Alofanatna hidrolaza
| Alofanatna hidrolaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.5.1.54 | ||||||||
| CAS broj | 9076-72-6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Alofanatna hidrolaza (EC 3.5.1.54, alofanatna lijaza, AtzF, TrzF) je enzim sa sistematskim imenom ureja-1-karboksilat amidohidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ureja-1-karboksilat + H2O 2 CO2 + 2 NH3
Zajedno sa EC 3.5.2.15 (cijanurinsko kiselinska amidohidrolaza) i EC 3.5.1.84 (biuretna amidohidrolaza), ovaj enzim formira deo cijanurinsko-kiselinskog metaboličkog puta.
Reference
- ↑ Maitz, G.S., Haas, E.M. and Castric, P.A. (1982). „Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii”. Biochim. Biophys. Acta 714: 486-491.
- ↑ Roon, R.J. and Levenberg, B. (1972). „Urea amidolyase. I. Properties of the enzyme from Candida utilis”. J. Biol. Chem. 247: 4107-4113. PMID 4556303.
- ↑ Sumrada, R.A. and Cooper, T.G. (1982). „Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast”. J. Biol. Chem. 257: 9119-9127. PMID 6124544.
- ↑ Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H. and Imanaka, T. (2005). „Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea”. FEMS Microbiol. Lett. 245: 61-65. PMID 15796980.
- ↑ Cheng, G., Shapir, N., Sadowsky, M.J. and Wackett, L.P. (2005). „Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism”. Appl. Environ. Microbiol. 71: 4437-4445. PMID 16085834.
- ↑ Shapir, N., Sadowsky, M.J. and Wackett, L.P. (2005). „Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP”. J. Bacteriol. 187: 3731-3738. PMID 15901697.
- ↑ Shapir, N., Cheng, G., Sadowsky, M.J. and Wackett, L.P. (2006). „Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth”. Appl. Environ. Microbiol. 72: 2491-2495. PMID 16597948.
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 Allophanate+hydrolase
- 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
