2-Hidroksimukonatna tautomeraza
2-Hidroksimukonatna tautomeraza (EC 5.3.2.6, 4-oksalokrotonatna tautomeraza, 4-oksalokrotonatna izomeraza, cnbG (gen), praC (gen), xylH (gen)) je enzim sa sistematskim imenom (2Z,4E)-2-hidroksiheksa-2,4-dienedioat keto—enol izomeraza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| 2-Hidroksimukonatna tautomeraza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 5.3.2.6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- (2Z,4E)-2-hidroksiheksa-2,4-dienedioat (3E)-2-oksoheks-3-enedioat
Ovaj enzim učestvuje u putu meta-odvajanja tokom degradacije fenola.
Reference uredi
- ↑ Whitman, C.P., Aird, B.A., Gillespie, W.R. and Stolowich, N.J. (1991). „Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol”. J. Am. Chem. Soc. 113: 3154-3162.
- ↑ Whitman, C.P., Hajipour, G., Watson, R.J., Johnson, W.H., Jr., Bembenek, M.E. and Stolowich, N.J. (1992). „Stereospecific ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase and 5-(carboxymethyl)-2-hydroxymuconate isomerase”. J. Am. Chem. Soc. 114: 10104-10110.
- ↑ Subramanya, H.S., Roper, D.I., Dauter, Z., Dodson, E.J., Davies, G.J., Wilson, K.S. and Wigley, D.B. (1996). „Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases”. Biochemistry 35: 792-802. PMID 8547259.
- ↑ Stivers, J.T., Abeygunawardana, C., Mildvan, A.S., Hajipour, G., Whitman, C.P. and Chen, L.H. (1996). „Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies”. Biochemistry 35: 803-813. PMID 8547260.
- ↑ Wang, S.C., Johnson, W.H., Jr., Czerwinski, R.M., Stamps, S.L. and Whitman, C.P. (2007). „Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in Bacillus subtilis: mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions”. Biochemistry 46: 11919-11929. PMID 17902707.
- ↑ Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. (2009). „Uncovering the protocatechuate 2,3-cleavage pathway genes”. J. Bacteriol. 191: 6758-6768. PMID 19717587.
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.