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]] }} | ||
| - | + | == Function == | |
'''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>. | '''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>. | ||
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| + | ==Structural highlights == | ||
| + | AroE changes its conformation from an open to closed one upon binding of the cofactor NADP. The active site contains the substrate shikimate<ref>PMID:17825835</ref>. | ||
== 3D Structures of shikimate dehydrogenase == | == 3D Structures of shikimate dehydrogenase == | ||
Revision as of 06:22, 29 August 2016
Contents |
Function
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].
Structural highlights
AroE changes its conformation from an open to closed one upon binding of the cofactor NADP. The active site contains the substrate shikimate[2].
3D Structures of shikimate dehydrogenase
Updated on 29-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
- ↑ Bagautdinov B, Kunishima N. Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism. J Mol Biol. 2007 Oct 19;373(2):424-38. Epub 2007 Aug 21. PMID:17825835 doi:10.1016/j.jmb.2007.08.017
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