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.

Requirement of branched chain and long chain fatty acids in C. elegans

2009 ◽  
Vol 160 ◽  
pp. S6
Author(s):  
Teymuras V. Kurzchalia ◽  
Eugeni V. Entchev ◽  
Dominik Schwudke ◽  
Vyacheslav Zagoriy ◽  
Vitali Matyash ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Long Chain Fatty Acids ◽  
C Elegans ◽  
Branched Chain ◽  
Long Chain ◽  
Chain Fatty Acids

scholarly journals Escherichia coli YigI is a conserved γ-proteobacterial acyl-CoA thioesterase permitting metabolism of unusual fatty acid substrates

2022 ◽  
Author(s):  
Michael Schmidt ◽  
Theresa Proctor ◽  
Rucheng Diao ◽  
Peter L. Freddolino
Keyword(s):  
Escherichia Coli ◽  
Critical Role ◽  
Acidic Environment ◽  
Unusual Fatty Acid ◽  
E Coli ◽  
Chain Acyl ◽  
Domains Of Life ◽  
Shed Light ◽  
Long Chain

Thioesterases play a critical role in metabolism, membrane biosynthesis, and overall homeostasis for all domains of life. In this present study, we characterize a putative thioesterase from Escherichia coli MG1655 and define its role as a cytosolic enzyme. Building on structure-guided functional predictions, we show that YigI is a medium- to -long chain acyl-CoA thioesterase that is involved in the degradation of conjugated linoleic acid (CLA) in vivo, showing overlapping specificity with two previously defined E. coli thioesterases TesB and FadM. We then bioinformatically identify the regulatory relationships that induce YigI expression, which include: an acidic environment, high oxygen availability, and exposure to aminoglycosides. Our findings define a role for YigI and shed light on why the E. coli genome harbors numerous thioesterases with closely related functions.

scholarly journals LET-767 Is Required for the Production of Branched Chain and Long Chain Fatty Acids inCaenorhabditis elegans

2008 ◽  
Vol 283 (25) ◽  
pp. 17550-17560 ◽  
Author(s):  
Eugeni V. Entchev ◽  
Dominik Schwudke ◽  
Vyacheslav Zagoriy ◽  
Vitali Matyash ◽  
Aliona Bogdanova ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Long Chain Fatty Acids ◽  
Branched Chain ◽  
Long Chain ◽  
Chain Fatty Acids

scholarly journals Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors

1999 ◽  
Vol 344 (1) ◽  
pp. 135-143 ◽  
Author(s):  
Kiran T. MALHOTRA ◽  
Khushbeer MALHOTRA ◽  
Bertram H. LUBIN ◽  
Frans A. KUYPERS
Keyword(s):  
Plasma Membranes ◽  
Fetal Liver ◽  
Erythrocyte Membranes ◽  
Long Chain Fatty Acids ◽  
Mature Erythrocyte ◽  
Haemopoietic Stem Cells ◽  
Chain Acyl ◽  
Kidney Liver ◽  
Long Chain

Full-length cDNA species encoding two forms of acyl-CoA synthetase from a K-562 human erythroleukaemic cell line were cloned, sequenced and expressed. The first form, named long-chain acyl-CoA synthetase 5 (LACS5), was found to be a novel, unreported, human acyl-CoA synthetase with high similarity to rat brain ACS2 (91% identical). The second form (66% identical with LACS5) was 97% identical with human liver LACS1. The LACS5 gene encodes a highly expressed 2.9 kb mRNA transcript in human haemopoietic stem cells from cord blood, bone marrow, reticulocytes and fetal blood cells derived from fetal liver. An additional 6.3 kb transcript is also found in these erythrocyte precursors; 2.9 and 9.6 kb transcripts of LACS5 are found in human brain, but transcripts are virtually absent from human heart, kidney, liver, lung, pancreas, spleen and skeletal muscle. The 78 kDa expressed LACS5 protein used the long-chain fatty acids palmitic acid, oleic acid and arachidonic acid as substrates. Antibodies directed against LACS5 cross-reacted with erythrocyte membranes. We conclude that early erythrocyte precursors express at least two different forms of acyl-CoA synthetase and that LACS5 is present in mature erythrocyte plasma membranes.

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