Biochemical characterization of the very long-chain fatty acid elongase ELOVL7

Tatsuro Naganuma; Yuichiro Sato; Takayuki Sassa; Yusuke Ohno; Akio Kihara

doi:10.1016/j.febslet.2011.09.024

Biochemical characterization of the very long-chain fatty acid elongase ELOVL7

Tatsuro Naganuma, Yuichiro Sato, Takayuki Sassa, Yusuke Ohno, Akio Kihara

Research output: Contribution to journal › Article › peer-review

73 Citations (Scopus)

Abstract

Very long-chain fatty acids (VLCFAs) have a variety of physiological functions and are related to numerous disorders. The key step of VLCFA elongation is catalyzed by members of the elongase family, ELOVLs. Mammals have seven ELOVLs (ELOVL1-7), yet none of them has been purified and analyzed. In the presented study we purified ELOVL7 and measured its activity by reconstituting it into proteoliposomes. Purified ELOVL7 exhibited high activity toward acyl-CoAs with C18 carbon chain length. The calculated K _m values toward C18:3(n-3)-CoA and malonyl-CoA were both in the μM range. We also found that progression of the VLCFA cycle enhances ELOVL7 activity.

Original language	English
Pages (from-to)	3337-3341
Number of pages	5
Journal	FEBS Letters
Volume	585
Issue number	20
DOIs	https://doi.org/10.1016/j.febslet.2011.09.024
Publication status	Published - 2011 Oct 20
Externally published	Yes

Keywords

ELOVL
Elongase
Lipid
Membrane
Very long-chain fatty acid

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2011.09.024

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title = "Biochemical characterization of the very long-chain fatty acid elongase ELOVL7",

abstract = "Very long-chain fatty acids (VLCFAs) have a variety of physiological functions and are related to numerous disorders. The key step of VLCFA elongation is catalyzed by members of the elongase family, ELOVLs. Mammals have seven ELOVLs (ELOVL1-7), yet none of them has been purified and analyzed. In the presented study we purified ELOVL7 and measured its activity by reconstituting it into proteoliposomes. Purified ELOVL7 exhibited high activity toward acyl-CoAs with C18 carbon chain length. The calculated K m values toward C18:3(n-3)-CoA and malonyl-CoA were both in the μM range. We also found that progression of the VLCFA cycle enhances ELOVL7 activity.",

keywords = "ELOVL, Elongase, Lipid, Membrane, Very long-chain fatty acid",

author = "Tatsuro Naganuma and Yuichiro Sato and Takayuki Sassa and Yusuke Ohno and Akio Kihara",

note = "Funding Information: We are grateful to Dr. E.A. Sweeney for scientific editing of the manuscript. This work was supported by a Grant-in-Aid for Scientific Research (B) ( 23370057 ) from the Japan Society for the Promotion of Science (JSPS) .",

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doi = "10.1016/j.febslet.2011.09.024",

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T1 - Biochemical characterization of the very long-chain fatty acid elongase ELOVL7

AU - Naganuma, Tatsuro

AU - Sato, Yuichiro

AU - Sassa, Takayuki

AU - Ohno, Yusuke

AU - Kihara, Akio

N1 - Funding Information: We are grateful to Dr. E.A. Sweeney for scientific editing of the manuscript. This work was supported by a Grant-in-Aid for Scientific Research (B) ( 23370057 ) from the Japan Society for the Promotion of Science (JSPS) .

PY - 2011/10/20

Y1 - 2011/10/20

N2 - Very long-chain fatty acids (VLCFAs) have a variety of physiological functions and are related to numerous disorders. The key step of VLCFA elongation is catalyzed by members of the elongase family, ELOVLs. Mammals have seven ELOVLs (ELOVL1-7), yet none of them has been purified and analyzed. In the presented study we purified ELOVL7 and measured its activity by reconstituting it into proteoliposomes. Purified ELOVL7 exhibited high activity toward acyl-CoAs with C18 carbon chain length. The calculated K m values toward C18:3(n-3)-CoA and malonyl-CoA were both in the μM range. We also found that progression of the VLCFA cycle enhances ELOVL7 activity.

AB - Very long-chain fatty acids (VLCFAs) have a variety of physiological functions and are related to numerous disorders. The key step of VLCFA elongation is catalyzed by members of the elongase family, ELOVLs. Mammals have seven ELOVLs (ELOVL1-7), yet none of them has been purified and analyzed. In the presented study we purified ELOVL7 and measured its activity by reconstituting it into proteoliposomes. Purified ELOVL7 exhibited high activity toward acyl-CoAs with C18 carbon chain length. The calculated K m values toward C18:3(n-3)-CoA and malonyl-CoA were both in the μM range. We also found that progression of the VLCFA cycle enhances ELOVL7 activity.

KW - ELOVL

KW - Elongase

KW - Lipid

KW - Membrane

KW - Very long-chain fatty acid

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JO - FEBS Letters

JF - FEBS Letters

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ER -

Biochemical characterization of the very long-chain fatty acid elongase ELOVL7

Abstract

Keywords

ASJC Scopus subject areas

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