Non-homologous isofunctional enzymes: Difference between revisions
Content deleted Content added
there is no confusion with the EC system |
templated citations |
||
| Line 1: | Line 1: | ||
{{Orphan|date=January 2014}} |
{{Orphan|date=January 2014}} |
||
'''Non-homologous isofunctional enzymes''' (NISE) are two [[homology (biology)|evolutionarily]] unrelated [[enzyme]]s that catalyzes the same chemical reaction. As the [[Enzyme Commission number]] (EC) is based on the reaction catalyzed by the enzyme, NISEs that catalyzed the same reaction would be assigned the same EC number, even though there may be no similarity in their [[protein sequence]]s. |
'''Non-homologous isofunctional enzymes''' (NISE) are two [[homology (biology)|evolutionarily]] unrelated [[enzyme]]s that catalyzes the same chemical reaction.<ref name="Omelchenko_2010">{{cite journal | vauthors = Omelchenko MV, Galperin MY, Wolf YI, Koonin EV | title = Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution | journal = Biology Direct | volume = 5 | issue = | pages = 31 | year = 2010 | pmid = 20433725 | pmc = 2876114 | doi = 10.1186/1745-6150-5-31 }}</ref> As the [[Enzyme Commission number]] (EC) is based on the reaction catalyzed by the enzyme, NISEs that catalyzed the same reaction would be assigned the same EC number, even though there may be no similarity in their [[protein sequence]]s. |
||
A recent example is of the enzyme [[urate hydroxylase]] (EC 1.14.13.113) which catalyzes the decomposition of [[urate]], an important constituent of [[nitrogen cycling]]. The newly discovered HpyO gene was non-homologous in sequence to the original gene HpxO |
A recent example is of the enzyme [[urate hydroxylase]] (EC 1.14.13.113) which catalyzes the decomposition of [[urate]], an important constituent of [[nitrogen cycling]]. The newly discovered HpyO gene was non-homologous in sequence to the original gene HpxO<ref name="O'Leary_2009">{{cite journal | vauthors = O'Leary SE, Hicks KA, Ealick SE, Begley TP | title = Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase | journal = Biochemistry | volume = 48 | issue = 14 | pages = 3033–5 | year = 2009 | pmid = 19260710 | pmc = 2842088 | doi = 10.1021/bi900160b }}</ref> but yet shared certain characteristics enabling it to perform a similar reaction.<ref name="Michiel_2012">{{cite journal | vauthors = Michiel M, Perchat N, Perret A, Tricot S, Papeil A, Besnard M, de Berardinis V, Salanoubat M, Fischer C | title = Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO | journal = Environmental Microbiology Reports | volume = 4 | issue = 6 | pages = 642–7 | year = 2012 | pmid = 23760935 | doi = 10.1111/j.1758-2229.2012.00390.x }}</ref> |
||
== References == |
== References == |
||
{{reflist}} |
{{reflist}} |
||
* Marina V Omelchenko, Michael Y Galperin, Yuri I Wolf and Eugene V Koonin. (2010). Non-homologous isofunctional enzymes: A systematic analysis of alternative solutions in enzyme evolution. Biology Direct, 5(31). |
|||
* Seán E. O’Leary, Katherine A. Hicks, Steven E. Ealick, and Tadhg P. Begley. (2009). Biochemical Characterization of the HpxO Enzyme from Klebsiella pneumoniae, a Novel FAD–Dependent Urate Oxidase. Biochemistry. 2009 April 14; 48(14): 3033–3035. doi:10.1021/bi900160b. |
|||
* Magalie Michiel, Nadia Perchat, Alain Perret, Sabine Tricot, Aude Papeil, Marielle Besnard, Véronique de Berardinis, Marcel Salanoubat, and Cécile Fischer. (2012). Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO. Environmental Microbiology reports 4 (6): 642–647. doi:10.1111/j.1758-2229.2012.00390.x. PMID 23760935 |
|||
[[Category:Enzymes]] |
[[Category:Enzymes]] |
||
Revision as of 15:50, 29 April 2017
Non-homologous isofunctional enzymes (NISE) are two evolutionarily unrelated enzymes that catalyzes the same chemical reaction.[1] As the Enzyme Commission number (EC) is based on the reaction catalyzed by the enzyme, NISEs that catalyzed the same reaction would be assigned the same EC number, even though there may be no similarity in their protein sequences.
A recent example is of the enzyme urate hydroxylase (EC 1.14.13.113) which catalyzes the decomposition of urate, an important constituent of nitrogen cycling. The newly discovered HpyO gene was non-homologous in sequence to the original gene HpxO[2] but yet shared certain characteristics enabling it to perform a similar reaction.[3]
References
- ^ Omelchenko MV, Galperin MY, Wolf YI, Koonin EV (2010). "Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution". Biology Direct. 5: 31. doi:10.1186/1745-6150-5-31. PMC 2876114. PMID 20433725.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ O'Leary SE, Hicks KA, Ealick SE, Begley TP (2009). "Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase". Biochemistry. 48 (14): 3033–5. doi:10.1021/bi900160b. PMC 2842088. PMID 19260710.
- ^ Michiel M, Perchat N, Perret A, Tricot S, Papeil A, Besnard M, de Berardinis V, Salanoubat M, Fischer C (2012). "Microbial urate catabolism: characterization of HpyO, a non-homologous isofunctional isoform of the flavoprotein urate hydroxylase HpxO". Environmental Microbiology Reports. 4 (6): 642–7. doi:10.1111/j.1758-2229.2012.00390.x. PMID 23760935.
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |