Alofanatna hidrolaza
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
| Alofanatna hidrolaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.5.1.54 | ||||||||
| CAS broj | 9076-72-6 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- 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
уреди- ^ 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. & Levenberg, B. (1972). „Urea amidolyase. I. Properties of the enzyme from Candida utilis”. J. Biol. Chem. 247: 4107—4113. PMID 4556303.
- ^ Sumrada, R.A. & 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
уреди- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
уреди- Allophanate+hydrolase на US National Library of Medicine Medical Subject Headings (MeSH)
