolation, purification, property, and mechanism studies of the enzyme system”. J. Biol. Chem. 243: 376-380. PMID 4295091.
- ↑ Boehlein, S.K., Richards, N.G. and Schuster, S.M. (1994). „Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad”. J. Biol. Chem. 269: 7450-7457. PMID 7907328.
- ↑ Richards, N.G. and Schuster, S.M. (1998). „Mechanistic issues in asparagine synthetase catalysis”. Adv. Enzymol. Relat. Areas Mol. Biol. 72: 145-198. PMID 9559053.
- ↑ Larsen, T.M., Boehlein, S.K., Schuster, S.M., Richards, N.G., Thoden, J.B., Holden, H.M. and Rayment, I. (1999). „Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product”. Biochemistry 38: 16146-16157. PMID 10587437.
- ↑ Huang, X., Holden, H.M. and Raushel, F.M. (2001). „Channeling of substrates and intermediates in enzyme-catalyzed reactions”. Annu. Rev. Biochem. 70: 149-180. PMID 11395405.
- ↑ Tesson, A.R., Soper, T.S., Ciustea, M. and Richards, N.G. (2003). „Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli”. Arch. Biochem. Biophys. 413: 23-31. PMID 12706338.
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.