Fatty Acyl-CoA Synthetases

Paul A Watkins

doi:10.1016/B978-0-12-378630-2.00100-6

Fatty Acyl-CoA Synthetases

Paul A Watkins

Kennedy Krieger Institute

Research output: Chapter in Book/Report/Conference proceeding › Chapter

1 Scopus citations

Abstract

Fatty acyl-CoA synthetase (ACS) catalyzes the adenosine triphosphate dependent formation of a thioester bond between a fatty acid and coenzyme A. This fundamental reaction allows the fatty acid to be degraded for energy production, incorporated into complex lipids, or participate in other metabolic pathways. Different ACS proteins exhibit preferences for fatty acid substrates of varying chain lengths, ranging from 2 to more than 30 carbon atoms. ACSs also differ in their tissue and cellular expression patterns, and subcellular locations. Humans and mice have 26 different ACSs. Emerging evidence suggests that each may perform a unique function essential for the maintenance of normal lipid homeostasis.

Original language	English (US)
Title of host publication	Encyclopedia of Biological Chemistry
Subtitle of host publication	Second Edition
Publisher	Elsevier Inc.
Pages	290-295
Number of pages	6
ISBN (Electronic)	9780123786319
ISBN (Print)	9780123786302
DOIs	https://doi.org/10.1016/B978-0-12-378630-2.00100-6
State	Published - Feb 15 2013

Keywords

Activated fatty acid
Acyl-CoA
Acyl-CoA synthetase
Bubblegum acyl-CoA synthetase
Coenzyme A
Fatty acid
Fatty acid activation
Fatty acid transport protein
Fatty acyl-CoA synthetase
Long-chain acyl-CoA synthetase
Medium-chain acyl-CoA synthetase
Motif
Short-chain acyl-CoA synthetase
Thioester bond
Very long chain acyl-CoA synthetase

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

Access to Document

10.1016/B978-0-12-378630-2.00100-6

Cite this

@inbook{c01a12a6636e4262a78884394f69f292,

title = "Fatty Acyl-CoA Synthetases",

abstract = "Fatty acyl-CoA synthetase (ACS) catalyzes the adenosine triphosphate dependent formation of a thioester bond between a fatty acid and coenzyme A. This fundamental reaction allows the fatty acid to be degraded for energy production, incorporated into complex lipids, or participate in other metabolic pathways. Different ACS proteins exhibit preferences for fatty acid substrates of varying chain lengths, ranging from 2 to more than 30 carbon atoms. ACSs also differ in their tissue and cellular expression patterns, and subcellular locations. Humans and mice have 26 different ACSs. Emerging evidence suggests that each may perform a unique function essential for the maintenance of normal lipid homeostasis.",

keywords = "Activated fatty acid, Acyl-CoA, Acyl-CoA synthetase, Bubblegum acyl-CoA synthetase, Coenzyme A, Fatty acid, Fatty acid activation, Fatty acid transport protein, Fatty acyl-CoA synthetase, Long-chain acyl-CoA synthetase, Medium-chain acyl-CoA synthetase, Motif, Short-chain acyl-CoA synthetase, Thioester bond, Very long chain acyl-CoA synthetase",

author = "Watkins, {Paul A}",

year = "2013",

month = feb,

day = "15",

doi = "10.1016/B978-0-12-378630-2.00100-6",

language = "English (US)",

isbn = "9780123786302",

pages = "290--295",

booktitle = "Encyclopedia of Biological Chemistry",

publisher = "Elsevier Inc.",

}

TY - CHAP

T1 - Fatty Acyl-CoA Synthetases

AU - Watkins, Paul A

PY - 2013/2/15

Y1 - 2013/2/15

N2 - Fatty acyl-CoA synthetase (ACS) catalyzes the adenosine triphosphate dependent formation of a thioester bond between a fatty acid and coenzyme A. This fundamental reaction allows the fatty acid to be degraded for energy production, incorporated into complex lipids, or participate in other metabolic pathways. Different ACS proteins exhibit preferences for fatty acid substrates of varying chain lengths, ranging from 2 to more than 30 carbon atoms. ACSs also differ in their tissue and cellular expression patterns, and subcellular locations. Humans and mice have 26 different ACSs. Emerging evidence suggests that each may perform a unique function essential for the maintenance of normal lipid homeostasis.

AB - Fatty acyl-CoA synthetase (ACS) catalyzes the adenosine triphosphate dependent formation of a thioester bond between a fatty acid and coenzyme A. This fundamental reaction allows the fatty acid to be degraded for energy production, incorporated into complex lipids, or participate in other metabolic pathways. Different ACS proteins exhibit preferences for fatty acid substrates of varying chain lengths, ranging from 2 to more than 30 carbon atoms. ACSs also differ in their tissue and cellular expression patterns, and subcellular locations. Humans and mice have 26 different ACSs. Emerging evidence suggests that each may perform a unique function essential for the maintenance of normal lipid homeostasis.

KW - Activated fatty acid

KW - Acyl-CoA

KW - Acyl-CoA synthetase

KW - Bubblegum acyl-CoA synthetase

KW - Coenzyme A

KW - Fatty acid

KW - Fatty acid activation

KW - Fatty acid transport protein

KW - Fatty acyl-CoA synthetase

KW - Long-chain acyl-CoA synthetase

KW - Medium-chain acyl-CoA synthetase

KW - Motif

KW - Short-chain acyl-CoA synthetase

KW - Thioester bond

KW - Very long chain acyl-CoA synthetase

UR - http://www.scopus.com/inward/record.url?scp=85042800881&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85042800881&partnerID=8YFLogxK

U2 - 10.1016/B978-0-12-378630-2.00100-6

DO - 10.1016/B978-0-12-378630-2.00100-6

M3 - Chapter

AN - SCOPUS:85042800881

SN - 9780123786302

SP - 290

EP - 295

BT - Encyclopedia of Biological Chemistry

PB - Elsevier Inc.

ER -

Fatty Acyl-CoA Synthetases

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this