8phf: Difference between revisions

Latest revision as of 16:54, 9 July 2025

Cryo-EM structure of human ACAD9-S191A

Structural highlights

8phf is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.6Å
Ligands:	FAD
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ACAD9_HUMAN Acyl-CoA dehydrogenase 9 deficiency. The disease is caused by variants affecting the gene represented in this entry.

Function

ACAD9_HUMAN As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation (PubMed:20816094, PubMed:24158852, PubMed:32320651). This moonlighting protein also has a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs (PubMed:12359260, PubMed:16020546, PubMed:21237683, PubMed:24158852). However, in vivo, it does not seem to play a primary role in fatty acid oxidation (PubMed:20816094, PubMed:24158852). In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein (PubMed:24158852).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

References

↑ Zhang J, Zhang W, Zou D, Chen G, Wan T, Zhang M, Cao X. Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family. Biochem Biophys Res Commun. 2002 Oct 4;297(4):1033-42. PMID:12359260 doi:10.1016/s0006-291x(02)02336-7
↑ Ensenauer R, He M, Willard JM, Goetzman ES, Corydon TJ, Vandahl BB, Mohsen AW, Isaya G, Vockley J. Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids. J Biol Chem. 2005 Sep 16;280(37):32309-16. PMID:16020546 doi:10.1074/jbc.M504460200
↑ Nouws J, Nijtmans L, Houten SM, van den Brand M, Huynen M, Venselaar H, Hoefs S, Gloerich J, Kronick J, Hutchin T, Willems P, Rodenburg R, Wanders R, van den Heuvel L, Smeitink J, Vogel RO. Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I. Cell Metab. 2010 Sep 8;12(3):283-94. PMID:20816094 doi:10.1016/j.cmet.2010.08.002
↑ He M, Pei Z, Mohsen AW, Watkins P, Murdoch G, Van Veldhoven PP, Ensenauer R, Vockley J. Identification and characterization of new long chain acyl-CoA dehydrogenases. Mol Genet Metab. 2011 Apr;102(4):418-29. PMID:21237683 doi:10.1016/j.ymgme.2010.12.005
↑ Nouws J, Te Brinke H, Nijtmans LG, Houten SM. ACAD9, a complex I assembly factor with a moonlighting function in fatty acid oxidation deficiencies. Hum Mol Genet. 2014 Mar 1;23(5):1311-9. PMID:24158852 doi:10.1093/hmg/ddt521
↑ Formosa LE, Muellner-Wong L, Reljic B, Sharpe AJ, Jackson TD, Beilharz TH, Stojanovski D, Lazarou M, Stroud DA, Ryan MT. Dissecting the Roles of Mitochondrial Complex I Intermediate Assembly Complex Factors in the Biogenesis of Complex I. Cell Rep. 2020 Apr 21;31(3):107541. PMID:32320651 doi:10.1016/j.celrep.2020.107541

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OCA

[1] Zhang J, Zhang W, Zou D, Chen G, Wan T, Zhang M, Cao X. Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family. Biochem Biophys Res Commun. 2002 Oct 4;297(4):1033-42. PMID:12359260 doi:10.1016/s0006-291x(02)02336-7

[2] Ensenauer R, He M, Willard JM, Goetzman ES, Corydon TJ, Vandahl BB, Mohsen AW, Isaya G, Vockley J. Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids. J Biol Chem. 2005 Sep 16;280(37):32309-16. PMID:16020546 doi:10.1074/jbc.M504460200

[3] Nouws J, Nijtmans L, Houten SM, van den Brand M, Huynen M, Venselaar H, Hoefs S, Gloerich J, Kronick J, Hutchin T, Willems P, Rodenburg R, Wanders R, van den Heuvel L, Smeitink J, Vogel RO. Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative phosphorylation complex I. Cell Metab. 2010 Sep 8;12(3):283-94. PMID:20816094 doi:10.1016/j.cmet.2010.08.002

[4] He M, Pei Z, Mohsen AW, Watkins P, Murdoch G, Van Veldhoven PP, Ensenauer R, Vockley J. Identification and characterization of new long chain acyl-CoA dehydrogenases. Mol Genet Metab. 2011 Apr;102(4):418-29. PMID:21237683 doi:10.1016/j.ymgme.2010.12.005

[5] Nouws J, Te Brinke H, Nijtmans LG, Houten SM. ACAD9, a complex I assembly factor with a moonlighting function in fatty acid oxidation deficiencies. Hum Mol Genet. 2014 Mar 1;23(5):1311-9. PMID:24158852 doi:10.1093/hmg/ddt521

[6] Formosa LE, Muellner-Wong L, Reljic B, Sharpe AJ, Jackson TD, Beilharz TH, Stojanovski D, Lazarou M, Stroud DA, Ryan MT. Dissecting the Roles of Mitochondrial Complex I Intermediate Assembly Complex Factors in the Biogenesis of Complex I. Cell Rep. 2020 Apr 21;31(3):107541. PMID:32320651 doi:10.1016/j.celrep.2020.107541

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[5]

[6]

@@ Line 11: / Line 11: @@
 [https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] Acyl-CoA dehydrogenase 9 deficiency. The disease is caused by variants affecting the gene represented in this entry.
 == Function ==
-[https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation (PubMed:20816094, PubMed:24158852, PubMed:32320651). This moonlighting protein has also a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs (PubMed:12359260, PubMed:16020546, PubMed:21237683, PubMed:24158852). However, in vivo, it does not seem to play a primary role in fatty acid oxidation (PubMed:20816094, PubMed:24158852). In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein (PubMed:24158852).<ref>PMID:12359260</ref> <ref>PMID:16020546</ref> <ref>PMID:20816094</ref> <ref>PMID:21237683</ref> <ref>PMID:24158852</ref> <ref>PMID:32320651</ref>
+[https://www.uniprot.org/uniprot/ACAD9_HUMAN ACAD9_HUMAN] As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation (PubMed:20816094, PubMed:24158852, PubMed:32320651). This moonlighting protein also has a dehydrogenase activity toward a broad range of substrates with greater specificity for long-chain unsaturated acyl-CoAs (PubMed:12359260, PubMed:16020546, PubMed:21237683, PubMed:24158852). However, in vivo, it does not seem to play a primary role in fatty acid oxidation (PubMed:20816094, PubMed:24158852). In addition, the function in complex I assembly is independent of the dehydrogenase activity of the protein (PubMed:24158852).<ref>PMID:12359260</ref> <ref>PMID:16020546</ref> <ref>PMID:20816094</ref> <ref>PMID:21237683</ref> <ref>PMID:24158852</ref> <ref>PMID:32320651</ref>
 == References ==
 <references/>

8phf: Difference between revisions

Latest revision as of 16:54, 9 July 2025

Cryo-EM structure of human ACAD9-S191A

Structural highlights

Disease

Function

References

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