4d5g: Difference between revisions
New page: '''Unreleased structure''' The entry 4d5g is ON HOLD Authors: Loschonsky, S., Wacker, T., Waltzer, S., Giovannini, P.P., McLeish, M.J., Andrade, S.L.A., Mueller, M. Description: Struct... |
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==Structure of recombinant CDH-H28AN484A== | |||
<StructureSection load='4d5g' size='340' side='right'caption='[[4d5g]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4d5g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azoarcus_olearius Azoarcus olearius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D5G FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4d5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d5g OCA], [https://pdbe.org/4d5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d5g RCSB], [https://www.ebi.ac.uk/pdbsum/4d5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d5g ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CHDH_AZOSP CHDH_AZOSP] Catalyzes the ring-opening cleavage of the alicyclic alcohol cyclohexane-1,2-dione.[REFERENCE:1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ThDP-dependent cyclohexane-1,2-dione hydrolase (CDH) catalyzes the CC bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin condensation between benzaldehyde and pyruvate. One of the two reactivities of CDH was selectively knocked down by mutation experiments. CDH-H28A is much less able to catalyze the CC bond formation, while the ability for CC bond cleavage is still intact. The double variant CDH-H28A/N484A shows the opposite behavior and catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol. Several acyloins of tertiary alcohols are formed with 54-94 % enantiomeric excess. In addition to pyruvate, methyl pyruvate and butane-2,3-dione are alternative donor substrates for CC bond formation. Thus, the very rare aldehyde-ketone cross-benzoin reaction has been solved by design of an enzyme variant. | |||
Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligation.,Loschonsky S, Wacker T, Waltzer S, Giovannini PP, McLeish MJ, Andrade SL, Muller M Angew Chem Int Ed Engl. 2014 Dec 22;53(52):14402-6. doi: 10.1002/anie.201408287. , Epub 2014 Nov 7. PMID:25382418<ref>PMID:25382418</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4d5g" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Azoarcus olearius]] | |||
[[Category: Large Structures]] | |||
[[Category: Andrade SLA]] | |||
[[Category: Giovannini PP]] | |||
[[Category: Loschonsky S]] | |||
[[Category: McLeish MJ]] | |||
[[Category: Mueller M]] | |||
[[Category: Wacker T]] | |||
[[Category: Waltzer S]] | |||
Latest revision as of 14:17, 9 May 2024
Structure of recombinant CDH-H28AN484AStructure of recombinant CDH-H28AN484A
Structural highlights
FunctionCHDH_AZOSP Catalyzes the ring-opening cleavage of the alicyclic alcohol cyclohexane-1,2-dione.[REFERENCE:1] Publication Abstract from PubMedThDP-dependent cyclohexane-1,2-dione hydrolase (CDH) catalyzes the CC bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin condensation between benzaldehyde and pyruvate. One of the two reactivities of CDH was selectively knocked down by mutation experiments. CDH-H28A is much less able to catalyze the CC bond formation, while the ability for CC bond cleavage is still intact. The double variant CDH-H28A/N484A shows the opposite behavior and catalyzes the addition of pyruvate to cyclohexane-1,2-dione, resulting in the formation of a tertiary alcohol. Several acyloins of tertiary alcohols are formed with 54-94 % enantiomeric excess. In addition to pyruvate, methyl pyruvate and butane-2,3-dione are alternative donor substrates for CC bond formation. Thus, the very rare aldehyde-ketone cross-benzoin reaction has been solved by design of an enzyme variant. Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligation.,Loschonsky S, Wacker T, Waltzer S, Giovannini PP, McLeish MJ, Andrade SL, Muller M Angew Chem Int Ed Engl. 2014 Dec 22;53(52):14402-6. doi: 10.1002/anie.201408287. , Epub 2014 Nov 7. PMID:25382418[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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