6hs9: Difference between revisions
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The | ==The crystal structure of type II Dehydroquinase from Butyrivibrio crossotus DSM 2876== | ||
<StructureSection load='6hs9' size='340' side='right'caption='[[6hs9]], [[Resolution|resolution]] 1.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6hs9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HS9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HS9 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3DS:(4S,5R)-4,5-DIHYDROXY-3-OXOCYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>3DS</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hs9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hs9 OCA], [http://pdbe.org/6hs9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hs9 RCSB], [http://www.ebi.ac.uk/pdbsum/6hs9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hs9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/D4S0D1_9FIRM D4S0D1_9FIRM]] Catalyzes a trans-dehydration via an enolate intermediate.[HAMAP-Rule:MF_00169] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
3-Dehydroquinate dehydratase (DHQase) catalyzes the conversion of 3-dehydroquinic acid to 3-dehydroshikimic acid of the shikimate pathway. In this study, 3180 prokaryotic genomes were examined and 459 DHQase sequences were retrieved. Based on sequence analysis and their original hosts, 38 DHQase genes were selected for chemical synthesis. The selected DHQases were translated into new DNA sequences according to the genetic codon usage bias by both Escherichia coli and Corynebacterium glutamicum. The new DNA sequences were customized for synthetic biological applications by adding Biobrick adapters at both ends and by removal of any related restriction endonuclease sites. The customized DHQase genes were successfully expressed in E. coli, and functional DHQases were obtained. Kinetic parameters of Km, kcat, and Vmax of DHQases were determined with a newly established high-throughput method for DHQase activity assay. Results showed that DHQases possessed broad strength of substrate affinities and catalytic capacities. In addition to the DHQase kinetic diversities, this study generated a DHQase library with known catalytic constants that could be applied to design artificial modules of shikimate pathway for metabolic engineering and synthetic biology. | |||
Unraveling the kinetic diversity of microbial 3-dehydroquinate dehydratases of shikimate pathway.,Liu C, Liu YM, Sun QL, Jiang CY, Liu SJ AMB Express. 2015 Feb 1;5:7. doi: 10.1186/s13568-014-0087-y. eCollection 2015. PMID:25852984<ref>PMID:25852984</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6hs9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: 3-dehydroquinate dehydratase]] | |||
[[Category: Large Structures]] | |||
[[Category: Lapthorn, A J]] | |||
[[Category: Roszak, A W]] | |||
[[Category: Biosynthetic protein]] | |||
[[Category: Dehydratase]] | |||
[[Category: Shikimate pathway]] | |||
Revision as of 09:44, 23 October 2019
The crystal structure of type II Dehydroquinase from Butyrivibrio crossotus DSM 2876The crystal structure of type II Dehydroquinase from Butyrivibrio crossotus DSM 2876
Structural highlights
Function[D4S0D1_9FIRM] Catalyzes a trans-dehydration via an enolate intermediate.[HAMAP-Rule:MF_00169] Publication Abstract from PubMed3-Dehydroquinate dehydratase (DHQase) catalyzes the conversion of 3-dehydroquinic acid to 3-dehydroshikimic acid of the shikimate pathway. In this study, 3180 prokaryotic genomes were examined and 459 DHQase sequences were retrieved. Based on sequence analysis and their original hosts, 38 DHQase genes were selected for chemical synthesis. The selected DHQases were translated into new DNA sequences according to the genetic codon usage bias by both Escherichia coli and Corynebacterium glutamicum. The new DNA sequences were customized for synthetic biological applications by adding Biobrick adapters at both ends and by removal of any related restriction endonuclease sites. The customized DHQase genes were successfully expressed in E. coli, and functional DHQases were obtained. Kinetic parameters of Km, kcat, and Vmax of DHQases were determined with a newly established high-throughput method for DHQase activity assay. Results showed that DHQases possessed broad strength of substrate affinities and catalytic capacities. In addition to the DHQase kinetic diversities, this study generated a DHQase library with known catalytic constants that could be applied to design artificial modules of shikimate pathway for metabolic engineering and synthetic biology. Unraveling the kinetic diversity of microbial 3-dehydroquinate dehydratases of shikimate pathway.,Liu C, Liu YM, Sun QL, Jiang CY, Liu SJ AMB Express. 2015 Feb 1;5:7. doi: 10.1186/s13568-014-0087-y. eCollection 2015. PMID:25852984[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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