4kvq
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal Structure of Prochlorococcus marinus aldehyde-deformylating oxygenase wild type with palmitic acid bound== | |
| - | + | <StructureSection load='4kvq' size='340' side='right' caption='[[4kvq]], [[Resolution|resolution]] 1.84Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4kvq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Prochlorococcus_marinus_str._mit_9313 Prochlorococcus marinus str. mit 9313]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KVQ FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oc5|2oc5]], [[4kvr|4kvr]], [[4kvs|4kvs]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT_1231 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=74547 Prochlorococcus marinus str. MIT 9313])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Octadecanal_decarbonylase Octadecanal decarbonylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.5 4.1.99.5] </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=4kvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kvq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kvq RCSB], [http://www.ebi.ac.uk/pdbsum/4kvq PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/ALDEC_PROMM ALDEC_PROMM]] Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.<ref>PMID:20671186</ref> | [[http://www.uniprot.org/uniprot/ALDEC_PROMM ALDEC_PROMM]] Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.<ref>PMID:20671186</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Biocatalytic propane production: structure-based engineering of aldehyde-deformylating oxygenase improves specificity for short- and medium-chain-length aldehydes and enhances the propane generation in whole-cell biotransformations. This presents new opportunities for developing biocatalytic modules for the production of volatile "drop-in" biofuels. | ||
| - | + | Production of Propane and Other Short-Chain Alkanes by Structure-Based Engineering of Ligand Specificity in Aldehyde-Deformylating Oxygenase.,Khara B, Menon N, Levy C, Mansell D, Das D, Marsh EN, Leys D, Scrutton NS Chembiochem. 2013 Jun 11. doi: 10.1002/cbic.201300307. PMID:23757044<ref>PMID:23757044</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Octadecanal decarbonylase]] | [[Category: Octadecanal decarbonylase]] | ||
[[Category: Prochlorococcus marinus str. mit 9313]] | [[Category: Prochlorococcus marinus str. mit 9313]] | ||
| - | [[Category: Das, D | + | [[Category: Das, D]] |
| - | [[Category: Khara, B | + | [[Category: Khara, B]] |
| - | [[Category: Levy, C W | + | [[Category: Levy, C W]] |
| - | [[Category: Leys, D | + | [[Category: Leys, D]] |
| - | [[Category: Mansell, D | + | [[Category: Mansell, D]] |
| - | [[Category: Marsh, E N.G | + | [[Category: Marsh, E N.G]] |
| - | [[Category: Menon, N | + | [[Category: Menon, N]] |
| - | [[Category: Scrutton, N S | + | [[Category: Scrutton, N S]] |
[[Category: Aldehyde-deformylating oxygenase]] | [[Category: Aldehyde-deformylating oxygenase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Propane production]] | [[Category: Propane production]] | ||
Revision as of 16:38, 25 December 2014
Crystal Structure of Prochlorococcus marinus aldehyde-deformylating oxygenase wild type with palmitic acid bound
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