Shikimate dehydrogenase
From Proteopedia
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| + | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | + | *Shikimate dehydrogenase | |
| - | [[1p74]], [[1p77]] – AroE – ''Haemophilus influenzae''<br /> | + | **[[1p74]], [[1p77]] – AroE – ''Haemophilus influenzae''<br /> |
| - | [[1wxd]] – TtAroE – ''Thermus thermophilus'' <br /> | + | **[[1wxd]] – TtAroE – ''Thermus thermophilus'' <br /> |
| - | [[2hk7]], [[2hk8]] – AaAroE – ''Aquifex aeolicus'' <br /> | + | **[[2hk7]], [[2hk8]] – AaAroE – ''Aquifex aeolicus'' <br /> |
| - | [[2egg]] – AroE – ''Geobacillus kaustophilus'' <br /> | + | **[[2egg]] – AroE – ''Geobacillus kaustophilus'' <br /> |
| - | [[3fbt]] – AroE/chorismate mutase – ''Clostridium acetobutylicum'' <br /> | + | **[[3fbt]] – AroE/chorismate mutase – ''Clostridium acetobutylicum'' <br /> |
| - | [[3don]] – SeAroE – ''Staphylococcus epidermidis'' <br /> | + | **[[3don]] – SeAroE – ''Staphylococcus epidermidis'' <br /> |
| - | [[3o8q]] – VcAroE – ''Vibrio cholerae'' <br /> | + | **[[3o8q]] – VcAroE – ''Vibrio cholerae'' <br /> |
| - | [[3pwz]] – AroE 3 – ''Pseudomonas putida'' <br /> | + | **[[3pwz]] – AroE 3 – ''Pseudomonas putida'' <br /> |
| - | [[3phg]] – HpAroE – ''Helicobacter pylori'' <br /> | + | **[[3phg]] – HpAroE – ''Helicobacter pylori'' <br /> |
| - | [[4foo]], [[4fpx]] – HpAroE (mutant) <br /> | + | **[[4foo]], [[4fpx]] – HpAroE (mutant) <br /> |
| - | [[3u62]] – AroE – ''Thermotoga maritima'' <br /> | + | **[[3u62]] – AroE – ''Thermotoga maritima'' <br /> |
| - | [[2nlo]] – CgAroE – ''Corynebacterium glutamicum''<br /> | + | **[[2nlo]] – CgAroE – ''Corynebacterium glutamicum''<br /> |
| - | + | *Shikimate dehydrogenase complex with NADP | |
| - | [[1nyt]], [[1vi2]] – EcAroE + NADP – ''Escherichia coli''<br /> | + | **[[1nyt]], [[1vi2]] – EcAroE + NADP – ''Escherichia coli''<br /> |
| - | [[1nvt]] – MjAroE + NADP – ''Methanocaldococcus jannaschii''<br /> | + | **[[1nvt]] – MjAroE + NADP – ''Methanocaldococcus jannaschii''<br /> |
| - | [[2cy0]] – TtAroE + NADP <br /> | + | **[[2cy0]] – TtAroE + NADP <br /> |
| - | [[3toz]] – LmAroE + NAD – ''Listeria monocytogenes''<br /> | + | **[[3toz]] – LmAroE + NAD – ''Listeria monocytogenes''<br /> |
| - | [[3t4e]] – AroE + NAD – ''Salmonella enterica''<br /> | + | **[[3t4e]] – AroE + NAD – ''Salmonella enterica''<br /> |
| - | [[3jyo]] - CgAroE + NAD <br /> | + | **[[3jyo]] - CgAroE + NAD <br /> |
| - | + | *Shikimate dehydrogenase complex with shikimate | |
| - | [[2d5c]] – TtAroE + shikimate <br /> | + | **[[2d5c]] – TtAroE + shikimate <br /> |
| - | [[3doo]] – SeAroE + shikimate <br /> | + | **[[3doo]] – SeAroE + shikimate <br /> |
| - | [[3pgj]] – VcAroE + shikimate <br /> | + | **[[3pgj]] – VcAroE + shikimate <br /> |
| - | [[3phh]] – HpAroE + shikimate <br /> | + | **[[3phh]] – HpAroE + shikimate <br /> |
| - | [[4fos]], [[4fq8]], [[4fr5]], [[4fsh]] – HpAroE (mutant) + shikimate <br /> | + | **[[4fos]], [[4fq8]], [[4fr5]], [[4fsh]] – HpAroE (mutant) + shikimate <br /> |
| - | [[3phj]] – HpAroE + 3-dihydroshikimate <br /> | + | **[[3phj]] – HpAroE + 3-dihydroshikimate <br /> |
| - | + | *Shikimate dehydrogenase complex with NADP and shikimate | |
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| + | **[[2ev9]] – TtAroE + shikimate + NADP <br /> | ||
| + | **[[2hk9]] – AaAroE + shikimate + NADP <br /> | ||
| + | **[[3sef]] – VcAroE + shikimate + NADP <br /> | ||
| + | **[[3tnl]] – LmAroE + shikimate + NAD <br /> | ||
| + | **[[3phi]] – HpAroE + shikimate + NADP <br /> | ||
| + | **[[3jyp]] - CgAroE + quinate + NAD <br /> | ||
| + | **[[3jyq]] - CgAroE + shikimate + NAD <br /> | ||
| + | }} | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:12, 10 December 2014
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.
3D Structures of shikimate dehydrogenase
Updated on 10-December-2014
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Sohail Jooma
