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| | <StructureSection load='4tmb' size='340' side='right'caption='[[4tmb]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4tmb' size='340' side='right'caption='[[4tmb]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tmb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_712 Cbs 712]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TMB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TMB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tmb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_marxianus Kluyveromyces marxianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TMB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tmc|4tmc]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oye ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4911 CBS 712])</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=4tmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tmb OCA], [https://pdbe.org/4tmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tmb RCSB], [https://www.ebi.ac.uk/pdbsum/4tmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tmb ProSAT]</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=4tmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tmb OCA], [http://pdbe.org/4tmb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tmb RCSB], [http://www.ebi.ac.uk/pdbsum/4tmb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tmb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6I7B7_KLUMA Q6I7B7_KLUMA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 712]] | + | [[Category: Kluyveromyces marxianus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Horita, S]] | + | [[Category: Horita S]] |
| - | [[Category: Kataoka, M]] | + | [[Category: Kataoka M]] |
| - | [[Category: Kitamura, N]] | + | [[Category: Kitamura N]] |
| - | [[Category: Miyakawa, T]] | + | [[Category: Miyakawa T]] |
| - | [[Category: Nagata, K]] | + | [[Category: Nagata K]] |
| - | [[Category: Nakagawa, T]] | + | [[Category: Nakagawa T]] |
| - | [[Category: Ohtsuka, J]] | + | [[Category: Ohtsuka J]] |
| - | [[Category: Shimizu, S]] | + | [[Category: Shimizu S]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Tanokura M]] |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Tim barrel motif]]
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| Structural highlights
Function
Q6I7B7_KLUMA
Publication Abstract from PubMed
(4R,6R)-Actinol can be stereo-selectively synthesized from ketoisophorone by a two-step conversion using a mixture of two enzymes: Candida macedoniensis old yellow enzyme (CmOYE) and Corynebacterium aquaticum (6R)-levodione reductase. However, (4S)-phorenol, an intermediate, accumulates because of the limited substrate range of CmOYE. To address this issue, we solved crystal structures of CmOYE in the presence and absence of a substrate analogue p-HBA, and introduced point mutations into the substrate-recognition loop. The most effective mutant (P295G) showed two- and 12-fold higher catalytic activities toward ketoisophorone and (4S)-phorenol, respectively, than the wild-type, and improved the yield of the two-step conversion from 67.2 to 90.1 %. Our results demonstrate that the substrate range of an enzyme can be changed by introducing mutation(s) into a substrate-recognition loop. This method can be applied to the development of other favorable OYEs with different substrate preferences.
An Engineered Old Yellow Enzyme that Enables Efficient Synthesis of (4R,6R)-Actinol in a One-Pot Reduction System.,Horita S, Kataoka M, Kitamura N, Nakagawa T, Miyakawa T, Ohtsuka J, Nagata K, Shimizu S, Tanokura M Chembiochem. 2015 Feb 9;16(3):440-5. doi: 10.1002/cbic.201402555. Epub 2015 Jan, 14. PMID:25639703[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Horita S, Kataoka M, Kitamura N, Nakagawa T, Miyakawa T, Ohtsuka J, Nagata K, Shimizu S, Tanokura M. An Engineered Old Yellow Enzyme that Enables Efficient Synthesis of (4R,6R)-Actinol in a One-Pot Reduction System. Chembiochem. 2015 Feb 9;16(3):440-5. doi: 10.1002/cbic.201402555. Epub 2015 Jan, 14. PMID:25639703 doi:http://dx.doi.org/10.1002/cbic.201402555
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