Shikimate dehydrogenase
From Proteopedia
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{{STRUCTURE_2ev9| PDB=2ev9 | SIZE=350| SCENE= |right|CAPTION=Shikimate dehydrogenase dimer complex with shikimate, sulfate and NADP [[2ev9]] }} | {{STRUCTURE_2ev9| PDB=2ev9 | SIZE=350| SCENE= |right|CAPTION=Shikimate dehydrogenase dimer complex with shikimate, sulfate and NADP [[2ev9]] }} | ||
| - | '''Shikimate dehydrogenase''' (AroE) catalyzes the conversion of shikimate and NADP+ to 3-dihydroshikimate, NADPH and H+. It is part of the shikimate pathway which is responsible for the biosynthesis of phenylalanine, tyrosine and tryptophan. This pathway is found in bacteria, fungi, plants, algae and parasites and is missing in animals and humans. | + | '''Shikimate dehydrogenase''' (AroE) catalyzes the conversion of shikimate and NADP+ to 3-dihydroshikimate, NADPH and H+. It is part of the shikimate pathway which is responsible for the biosynthesis of phenylalanine, tyrosine and tryptophan. This pathway is found in bacteria, fungi, plants, algae and parasites and is missing in animals and humans<ref>PMID:18669580</ref>. |
== 3D Structures of shikimate dehydrogenase == | == 3D Structures of shikimate dehydrogenase == | ||
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**[[3jyq]] - CgAroE + shikimate + NAD <br /> | **[[3jyq]] - CgAroE + shikimate + NAD <br /> | ||
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| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:13, 28 August 2016
Shikimate dehydrogenase (AroE) catalyzes the conversion of shikimate and NADP+ to 3-dihydroshikimate, NADPH and H+. It is part of the shikimate pathway which is responsible for the biosynthesis of phenylalanine, tyrosine and tryptophan. This pathway is found in bacteria, fungi, plants, algae and parasites and is missing in animals and humans[1].
3D Structures of shikimate dehydrogenase
Updated on 28-August-2016
References
- ↑ Singh S, Stavrinides J, Christendat D, Guttman DS. A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass. Mol Biol Evol. 2008 Oct;25(10):2221-32. doi: 10.1093/molbev/msn170. Epub 2008 Jul, 31. PMID:18669580 doi:http://dx.doi.org/10.1093/molbev/msn170
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