HPLC measurement of testicular long chain acyl-CoA synthetases with different substrate specificities

Lipids ◽  
1986 ◽  
Vol 21 (1) ◽  
pp. 11-16 ◽  
Author(s):  
W. McLean Grogan ◽  
Ellen G. Huth
Keyword(s):  
Substrate Specificities ◽  
Chain Acyl ◽  
Hplc Measurement ◽  
Long Chain

scholarly journals ABC Transporter Subfamily D: Distinct Differences in Behavior between ABCD1–3 and ABCD4 in Subcellular Localization, Function, and Human Disease

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Kosuke Kawaguchi ◽  
Masashi Morita
Keyword(s):  
Abc Transporters ◽  
Critical Role ◽  
Vitamin B ◽  
Long Chain Fatty Acids ◽  
Substrate Specificities ◽  
Related Disease ◽  
Chain Acyl ◽  
Membrane Bound ◽  
Branched Chain ◽  
Long Chain

ATP-binding cassette (ABC) transporters are one of the largest families of membrane-bound proteins and transport a wide variety of substrates across both extra- and intracellular membranes. They play a critical role in maintaining cellular homeostasis. To date, four ABC transporters belonging to subfamily D have been identified. ABCD1–3 and ABCD4 are localized to peroxisomes and lysosomes, respectively. ABCD1 and ABCD2 are involved in the transport of long and very long chain fatty acids (VLCFA) or their CoA-derivatives into peroxisomes with different substrate specificities, while ABCD3 is involved in the transport of branched chain acyl-CoA into peroxisomes. On the other hand, ABCD4 is deduced to take part in the transport of vitamin B12from lysosomes into the cytosol. It is well known that the dysfunction of ABCD1 results in X-linked adrenoleukodystrophy, a severe neurodegenerative disease. Recently, it is reported that ABCD3 and ABCD4 are responsible for hepatosplenomegaly and vitamin B12deficiency, respectively. In this review, the targeting mechanism and physiological functions of the ABCD transporters are summarized along with the related disease.

Impact of the intramitochondrial enzyme organization on fatty acid oxidation

2001 ◽  
Vol 29 (2) ◽  
pp. 279-282 ◽  
Author(s):  
X. Liang ◽  
W. Le ◽  
D. Zhang ◽  
H. Schulz
Keyword(s):  
Acid Oxidation ◽  
Matrix System ◽  
Apparent Absence ◽  
Substrate Specificities ◽  
Chain Acyl ◽  
Membrane Bound ◽  
Enzyme Organization ◽  
Soluble Enzymes ◽  
Oxidation System ◽  
Long Chain

The enzymes of mitochondrial β-oxidation are thought to be organized in at least two functional complexes, a membrane-bound, long-chain-specific β-oxidation system and a matrix system consisting of soluble enzymes with preferences for medium-chain and short-chain substrates. This hypothesis is supported by the observation that the inactivation of long-chain 3-ketoacyl-CoA thiolase by 4-bromotiglic acid (4-bromo-2-methylbut-2-enoic acid) causes the complete inhibition of palmitate β-oxidation even though 3-ketoacyl-CoA thiolase, which acts on 3-ketopalmitoyl-CoA, remains partly active. The observed substrate specificities of long-chain acyl-CoA dehydrogenase (LCAD) and very-long-chain acyl-CoA dehydrogenase prompt the suggestion that LCAD is a functional component of the long-chain-specific β-oxidation system. Altogether, a view is emerging of the organization of β-oxidation enzymes in mitochondria that supports the idea of intermediate channelling and explains the apparent absence of true intermediates of β-oxidation from mitochondria.

scholarly journals Evidence for an essential role of long chain acyl-CoA synthetase in animal cell proliferation

1991 ◽  
Vol 266 (7) ◽  
pp. 4214-4219
Author(s):  
H Tomoda ◽  
K Igarashi ◽  
J C Cyong ◽  
S Omura
Keyword(s):  
Cell Proliferation ◽  
Essential Role ◽  
Animal Cell ◽  
Chain Acyl ◽  
Long Chain

scholarly journals Dietary restriction in the long-chain acyl-CoA dehydrogenase knockout mouse

2021 ◽  
Vol 27 ◽  
pp. 100749
Author(s):  
Eugène F. Diekman ◽  
Michel van Weeghel ◽  
Mayte Suárez-Fariñas ◽  
Carmen Argmann ◽  
Pablo Ranea-Robles ◽  
...  
Keyword(s):  
Dietary Restriction ◽  
Knockout Mouse ◽  
Chain Acyl ◽  
Long Chain
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