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4z5s

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Revision as of 07:40, 10 May 2023

Crystal structure of apo-form of aldehyde deformylating oxygenase from Synechocystis sp.PCC 6803

Structural highlights

4z5s is a 1 chain structure with sequence from Synechocystis sp. PCC 6803 substr. Kazusa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALDEC_SYNY3 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.[HAMAP-Rule:MF_00931]^[1]

Publication Abstract from PubMed

BACKGROUND: Aldehyde-deformylating oxygenase (ADO) is a key enzyme involved in the biosynthetic pathway of fatty alk(a/e)nes in cyanobacteria. However, cADO (cyanobacterial ADO) showed extreme low activity with the k cat value below 1 min-1, which would limit its application in biofuel production. To identify the activity related key residues of cADO is urgently required. RESULTS: The amino acid residues which might affect cADO activity were identified based on the crystal structures and sequence alignment of cADOs, including the residues close to the di-iron center (Tyr39, Arg62, Gln110, Tyr122, Asp143 of cADO-1593), the protein surface (Trp 178 of cADO-1593), and those involved in two important hydrogen bonds (Gln49, Asn123 of cADO-1593, and Asp49, Asn123 of cADO-sll0208) and in the oligopeptide whose conformation changed in the absence of the di-iron center (Leu146, Asn149, Phe150 of cADO-1593, and Thr146, Leu148, Tyr150 of cADO-sll0208). The variants of cADO-1593 from Synechococcus elongatus PCC7942 and cADO-sll0208 from Synechocystis sp. PCC6803 were constructed, overexpressed, purified and kinetically characterized. The k cat values of L146T, Q49H/N123H/F150Y and W178R of cADO-1593 and L148R of cADO-sll0208 were increased by more than two-fold, whereas that of R62A dropped by 91.1%. N123H, Y39F and D143A of cADO-1593, and Y150F of cADO-sll0208 reduced activities by </= 20%. CONCLUSIONS: Some important amino acids, which exerted some effects on cADO activity, were identified. Several enzyme variants exhibited greatly reduced activity, while the k cat values of several mutants are more than two-fold higher than the wild type. This study presents the report on the relationship between amino acid residues and enzyme activity of cADOs, and the information will provide a guide for enhancement of cADO activity through protein engineering.

Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship.,Wang Q, Bao L, Jia C, Li M, Li JJ, Lu X BMC Biotechnol. 2017 Mar 16;17(1):31. doi: 10.1186/s12896-017-0351-8. PMID:28302170^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schirmer A, Rude MA, Li X, Popova E, del Cardayre SB. Microbial biosynthesis of alkanes. Science. 2010 Jul 30;329(5991):559-62. doi: 10.1126/science.1187936. PMID:20671186 doi:10.1126/science.1187936
↑ Wang Q, Bao L, Jia C, Li M, Li JJ, Lu X. Identification of residues important for the activity of aldehyde-deformylating oxygenase through investigation into the structure-activity relationship. BMC Biotechnol. 2017 Mar 16;17(1):31. doi: 10.1186/s12896-017-0351-8. PMID:28302170 doi:http://dx.doi.org/10.1186/s12896-017-0351-8

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4z5s"

Categories: Large Structures | Synechocystis sp. PCC 6803 substr. Kazusa | Chang W | Jia C | Li M

@@ Line 3: / Line 3: @@
 <StructureSection load='4z5s' size='340' side='right'caption='[[4z5s]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4z5s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z5S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z5S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4z5s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z5S FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sll0208 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</td></tr>
+</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=4z5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z5s OCA], [https://pdbe.org/4z5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z5s RCSB], [https://www.ebi.ac.uk/pdbsum/4z5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z5s ProSAT]</span></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=4z5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z5s OCA], [http://pdbe.org/4z5s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z5s RCSB], [http://www.ebi.ac.uk/pdbsum/4z5s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z5s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ALDEC_SYNY3 ALDEC_SYNY3]] 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.[HAMAP-Rule:MF_00931]<ref>PMID:20671186</ref>
+[https://www.uniprot.org/uniprot/ALDEC_SYNY3 ALDEC_SYNY3] 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.[HAMAP-Rule:MF_00931]<ref>PMID:20671186</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Octadecanal decarbonylase]]
+[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
-[[Category: Syny3]]
+[[Category: Chang W]]
-[[Category: Chang, W]]
+[[Category: Jia C]]
-[[Category: Jia, C]]
+[[Category: Li M]]
-[[Category: Li, M]]
-[[Category: Lyase]]
-[[Category: Oxygenase]]

4z5s

From Proteopedia

Revision as of 07:40, 10 May 2023

Crystal structure of apo-form of aldehyde deformylating oxygenase from Synechocystis sp.PCC 6803

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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