Dihydroorotase
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
| - | '''Dihydroorotase''' (DHO) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate<ref>PMID:15610022</ref>. | + | '''Dihydroorotase''' (DHO) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate in the pyrimidine biosynthesis pathway<ref>PMID:15610022</ref>. |
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== Relevance == | == Relevance == | ||
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| + | The difference between bacterial and mammalian DHO makes it a promising drug target<ref>PMID:31207330</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
The 3D structure of the complex of DHO with dihydroorotate and carbamoyl aspartate shows dihydroorotate bound to the protein subunit A active site via electrostatic interactions. The substrate carbamoyl aspartate binds to the active site of subunit B via 2 Thr residues<ref>PMID:17711307</ref>. | The 3D structure of the complex of DHO with dihydroorotate and carbamoyl aspartate shows dihydroorotate bound to the protein subunit A active site via electrostatic interactions. The substrate carbamoyl aspartate binds to the active site of subunit B via 2 Thr residues<ref>PMID:17711307</ref>. | ||
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| + | ==3D structures of dihydroorotase== | ||
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| + | [[Dihydroorotase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| + | [[Category:Topic Page]] | ||
Revision as of 07:19, 13 July 2022
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References
- ↑ Porter TN, Li Y, Raushel FM. Mechanism of the dihydroorotase reaction. Biochemistry. 2004 Dec 28;43(51):16285-92. doi: 10.1021/bi048308g. PMID:15610022 doi:http://dx.doi.org/10.1021/bi048308g
- ↑ Lipowska J, Miks CD, Kwon K, Shuvalova L, Zheng H, Lewinski K, Cooper DR, Shabalin IG, Minor W. Pyrimidine biosynthesis in pathogens - Structures and analysis of dihydroorotases from Yersinia pestis and Vibrio cholerae. Int J Biol Macromol. 2019 Sep 1;136:1176-1187. doi:, 10.1016/j.ijbiomac.2019.05.149. Epub 2019 Jun 15. PMID:31207330 doi:http://dx.doi.org/10.1016/j.ijbiomac.2019.05.149
- ↑ Lee M, Maher MJ, Christopherson RI, Guss JM. Kinetic and structural analysis of mutant Escherichia coli dihydroorotases: a flexible loop stabilizes the transition state. Biochemistry. 2007 Sep 18;46(37):10538-50. Epub 2007 Aug 21. PMID:17711307 doi:10.1021/bi701098e
