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4qgk

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Revision as of 07:52, 30 July 2014

Structure of the Human Sjogren Larsson Syndrome enzyme fatty aldehyde dehydrogenase (FALDH)

Structural highlights

4qgk is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Aldehyde dehydrogenase (NAD(+)), with EC number 1.2.1.3
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[AL3A2_HUMAN] Sjogren-Larsson syndrome. The disease is caused by mutations affecting the gene represented in this entry.^[1] ^[2] ^[3] ^[4] ^[5]

Function

[AL3A2_HUMAN] Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid.^[6]

References

↑ De Laurenzi V, Rogers GR, Hamrock DJ, Marekov LN, Steinert PM, Compton JG, Markova N, Rizzo WB. Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. Nat Genet. 1996 Jan;12(1):52-7. PMID:8528251 doi:http://dx.doi.org/10.1038/ng0196-52
↑ Sillen A, Jagell S, Wadelius C. A missense mutation in the FALDH gene identified in Sjogren-Larsson syndrome patients originating from the northern part of Sweden. Hum Genet. 1997 Aug;100(2):201-3. PMID:9254849
↑ Sillen A, Anton-Lamprecht I, Braun-Quentin C, Kraus CS, Sayli BS, Ayuso C, Jagell S, Kuster W, Wadelius C. Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjogren-Larsson syndrome. Hum Mutat. 1998;12(6):377-84. PMID:9829906 doi:<377::AID-HUMU3>3.0.CO;2-I http://dx.doi.org/10.1002/(SICI)1098-1004(1998)12:6<377::AID-HUMU3>3.0.CO;2-I
↑ Rizzo WB, Carney G, Lin Z. The molecular basis of Sjogren-Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene. Am J Hum Genet. 1999 Dec;65(6):1547-60. PMID:10577908 doi:http://dx.doi.org/S0002-9297(07)63574-5
↑ Aoki N, Suzuki H, Ito K, Ito M. A novel point mutation of the FALDH gene in a Japanese family with Sjogren-Larsson syndrome. J Invest Dermatol. 2000 May;114(5):1065-6. PMID:10792573 doi:http://dx.doi.org/10.1046/j.1523-1747.2000.00960-5.x
↑ Nakahara K, Ohkuni A, Kitamura T, Abe K, Naganuma T, Ohno Y, Zoeller RA, Kihara A. The Sjogren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway. Mol Cell. 2012 May 25;46(4):461-71. doi: 10.1016/j.molcel.2012.04.033. PMID:22633490 doi:http://dx.doi.org/10.1016/j.molcel.2012.04.033

1 Structural highlights
2 Disease
3 Function
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Structure of the Human Sjogren Larsson Syndrome enzyme fatty aldehyde dehydrogenase (FALDH)==
+<StructureSection load='4qgk' size='340' side='right' caption='[[4qgk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-The entry 4qgk is ON HOLD
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4qgk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QGK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QGK FirstGlance]. <br>
-Authors: Zander, U., Keller, M., Marquez J.A.
+</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(+)) Aldehyde dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.3 1.2.1.3] </span></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qgk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qgk RCSB], [http://www.ebi.ac.uk/pdbsum/4qgk PDBsum]</span></td></tr>
-Description: Structure of the Human Sjogren Larsson Syndrome enzyme fatty aldehyde dehydrogenase (FALDH)
+<table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/AL3A2_HUMAN AL3A2_HUMAN]] Sjogren-Larsson syndrome. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:8528251</ref> <ref>PMID:9254849</ref> <ref>PMID:9829906</ref> <ref>PMID:10577908</ref> <ref>PMID:10792573</ref>
+== Function ==
+[[http://www.uniprot.org/uniprot/AL3A2_HUMAN AL3A2_HUMAN]] Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid.<ref>PMID:22633490</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Keller, M.]]
+[[Category: Marquez, J A.]]
+[[Category: Zander, U.]]
+[[Category: Aldehyde dehydrogenase]]
+[[Category: Fatty aldehyde dehydrogenase]]
+[[Category: Oxidoreductase]]
+[[Category: Sjogren larsson syndrome]]

4qgk

From Proteopedia

Revision as of 07:52, 30 July 2014

Structure of the Human Sjogren Larsson Syndrome enzyme fatty aldehyde dehydrogenase (FALDH)

Structural highlights

Disease

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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