Aristolohenska sintaza
| Aristolohenska sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 4.2.3.9 | ||||||||
| CAS broj | 94185-89-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Aristolohenska sintaza (EC 4.2.3.9, seskviterpenska ciklaza, trans,trans-farnezil difosfat aristolohen-lijaza, trans,trans-farnezil-difosfat difosfat-lijaza (ciklizacija, formira aristolohen)) je enzim sa sistematskim imenom (2E,6E)-farnezil-difosfat difosfat-lijaza (ciklizacija, formira aristolohen).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (2E,6E)-farnezil difosfat aristolohen + difosfat
Inicijalna interna ciklizacija formira monociklični intermedijer germakren A.
Reference
- ↑ Cane, D.E., Prabhakaran, P.C., Oliver, J.S. and McIlwaine, D.B. (1990). „Aristolochene biosynthesis. Stereochemistry of the deprotonation steps in the enzymatic cyclization of farnesyl pyrophosphate”. J. Am. Chem. Soc. 112: 3209-3210.
- ↑ Cane, D.E., Prabhakaran, P.C., Salaski, E.J., Harrison, P.M.H., Noguchi, H. and Rawlings, B.J. (1989). „Aristolochene biosynthesis and enzymatic cyclization of farnesyl pyrophosphate”. J. Am. Chem. Soc. 111: 8914-8916.
- ↑ Hohn, T.M. and Plattner, R.D. (1989). „Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti”. Arch. Biochem. Biophys. 272: 137-143. PMID 2544140.
- ↑ Proctor, R.H. and Hohn, T.M. (1993). „Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti”. J. Biol. Chem. 268: 4543-4548. PMID 8440737.
- ↑ Calvert, M.J., Ashton, P.R. and Allemann, R.K. (2002). „Germacrene A is a product of the aristolochene synthase-mediated conversion of farnesylpyrophosphate to aristolochene”. J. Am. Chem. Soc. 124: 11636-11641. PMID 12296728.
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 Aristolochene+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
