Acireduktonska sintaza
| Acireduktonska sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.1.3.77 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Acireduktonska sintaza (EC 3.1.3.77, E1, E-1 enolaza-fosfataza) je enzim sa sistematskim imenom 5-(metiltio)-2,3-dioksopentil-fosfat fosfohidrolaza (izomerizacija).[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 5-(metiltio)-2,3-dioksopentil fosfat + H2O 1,2-dihidroksi-5-(metiltio)pent-1-en-3-on + fosfat (sveukupna reakcija)
- (1a) 5-(metiltio)-2,3-dioksopentil fosfat 2-hidroksi-5-(metiltio)-3-oksopent-1-enil fosfat (verovatno spontana reakcija)
- (1b) 2-hidroksi-5-(metiltio)-3-oksopent-1-enil fosfat + H2O 1,2-dihidroksi-5-(metiltio)pent-1-en-3-on + fosfat
Ovaj bifunkcionalanni enzim prvo enolizuje supstrat i formira intermedijer 2-hidroksi-5-(metiltio)-3-oksopent-1-enil fosfat, koji se zatim defosforiliše do aciredukton 1,2-dihidroksi-5-(metiltio)pent-1-en-3-ona.
Reference
- ↑ Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. (1993). „Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae”. J. Biol. Chem. 268: 24785-24791. PMID 8227039.
- ↑ Wray, J.W. and Abeles, R.H. (1995). „The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases”. J. Biol. Chem. 270: 3147-3153. PMID 7852397.
- ↑ Wang, H., Pang, H., Bartlam, M. and Rao, Z. (2005). „Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity”. J. Mol. Biol. 348: 917-926. PMID 15843022.
Literatura
- 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.
Vanjske veze
- MeSH Acireductone+synthase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
