Aminociklopropankarboksilat oksidaza
| Aminociklopropankarboksilat oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.17.4 | ||||||||
| CAS broj | 98668-53-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Aminociklopropankarboksilat oksidaza (EC 1.14.17.4, ACC oksidaza, etilen-formirajući enzim) je enzim sa sistematskim imenom 1-aminociklopropan-1-karboksilat oksigenaza (formira etilen).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 1-aminociklopropan-1-karboksilat + askorbat + O2 etilen + cijanid + dehidroaskorbat + CO2 + 2H2O
Ovaj enzim sadrži gvožđe nevezano za hem. Za njegov rad je neophodan CO2.
Reference
- ↑ Zhang, Z.H., Schofield, C.J., Baldwin, J.E., Thomas, P. and John, P. (1995). „Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli”. Biochem. J. 307: 77-85. PMID 7717997.
- ↑ Zhang, Z.H., Barlow, J.N., Baldwin, J.E. and Schofield, C.J. (1997). „Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase”. Biochemistry 36: 15999-16007. PMID 9398335.
- ↑ Pirrung, M.C. (1999). „Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid”. Acc. Chem. Res. 32: 711-718.
- ↑ Charng, Y., Chou, S.J., Jiaang, W.T., Chen, S.T. and Yang, S.F. (2001). „The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid oxidase”. Arch. Biochem. Biophys. 385: 179-185. PMID 11361015.
- ↑ Thrower, J.S., Blalock, R. and Klinman, J.P. (2001). „Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase”. Biochemistry 40: 9717-9724. PMID 11583172.
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 Aminocyclopropanecarboxylate+oxidase
- 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
