Aminopirimidna aminohidrolaza
Tiaminaza (EC 3.5.99.2, tiaminaza II, tenA (gen)) je enzim sa sistematskim imenom 4-amino-5-aminometil-2-metilpirimidin aminohidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Tiaminaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.5.99.2 | ||||||||
| CAS broj | 9024-80-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- (1) 4-amino-5-aminometil-2-metilpirimidin + H2O 4-amino-5-hidroksimetil-2-metilpirimidin + amonijak
- (2) tiamin +H2O 4-amino-5-hidroksimetil-2-metilpirimidin + 5-(2-hidroksietil)-4-metiltiazol
Ovaj enzim učestvuje u regeneraciji tiaminskog pirimidina.
Reference uredi
- ↑ Fujita, A., Nose, Y. and Kuratani, K. (1954). „Second type of bacterial thiaminase”. J. Vitaminol. (Kyoto) 1: 1-7. PMID 13243520.
- ↑ Ikehata, H. (1960). „Purification of thiaminase II”. J. Gen. Appl. Microbiol. 6: 30-39.
- ↑ Toms, A.V., Haas, A.L., Park, J.H., Begley, T.P. and Ealick, S.E. (2005). „Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II”. Biochemistry 44: 2319-2329. PMID 15709744.
- ↑ Benach, J., Edstrom, W.C., Lee, I., Das, K., Cooper, B., Xiao, R., Liu, J., Rost, B., Acton, T.B., Montelione, G.T. and Hunt, J.F. (2005). „The 2.35 Å structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism”. Acta Crystallogr. D Biol. Crystallogr. 61: 589-598. PMID 15858269.
- ↑ Jenkins, A.H., Schyns, G., Potot, S., Sun, G. and Begley, T.P. (2007). „A new thiamin salvage pathway”. Nat. Chem. Biol. 3: 492-497. PMID 17618314.
- ↑ Jenkins, A.L., Zhang, Y., Ealick, S.E. and Begley, T.P. (2008). „Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis”. Bioorg. Chem. 36: 29-32. PMID 18054064.
- ↑ French, J.B., Begley, T.P. and Ealick, S.E. (2011). „Structure of trifunctional THI20 from yeast”. Acta Crystallogr. D Biol. Crystallogr. 67: 784-791. PMID 21904031.
Literatura uredi
- 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.