5ucw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:25, 4 October 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Cytochrome P411 P-4 A82L A78V F263L amination catalyst==
==Cytochrome P411 P-4 A82L A78V F263L amination catalyst==
-
<StructureSection load='5ucw' size='340' side='right' caption='[[5ucw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+
<StructureSection load='5ucw' size='340' side='right'caption='[[5ucw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5ucw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UCW FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5ucw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UCW FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.7&#8491;</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=5ucw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ucw OCA], [http://pdbe.org/5ucw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ucw RCSB], [http://www.ebi.ac.uk/pdbsum/5ucw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ucw ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=5ucw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ucw OCA], [https://pdbe.org/5ucw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ucw RCSB], [https://www.ebi.ac.uk/pdbsum/5ucw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ucw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/F2Q7T0_BACME F2Q7T0_BACME]] Functions as a fatty acid monooxygenase.[PIRNR:PIRNR000209]
+
[https://www.uniprot.org/uniprot/CPXB_PRIM2 CPXB_PRIM2] Functions as a fatty acid monooxygenase (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028). Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637). Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460).<ref>PMID:11695892</ref> <ref>PMID:14653735</ref> <ref>PMID:16403573</ref> <ref>PMID:16566047</ref> <ref>PMID:17077084</ref> <ref>PMID:1727637</ref> <ref>PMID:17868686</ref> <ref>PMID:18004886</ref> <ref>PMID:18020460</ref> <ref>PMID:18298086</ref> <ref>PMID:18619466</ref> <ref>PMID:18721129</ref> <ref>PMID:19492389</ref> <ref>PMID:20180779</ref> <ref>PMID:21110374</ref> <ref>PMID:21875028</ref> <ref>PMID:3106359</ref> <ref>PMID:7578081</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
C-H bonds are ubiquitous structural units of organic molecules. Although these bonds are generally considered to be chemically inert, the recent emergence of methods for C-H functionalization promises to transform the way synthetic chemistry is performed. The intermolecular amination of C-H bonds represents a particularly desirable and challenging transformation for which no efficient, highly selective, and renewable catalysts exist. Here we report the directed evolution of an iron-containing enzymatic catalyst-based on a cytochrome P450 monooxygenase-for the highly enantioselective intermolecular amination of benzylic C-H bonds. The biocatalyst is capable of up to 1,300 turnovers, exhibits excellent enantioselectivities, and provides access to valuable benzylic amines. Iron complexes are generally poor catalysts for C-H amination: in this catalyst, the enzyme's protein framework confers activity on an otherwise unreactive iron-haem cofactor.
 +
 
 +
Enantioselective, intermolecular benzylic C-H amination catalysed by an engineered iron-haem enzyme.,Prier CK, Zhang RK, Buller AR, Brinkmann-Chen S, Arnold FH Nat Chem. 2017 Jul;9(7):629-634. doi: 10.1038/nchem.2783. Epub 2017 May 29. PMID:28644476<ref>PMID:28644476</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5ucw" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
 +
*[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 14581]]
+
[[Category: Large Structures]]
-
[[Category: Arnold, F H]]
+
[[Category: Priestia megaterium]]
-
[[Category: Buller, A R]]
+
[[Category: Arnold FH]]
-
[[Category: Zhang, R K]]
+
[[Category: Buller AR]]
-
[[Category: C-h functionalization]]
+
[[Category: Zhang RK]]
-
[[Category: Engineered]]
+
-
[[Category: Nitrene transfer]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: P411cha]]
+

Current revision

Cytochrome P411 P-4 A82L A78V F263L amination catalyst

PDB ID 5ucw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ucw"
Personal tools