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ATP + H2O + C10-carnitine[side 1]
ADP + phosphate + C10-carnitine[side 2]
low activity
-
-
?
ATP + H2O + C12-carnitine[side 1]
ADP + phosphate + C12-carnitine[side 2]
-
-
-
?
ATP + H2O + C16-carnitine[side 1]
ADP + phosphate + C16-carnitine[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
ATP + H2O + heptadecanoyl-CoA/cis
ADP + phosphate + heptadecanoyl-CoA/trans
ATP + H2O + lauroyl-CoA[side 1]
ADP + phosphate + lauroyl-CoA[side 2]
-
-
-
?
ATP + H2O + long-chain fatty acyl CoA/cis
ADP + phosphate + long-chain fatty acyl CoA/trans
-
-
-
?
ATP + H2O + NBD-palmitoyl-CoA[side 1]
ADP + phosphate + NBD-palmitoyl-CoA[side 2]
-
-
-
?
ATP + H2O + palmitoyl-CoA[side 1]
ADP + phosphate + palmitoyl-CoA[side 2]
-
-
-
?
C18:1-CoA/out + ATP + H2O
C18:1-CoA/in + ADP + phosphate
cerotic acid + ATP + H2O
?
-
-
-
-
?
additional information
?
-
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs into the organelle
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
the dysfunction of ALDP is responsible for X-linked adrenoleukodystrophy, a neurodegenerative disorder, loss of ALDP dimerization plays a role in pathogenesis
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
PMp70 is involved in metabolic transport of long chain acyl-CoASs across the peroxisomal membranes
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
a defect in the gene for fatty-acyl-CoA-transporting ATPase is responsible for adrenoleukodystrophy, a demyelinating disorder characterized by the accumulation of saturated very-long-chain fatty acids
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
enzyme is involved in active transport across the peroxisomal membrane
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
ABCD gene encoded enzymes participate in the import of specific fatty acids in the peroxisomal matrix. ABCD1 deficiency is associated with X-linked adrenoleukodystrophy, X-ALD, the most frequent peroxisomal disorder, which is characterized by the accumulation of saturated very-long-chain fatty acids, VLCFA
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
enzyme is involved in metabolite transport across the peroxisomal membrane
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via the peroxisomal membrane proteins Pat1p and Pat2p
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
enzyme is required for import of activated fatty acids into peroxisomes
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
C18:1-CoA enters the peroxisome via the peroxisomal ATP-binding-cassette transporter Pxa2p
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
C18:1-CoA enters the peroxisome via the peroxisomal ATP-binding-cassette transporter Pxa2p
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
specificity of the two different uptake routes in peroxisomal beta-oxidation of fatty acids, overview
-
-
?
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
ALDP can function as a homodimer and accepts a range of acyl-CoA esters
-
-
?
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
specificity of the two different uptake routes in peroxisomal beta-oxidation of fatty acids, overview
-
-
?
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
ALDP can function as a homodimer and accepts a range of acyl-CoA esters
-
-
?
ATP + H2O + heptadecanoyl-CoA/cis
ADP + phosphate + heptadecanoyl-CoA/trans
-
-
-
-
?
ATP + H2O + heptadecanoyl-CoA/cis
ADP + phosphate + heptadecanoyl-CoA/trans
-
-
-
-
?
C18:1-CoA/out + ATP + H2O
C18:1-CoA/in + ADP + phosphate
-
-
-
?
C18:1-CoA/out + ATP + H2O
C18:1-CoA/in + ADP + phosphate
-
-
-
?
additional information
?
-
-
best substrates for rescue of a yeast pxa1/pxa2 deletion mutant by ABCD1 are C22:0 and different unsaturated very long-chain fatty acids including C24:6 and especially C22:6
-
-
?
additional information
?
-
best substrates for rescue of a yeast pxa1/pxa2 deletion mutant by ABCD1 are C22:0 and different unsaturated very long-chain fatty acids including C24:6 and especially C22:6
-
-
?
additional information
?
-
-
best substrates for rescue of a yeast pxa1/pxa2 deletion mutant by ABCD1 are C24:0 and C26:0 fatty acids
-
-
?
additional information
?
-
best substrates for rescue of a yeast pxa1/pxa2 deletion mutant by ABCD1 are C24:0 and C26:0 fatty acids
-
-
?
additional information
?
-
peroxisomes accept the CoA and carnitine ester of C12:0 andC16:0 as substrate in a mechanism possibly involving ABCD3. Production of CO2 and acid-soluble products from[1-14C]C16-carnitine. Concentrations of the C16:1-, C16-, C18:2-, C18:1-, and C18-carnitines and the ratio (C16+C18:1) in CPT2 inhibited cells, overview
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Ellman's reagent, 5,5-dithiobis(2-nitrobenzoic acid), is not sensitive enough to measure the activity of hABCD1. The enzyme possesses an equal levels of acyl-CoA thioesterase activity
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Ellman's reagent, 5,5-dithiobis(2-nitrobenzoic acid), is not sensitive enough to measure the activity of hABCD1. The enzyme possesses an equal levels of acyl-CoA thioesterase activity
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Ellman's reagent, 5,5-dithiobis(2-nitrobenzoic acid), is not sensitive enough to measure the activity of hABCD1. The enzyme possesses an equal levels of acyl-CoA thioesterase activity
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Enzyme hABCD2 possesses acyl-CoA thioesterase activity
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Enzyme hABCD2 possesses acyl-CoA thioesterase activity
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Enzyme hABCD2 possesses acyl-CoA thioesterase activity
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Enzyme hABCD3 possesses acyl-CoA thioesterase activity
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Enzyme hABCD3 possesses acyl-CoA thioesterase activity
-
-
?
additional information
?
-
activity measurement by malachite green phosphate determination assay. Enzyme hABCD3 possesses acyl-CoA thioesterase activity
-
-
?
additional information
?
-
-
lack of peroxisomal ABC transporters does not prevent peroxisomal long-chain fatty acid oxidation, suggesting the existence of another pathway for their import into peroxisomes, genetic regulation in the peroxisomal beta-oxidation, overview
-
-
?
additional information
?
-
lack of peroxisomal ABC transporters does not prevent peroxisomal long-chain fatty acid oxidation, suggesting the existence of another pathway for their import into peroxisomes, genetic regulation in the peroxisomal beta-oxidation, overview
-
-
?
additional information
?
-
-
Whatever the diet, no differences occur in gene expression of abcd genes in adrenals and brain. However, the hepatic expression level of abcd2 and abcd3 genes is signficantly higher in the n-3-de?cient rats than in the rats fed ALA diet or DHA supplemented diets. This is accompanied by important changes in hepatic fatty acid composition, the hepatic expression of abcd2 and abcd3, but not of abcd1 and abcd4, appears to be highly sensitive towards dietary polyunsaturated fatty acids, overview
-
-
?
additional information
?
-
-
proton gradient across the peroxisomal membrane depends on enzyme activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + C12-carnitine[side 1]
ADP + phosphate + C12-carnitine[side 2]
-
-
-
?
ATP + H2O + C16-carnitine[side 1]
ADP + phosphate + C16-carnitine[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
ATP + H2O + lauroyl-CoA[side 1]
ADP + phosphate + lauroyl-CoA[side 2]
-
-
-
?
ATP + H2O + long-chain fatty acyl CoA/cis
ADP + phosphate + long-chain fatty acyl CoA/trans
-
-
-
?
ATP + H2O + palmitoyl-CoA[side 1]
ADP + phosphate + palmitoyl-CoA[side 2]
-
-
-
?
additional information
?
-
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs into the organelle
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
the dysfunction of ALDP is responsible for X-linked adrenoleukodystrophy, a neurodegenerative disorder, loss of ALDP dimerization plays a role in pathogenesis
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
PMp70 is involved in metabolic transport of long chain acyl-CoASs across the peroxisomal membranes
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
a defect in the gene for fatty-acyl-CoA-transporting ATPase is responsible for adrenoleukodystrophy, a demyelinating disorder characterized by the accumulation of saturated very-long-chain fatty acids
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
enzyme is involved in active transport across the peroxisomal membrane
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
ABCD gene encoded enzymes participate in the import of specific fatty acids in the peroxisomal matrix. ABCD1 deficiency is associated with X-linked adrenoleukodystrophy, X-ALD, the most frequent peroxisomal disorder, which is characterized by the accumulation of saturated very-long-chain fatty acids, VLCFA
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
enzyme is involved in metabolite transport across the peroxisomal membrane
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via the peroxisomal membrane proteins Pat1p and Pat2p
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
enzyme is required for import of activated fatty acids into peroxisomes
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
C18:1-CoA enters the peroxisome via the peroxisomal ATP-binding-cassette transporter Pxa2p
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
C18:1-CoA enters the peroxisome via the peroxisomal ATP-binding-cassette transporter Pxa2p
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
specificity of the two different uptake routes in peroxisomal beta-oxidation of fatty acids, overview
-
-
?
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
specificity of the two different uptake routes in peroxisomal beta-oxidation of fatty acids, overview
-
-
?
additional information
?
-
peroxisomes accept the CoA and carnitine ester of C12:0 andC16:0 as substrate in a mechanism possibly involving ABCD3. Production of CO2 and acid-soluble products from[1-14C]C16-carnitine. Concentrations of the C16:1-, C16-, C18:2-, C18:1-, and C18-carnitines and the ratio (C16+C18:1) in CPT2 inhibited cells, overview
-
-
?
additional information
?
-
-
lack of peroxisomal ABC transporters does not prevent peroxisomal long-chain fatty acid oxidation, suggesting the existence of another pathway for their import into peroxisomes, genetic regulation in the peroxisomal beta-oxidation, overview
-
-
?
additional information
?
-
lack of peroxisomal ABC transporters does not prevent peroxisomal long-chain fatty acid oxidation, suggesting the existence of another pathway for their import into peroxisomes, genetic regulation in the peroxisomal beta-oxidation, overview
-
-
?
additional information
?
-
-
Whatever the diet, no differences occur in gene expression of abcd genes in adrenals and brain. However, the hepatic expression level of abcd2 and abcd3 genes is signficantly higher in the n-3-de?cient rats than in the rats fed ALA diet or DHA supplemented diets. This is accompanied by important changes in hepatic fatty acid composition, the hepatic expression of abcd2 and abcd3, but not of abcd1 and abcd4, appears to be highly sensitive towards dietary polyunsaturated fatty acids, overview
-
-
?
additional information
?
-
-
proton gradient across the peroxisomal membrane depends on enzyme activity
-
-
?
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malfunction
-
germination of ped3 mutants is significantly impaired, suggesting that PED3 regulates dormancy and germination. A ped3 abi5 (ABA insensitive 5) double mutant does not show any of the expression patterns of ped3 mutants and rescues the impaired germination phenotype of the ped3 mutant. The impaired germination of ped3 can also be rescued by removal of pectin from the seed coat using exogenous polygalacturonase or acidic conditions
metabolism
the peroxisomal import of fatty acids is mediated by 3 ATP-binding cassette transporters (ABCD1, -2, and -3). Transport mediated by ABCD3 is crucial in the peroxisomal degradation of medium-chain fatty acids and might be involved in the production of CO2 and acid-soluble products from C16-carnitine. Mitochondrial FAO inhibition with etomoxir does not lead to significant accumulation of any acylcarnitine species
evolution
ABCD1-3 belong to the ATP-binding cassette protein superfamily, subfamily D, membrane-bound proteins with highly conserved structure
evolution
the ABCD1 transporter belongs to the D subfamily of the ATP-binding cassette (ABC)2 transporter family and is encoded by the ABCD1 gene
evolution
the ABCD2 transporter belongs to the D subfamily of the ATP-binding cassette (ABC)2 transporter family and is encoded by the ABCD1 gene
evolution
the LLL motif likely belongs to a hydrophobic helix, which is quite well conserved in other ABCD transporters (20-23 in ABCD3). The IL motif near the TMH 5 (I307-L308) belongs to a consensus sequence composed of three hydrophobic residues
evolution
the LLL motif likely belongs to a hydrophobic helix, which is quite well conserved in other ABCD transporters (20-36 in ABCD1). The IL motif near the TMH 5 belongs to a consensus sequence composed of three hydrophobic residues [FL]-I-[FL] (LIL in ABCD1)
physiological function
-
ABC transporter ALDP interacts with ACLY and FATP4, ABC transporter PMP70 interacts with FASN and FATP4 involved in fatty acid metabolism, thus constituting a fatty acid synthesis-transport machinery at the cytoplasmic side of the peroxisomal membrane
physiological function
very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes with the CoA presumably being released into the cytoplasm. The Pxa1p-Pxa2p complex functionally interacts with the acyl-CoA synthetases Faa2p and/or Fat1p on the inner surface of the peroxisomal membrane for subsequent re-esterification of the very long chain fatty acids
physiological function
ABCD1 and its homologue ABCD2 are peroxisomal ATP-binding cassette (ABC) half-transporters of fatty acyl-CoAs with both distinct and overlapping substrate specificities
physiological function
the D-bifunctional protein (HSD17B4) and the peroxisomal ABC transporter ABCD3 are essential in peroxisomal oxidation of lauric and palmitic acid, besides mitochondrial carnitine palmitoyltransferase (CPT)2 (EC 2.3.1.21), leading to the production of peroxisomal acylcarnitine intermediates. Peroxisomes accept acyl-CoAs and oxidize acylcarnitines in a similar biochemical pathway as the mitochondria. Peroxisomal fatty acid beta-oxidation (FAO) is important when mitochondrial FAO is defective or overloaded. The peroxisomal import of fatty acids is mediated by 3 ATP-binding cassette transporters (ABCD1, -2, and -3). Transport mediated by ABCD3 is crucial in the peroxisomal degradation of medium-chain fatty acids. The peroxisomal ABC transporters transport acyl-CoA intermediates and C12/C16-carnitines, peroxisomes accept the CoA and carnitine ester of C12:0 and C16:0 as substrate in a mechanism possibly involving ABCD3
physiological function
-
very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes with the CoA presumably being released into the cytoplasm. The Pxa1p-Pxa2p complex functionally interacts with the acyl-CoA synthetases Faa2p and/or Fat1p on the inner surface of the peroxisomal membrane for subsequent re-esterification of the very long chain fatty acids
-
additional information
absence of interaction between solubilized ABCD1 and ABCD2 within supradimeric assemblies, but ABCD1 interacts with ABCD2 in the BV-2 microglial cell line and in cell lysates, interaction analysis. ABCD1 and ABCD2 tetrameric assemblies remain unchanged during the catalytic cycle of the transporters
additional information
absence of interaction between solubilized ABCD1 and ABCD2 within supradimeric assemblies, but ABCD1 interacts with ABCD2 in the BV-2 microglial cell line and in cell lysates, interaction analysis. ABCD1 and ABCD2 tetrameric assemblies remain unchanged during the catalytic cycle of the transporters
additional information
structure homology modeling using the the 2.85 A resolution rod form structure of ABCB10 (PDB ID 4AYX) as template
additional information
structure homology modeling using the the 2.85 A resolution rod form structure of ABCB10 (PDB ID 4AYX) as template
additional information
structure homology modeling using the the 2.85 A resolution rod form structure of ABCB10 (PDB ID 4AYX) as template
additional information
-
structure homology modeling using the the 2.85 A resolution rod form structure of ABCB10 (PDB ID 4AYX) as template
additional information
structure homology modeling using the the 2.85 A resolution rod form structure of ABCB10 (PDB ID 4AYX) as template, low similarity between ABCB10 and ABCD1
additional information
structure homology modeling using the the 2.85 A resolution rod form structure of ABCB10 (PDB ID 4AYX) as template, low similarity between ABCB10 and ABCD1
additional information
structure homology modeling using the the 2.85 A resolution rod form structure of ABCB10 (PDB ID 4AYX) as template, low similarity between ABCB10 and ABCD1
additional information
-
structure homology modeling using the the 2.85 A resolution rod form structure of ABCB10 (PDB ID 4AYX) as template, low similarity between ABCB10 and ABCD1
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?
x * 149400, deduced from gene sequence and SDS-PAGE
?
x * 70000, recombinant His-tagged ABCD3
?
x * 75000, recombinant His-tagged ABCD1
?
x * 75000, recombinant His-tagged ABCD2
?
-
ALDP, x * 59753, electrospray ionization mass spectrometry
?
-
PMP70, x * 75483, electrospray ionization mass spectrometry
?
-
x * 84000, calculation from amino acid sequence
dimer
-
ALDP can form homodimers as well as heterodimers with the peroxisomal membrane protein PMP70
dimer
-
homodimer and heterodimer with other peroxisomal ABC proteins
dimer
-
PMP70 can form homodimers as well as heterodimers with the adrenoleukodystrophy protein ALDP
dimer
-
homodimer or heterodimer
heterodimer
-
Pxa1, Pxa2
heterodimer
-
two peroxisomal half ABC transporters Pxa1p and Pxa2p form a heterodimeric complex in the peroxisomal membrane
heterodimer
-
two peroxisomal half ABC transporters Pxa1p and Pxa2p form a heterodimeric complex in the peroxisomal membrane
-
heterotetramer
quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview
heterotetramer
quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview
homodimer
dimerization is considered as an obligatory step for stability and function of peroxisomal ABC transporters
homodimer
quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview
homodimer
quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview
homodimer
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ALDP can function as a homodimer and accepts a range of acyl-CoA esters
homodimer
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ALDP can function as a homodimer and accepts a range of acyl-CoA esters
-
homotetramer
quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview
homotetramer
quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview
additional information
-
-
additional information
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ALDP, ALDRP and PMP70 have the structure of ABC half-transporters
additional information
structure modeling of ABCD1, overview
additional information
structure modeling of ABCD1, overview
additional information
structure modeling of ABCD1, overview
additional information
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structure modeling of ABCD1, overview
additional information
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ALDP, ALDRP and PMP70 have the structure of ABC half-transporters
additional information
both transporters, ABCD1 and ABCD2, exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies are also found but represent only a minor fraction
additional information
both transporters, ABCD1 and ABCD2, exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies are also found but represent only a minor fraction
additional information
both transporters, ABCD1 and ABCD2, exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies are also found but represented only a minor fraction
additional information
both transporters, ABCD1 and ABCD2, exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies are also found but represented only a minor fraction
additional information
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the Saccharomyces cerevisiae homolog of the human adrenoleukodystrophy transporter is a heterodimer of two half ATP-binding cassette transporters Pxa1p and Pxa2p
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K487A
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mutation in Walker A motif, no beta-oxidation activity
ALDP390
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mutant, comprises the amino acids 1 to 390
ALDP550
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mutant, comprises the amino acids 1 to 550
ALDP658
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mutant, comprises the amino acids 1 to 658
ALDPDELTA551-657
-
mutant, residues 551-657 are deleted
ALDPDELTANBF
-
mutant, residues 391-657 are deleted
G116R
-
naturally occuring missense mutation
H667D
-
naturally occuring missense mutation
Q544R
-
naturally occuring missense mutation
R104C
-
naturally occuring missense mutation
R617H
-
naturally occuring missense mutation
S342P
-
naturally occuring missense mutation
S606L
-
naturally occuring missense mutation
S606P
-
naturally occuring missense mutation
Y174C
-
naturally occuring missense mutation
additional information
isolation of enzyme mutant plants resistant to 2,4-dichlorophenoxybutyric acid, mutant seedlings have growth defects and a defect in degrading the seed-reserved lipids
additional information
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upon expression in Saccharomyces cerevisiae, CTS is correctly targeted to yeast peroxisomes, assembled into the membrane with its nucleotide binding domains in the cytosol, and exhibits basal ATPase activity that is sensitive to aluminum fluoride and abrogated by mutation of a conserved Walker A motif lysine residue. CTS rescues the oleate growth phenotype of the pxa1 pxa2 deletion mutant, and restores beta-oxidation of fatty acids with a range of chain lengths and varying degrees of desaturation. When expressed in yeast peroxisomal membranes, the basal ATPase activity of CTS can be stimulated by fatty acyl-CoAs but not by fatty acids
additional information
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full-length PMP70 molecule is clearly located in the endoplasmic reticulum in the absence of the N-terminal 80-segment, even when multiple peroxisome-targeting signals are retained
additional information
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when the N-terminal 80 amino acid residue (N80)-segment preceding transmembrane segment (TM) 1 is deleted and the TM1-TM2 region is fused to EGFP, the TM1 segment induces endoplasmic reticulum-targeting and integration in COS cells
additional information
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when the N-terminal 80-segment is fused to EGFP, the fusion protein is targeted to the outer mitochondrial membrane
additional information
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the phenotype of the pxa1/pxa2 yeast deletion mutant, i.e. impaired growth on oleate containing medium and deficient oxidation of oleic acid, can partially be rescued by human ABCD1. Cells expressing ABCD1 rescue of beta-oxidation activity is best with C24:0 and C26:0 as substrates
additional information
the phenotype of the pxa1/pxa2 yeast deletion mutant, i.e. impaired growth on oleate containing medium and deficient oxidation of oleic acid, can partially be rescued by human ABCD1. Cells expressing ABCD1 rescue of beta-oxidation activity is best with C24:0 and C26:0 as substrates
additional information
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the phenotype of the pxa1/pxa2 yeast deletion mutant, i.e. impaired growth on oleate containing medium and deficient oxidation of oleic acid, can partially be rescued by human ABCD2. Cells expressing ABCD2 rescue of beta-oxidation activity is best with C22:0 and different unsaturated very long-chain fatty acids including C24:6 and especially C22:6 as substrates
additional information
the phenotype of the pxa1/pxa2 yeast deletion mutant, i.e. impaired growth on oleate containing medium and deficient oxidation of oleic acid, can partially be rescued by human ABCD2. Cells expressing ABCD2 rescue of beta-oxidation activity is best with C22:0 and different unsaturated very long-chain fatty acids including C24:6 and especially C22:6 as substrates
additional information
construction of ABCD3 single-KO and CPT2/ABCD3 double-KO cell lines, which have undetectable ABCD3 protein levels
additional information
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construction of deletion mutants DELTApABC1 and DELTApABC1/DELTApABC2, which act as partial suppressors of DELTAfox2 and DELTAechA germination defects, three genes involved in peroxisomal, fox2, and mitochondrial, scdA and echA, beta-oxidation, phenotypes, overview
additional information
construction of deletion mutants DELTApABC1 and DELTApABC1/DELTApABC2, which act as partial suppressors of DELTAfox2 and DELTAechA germination defects, three genes involved in peroxisomal, fox2, and mitochondrial, scdA and echA, beta-oxidation, phenotypes, overview
additional information
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construction of deletion mutants DELTApABC2 and DELTApABC1/DELTApABC2, which act as partial suppressors of DELTAfox2 and DELTAechA germination defects, three genes involved in peroxisomal, fox2, and mitochondrial, scdA and echA, beta-oxidation, phenotypes, overview
additional information
construction of deletion mutants DELTApABC2 and DELTApABC1/DELTApABC2, which act as partial suppressors of DELTAfox2 and DELTAechA germination defects, three genes involved in peroxisomal, fox2, and mitochondrial, scdA and echA, beta-oxidation, phenotypes, overview
additional information
-
enzyme deletion mutant, no pH-gradient across peroxisomal membrane, while in wild-type, peroxisomal matrix is alkaline
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Kamijo, K.; Taketani, S.; Yokota, S.; Osumi, T.; Hashimoto, T.
The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily
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Genomic organization of the 70-kDa peroxisomal membrane protein gene (PXMP1)
Genomics
48
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Homo sapiens
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Hettema, E.H.; van Roermund, C.W.; Distel, B.; van den Berg, M.; Vilela, C.; Rodrigues-Pousada, C.; Wanders, R.J.; Tabak, H.F.
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Characterization of the 70-kDa peroxisomal membrane protein, an ATP binding cassette transporter
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274
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Homo- and heterodimerization of peroxisomal ATP-binding cassette half-transporters
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Homo sapiens, Mus musculus
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8
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Homo sapiens, Mus musculus
brenda
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A Saccharomyces cerevisiae homolog of the human adrenoleukodystrophy transporter is a heterodimer of two half ATP-binding cassette transporters
Proc. Natl. Acad. Sci. USA
93
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Saccharomyces cerevisiae, Homo sapiens
brenda
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Saccharomyces cerevisiae, Saccharomyces cerevisiae Pxa2p
brenda
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The peroxisomal lumen in Saccharomyces cerevisiae is alkaline
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117
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2004
Saccharomyces cerevisiae
brenda
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Ped3 is a peroxisomal ATP-binding cassette transporter that might supply substrates for fatty acid beta-oxidation
Plant Cell Physiol.
43
1-11
2002
Arabidopsis thaliana (Q94FB9)
brenda
Gueugnon, F.; Volodina, N.; Taouil, J.E.; Lopez, T.E.; Gondcaille, C.; Grand, A.S.; Mooijer, P.A.; Kemp, S.; Wanders, R.J.; Savary, S.
A novel cell model to study the function of the adrenoleukodystrophy-related protein
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341
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2006
Rattus norvegicus
brenda
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Mouse liver PMP70 and ALDP: homomeric interactions prevail in vivo
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1689
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2004
Mus musculus
brenda
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Role of Pex19p in the targeting of PMP70 to peroxisome
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1746
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2005
Homo sapiens
brenda
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ATP-binding and -hydrolysis activities of ALDP (ABCD1) and ALDRP (ABCD2), human peroxisomal ABC proteins, overexpressed in Sf21 cells
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29
1836-1842
2006
Rattus norvegicus
brenda
Hillebrand, M.; Verrier, S.E.; Ohlenbusch, A.; Schaefer, A.; Soeling, H.D.; Wouters, F.S.; Gaertner, J.
Live cell FRET microscopy: homo- and heterodimerization of two human peroxisomal ABC transporters, the adrenoleukodystrophy protein (ALDP, ABCD1) and PMP70 (ABCD3)
J. Biol. Chem.
282
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2007
Homo sapiens
brenda
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101
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Homo sapiens
brenda
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Mol. Genet. Metab.
90
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2007
Mammalia, Saccharomyces cerevisiae
brenda
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52
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2008
Rattus norvegicus
brenda
Leclercq, S.; Skrzypski, J.; Courvoisier, A.; Gondcaille, C.; Bonnetain, F.; Andre, A.; Chardigny, J.M.; Bellenger, S.; Bellenger, J.; Narce, M.; Savary, S.
Effect of dietary polyunsaturated fatty acids on the expression of peroxisomal ABC transporters
Biochimie
90
1602-1607
2008
Rattus norvegicus
brenda
van Roermund, C.W.; Visser, W.F.; Ijlst, L.; van Cruchten, A.; Boek, M.; Kulik, W.; Waterham, H.R.; Wanders, R.J.
The human peroxisomal ABC half transporter ALDP functions as a homodimer and accepts acyl-CoA esters
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22
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Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ1991
brenda
Boisnard, S.; Espagne, E.; Zickler, D.; Bourdais, A.; Riquet, A.L.; Berteaux-Lecellier, V.
Peroxisomal ABC transporters and beta-oxidation during the life cycle of the filamentous fungus Podospora anserina
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46
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Podospora anserina, Podospora anserina (Q7Z9L6)
brenda
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147
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Arabidopsis thaliana
brenda
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1811
148-152
2011
Homo sapiens, Homo sapiens (P33897)
brenda
Nyathi, Y.; De Marcos Lousa, C.; van Roermund, C.W.; Wanders, R.J.; Johnson, B.; Baldwin, S.A.; Theodoulou, F.L.; Baker, A.
The Arabidopsis peroxisomal ABC transporter, comatose, complements the Saccharomyces cerevisiae pxa1 pxa2Delta mutant for metabolism of long-chain fatty acids and exhibits fatty acyl-CoA-stimulated ATPase activity
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285
29892-29902
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Arabidopsis thaliana
brenda
van Roermund, C.W.; Ijlst, L.; Majczak, W.; Waterham, H.R.; Folkerts, H.; Wanders, R.J.; Hellingwerf, K.J.
Peroxisomal fatty acid uptake mechanism in Saccharomyces cerevisiae
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287
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Saccharomyces cerevisiae (P34230), Saccharomyces cerevisiae (P41909), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P34230), Saccharomyces cerevisiae ATCC 204508 (P41909)
brenda
Hillebrand, M.; Gersting, S.W.; Lotz-Havla, A.S.; Schaefer, A.; Rosewich, H.; Valerius, O.; Muntau, A.C.; Gaertner, J.
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Homo sapiens
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Okamoto, T.; Kawaguchi, K.; Watanabe, S.; Agustina, R.; Ikejima, T.; Ikeda, K.; Nakano, M.; Morita, M.; Imanaka, T.
Characterization of human ATP-binding cassette protein subfamily D reconstituted into proteoliposomes
Biochem. Biophys. Res. Commun.
496
1122-1127
2018
Homo sapiens (P28288), Homo sapiens (P33897), Homo sapiens (Q9UBJ2)
brenda
Violante, S.; Achetib, N.; van Roermund, C.W.T.; Hagen, J.; Dodatko, T.; Vaz, F.M.; Waterham, H.R.; Chen, H.; Baes, M.; Yu, C.; Argmann, C.A.; Houten, S.M.
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Homo sapiens (P28288)
brenda
Andreoletti, P.; Raas, Q.; Gondcaille, C.; Cherkaoui-Malki, M.; Trompier, D.; Savary, S.
Predictive structure and topology of peroxisomal ATP-binding cassette (ABC) transporters
Int. J. Mol. Sci.
18
E1593-E1607
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Homo sapiens (P28288), Homo sapiens (P33897), Homo sapiens (Q9UBJ2), Homo sapiens
brenda
Geillon, F.; Gondcaille, C.; Raas, Q.; Dias, A.M.M.; Pecqueur, D.; Truntzer, C.; Lucchi, G.; Ducoroy, P.; Falson, P.; Savary, S.; Trompier, D.
Peroxisomal ATP-binding cassette transporters form mainly tetramers
J. Biol. Chem.
292
6965-6977
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Mus musculus (P48410), Mus musculus (Q61285)
brenda