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Information on EC 7.6.2.4 - ABC-type fatty-acyl-CoA transporter
for references in articles please use BRENDA:EC7.6.2.4
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EC Tree 7 Translocases
7.6 Catalysing the translocation of other compounds
7.6.2 Linked to the hydrolysis of a nucleoside triphosphate
7.6.2.4 ABC-type fatty-acyl-CoA transporter
IUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger’s syndrome.
The enzyme appears in viruses and cellular organisms
- 7.6.2.4
- cerebral
- cardiac
-
admission
- consciousness
-
admitted
-
resuscitation
-
survivors
- artery
-
discharge
- intracranial
-
hypothermia
- hemorrhage
-
glasgow
- stroke
-
out-of-hospital
- trauma
-
x-linked
- seizure
-
traumatic
-
ventilation
- encephalopathy
- brainstem
- reflex
- woman
-
angiography
-
cardiopulmonary
- hematoma
-
subarachnoid
-
unconscious
- epilepticus
-
somatosensory
-
sedation
-
electroencephalogram
-
electroencephalography
-
subdural
-
vlcfas
-
neurosurgical
-
intubation
-
awaken
-
pupillary
-
evacuation
- pupil
-
rewarming
- hemiparesis
-
herniation
-
in-hospital
-
normothermia
-
nontraumatic
- medicine
-
craniectomy
-
prehospital
Reaction Schemes
show+
+
fatty acyl CoA[side 1]
=
+
+
fatty acyl CoA[side 2]
Synonyms
comatose, abcd1, abcd2, pmp70, abcd3, adrenoleukodystrophy protein, aldrp, pat1p, 70-kda peroxisomal membrane protein, peroxisomal abc transporter, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
70-kDa peroxisomal membrane protein
ABC half transporter
ABCD1
ABCD2
ABCD3
adrenoleukodystrophy protein
adrenoleukodystrophy-related protein
ALDP
ALDRP
EC 3.6.3.47
-
-
formerly
-
fatty acid transporter
fatty-acyl-CoA-transporting ATPase
Ped3
peroxisomal ABC transporter
PMP70
Pxa
Pxa1p
Pxa1p/Pxa2p
Pxa2p
fatty-acyl-CoA-transporting ATPase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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]
ALDP exhibits an affinity to both ADP and ATP, ALDRP exhibits an affinity to ADP but scarcely to ATP
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, fatty-acyl-CoA-transporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + (25R)-dihydroxycholestanoyl-CoA[side 1]
ADP + phosphate + (25R)-dihydroxycholestanoyl-CoA[side 2]
Substrates: -
Products: -
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?
ATP + H2O + (25R)-trihydroxycholestanoyl-CoA[side 1]
ADP + phosphate + (25R)-trihydroxycholestanoyl-CoA[side 2]
Substrates: -
Products: -
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?
ATP + H2O + 7-nitro-2-1,3-benzoxadiazol-4-yl-hexadecanoyl-CoA[side 1]
ADP + phosphate + 7-nitro-2-1,3-benzoxadiazol-4-yl-hexadecanoyl-CoA[side 2]
Substrates: -
Products: -
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?
ATP + H2O + behenoyl-CoA[side 1]
ADP + phosphate + behenoyl-CoA[side 2]
Substrates: -
Products: -
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?
ATP + H2O + C10-carnitine[side 1]
ADP + phosphate + C10-carnitine[side 2]
Substrates: low activity
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?
ATP + H2O + C12-carnitine[side 1]
ADP + phosphate + C12-carnitine[side 2]
Substrates: -
Products: -
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?
ATP + H2O + C16-carnitine[side 1]
ADP + phosphate + C16-carnitine[side 2]
Substrates: -
Products: -
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?
ATP + H2O + cerotoyl-CoA[side 1]
ADP + phosphate + cerotoyl-CoA[side 2]
Substrates: -
Products: -
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?
ATP + H2O + cholic acid[side 1]
ADP + phosphate + cholic acid[side 2]
-
Substrates: -
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?
ATP + H2O + choloyl-CoA[side 1]
ADP + phosphate + choloyl-CoA[side 2]
-
Substrates: -
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?
ATP + H2O + deoxycholoyl-CoA[side 1]
ADP + phosphate + ceoxycholoyl-CoA[side 2]
-
Substrates: -
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?
ATP + H2O + dihydroxycholestanoyl-CoA[side 1]
ADP + phosphate + dihydroxycholestanoyl-CoA[side 2]
-
Substrates: -
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?
ATP + H2O + docosahexaenoyl-CoA[side 1]
ADP + phosphate + docosahexaenoyl-CoA[side 2]
Substrates: isoform ABCD2 has an affinity for polyunsaturated fatty acids such as docosahexaenoyl-CoA
Products: -
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?
ATP + H2O + hexacosanoyl-CoA[side 1]
ADP + phosphate + hexacosanoyl-CoA[side 2]
Substrates: -
Products: -
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?
ATP + H2O + lignoceroyl-CoA[side 1]
ADP + phosphate + lignoceroyl-CoA[side 2]
Substrates: -
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?
ATP + H2O + long-chain dicarboxylic fatty acyl-CoA[side 1]
ADP + phosphate + long-chain dicarboxylic fatty acyl-CoA[side 2]
-
Substrates: -
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?
ATP + H2O + long-chain fatty acyl CoA/cis
ADP + phosphate + long-chain fatty acyl CoA/trans
Substrates: -
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?
ATP + H2O + muricholic acid[side 1]
ADP + phosphate + muricholic acid[side 2]
-
Substrates: -
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?
ATP + H2O + murichoyl-CoA[side 1]
ADP + phosphate + murichoyl-CoA[side 2]
-
Substrates: -
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ATP + H2O + myristoyl-CoA[side 1]
ADP + phosphate + myristoyl-CoA[side 2]
-
Substrates: -
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?
ATP + H2O + NBD-palmitoyl-CoA[side 1]
ADP + phosphate + NBD-palmitoyl-CoA[side 2]
Substrates: -
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?
ATP + H2O + oleoyl-CoA[side 1]
ADP + phosphate + oleoyl-CoA[side 2]
Substrates: -
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?
ATP + H2O + palmitoyl-CoA[side 1]
ADP + phosphate + palmitoyl-CoA[side 2]
Substrates: -
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ATP + H2O + phytanoyl-CoA[side 1]
ADP + phosphate + phytanoyl-CoA[side 2]
Substrates: -
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?
ATP + H2O + pristanoyl-CoA[side 1]
ADP + phosphate + pristanoyl-CoA[side 2]
Substrates: -
Products: -
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ATP + H2O + tetracosahexaenoyl-CoA[side 1]
ADP + phosphate + tetracosahexaenoyl-CoA[side 2]
Substrates: isoform ABCD2 has an affinity for polyunsaturated fatty acids such as tetracosahexaenoyl-CoA
Products: -
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?
ATP + H2O + trihydroxycholestanoyl-CoA[side 1]
ADP + phosphate + trihydroxycholestanoyl-CoA[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + very long chain fatty acyl-CoA[side 1]
ADP + phosphate + very long chain fatty acyl-CoA[side 2]
Substrates: -
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?
ATP + H2O + very long-chain fatty acyl-CoA[side 1]
ADP + phosphate + very long-chain fatty acyl-CoA[side 2]
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs into the organelle
Products: -
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: the dysfunction of ALDP is responsible for X-linked adrenoleukodystrophy, a neurodegenerative disorder, loss of ALDP dimerization plays a role in pathogenesis
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: PMp70 is involved in metabolic transport of long chain acyl-CoASs across the peroxisomal membranes
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: 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
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: enzyme is involved in active transport across the peroxisomal membrane
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: 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
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: enzyme is involved in metabolite transport across the peroxisomal membrane
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via the peroxisomal membrane proteins Pat1p and Pat2p
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: enzyme is required for import of activated fatty acids into peroxisomes
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: C18:1-CoA enters the peroxisome via the peroxisomal ATP-binding-cassette transporter Pxa2p
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: C18:1-CoA enters the peroxisome via the peroxisomal ATP-binding-cassette transporter Pxa2p
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ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
Substrates: -
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?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
Substrates: -
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?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
Substrates: -
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ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
Substrates: -
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ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
Substrates: specificity of the two different uptake routes in peroxisomal beta-oxidation of fatty acids, overview
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ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
Substrates: ALDP can function as a homodimer and accepts a range of acyl-CoA esters
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ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
Substrates: specificity of the two different uptake routes in peroxisomal beta-oxidation of fatty acids, overview
Products: -
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?
ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
Substrates: ALDP can function as a homodimer and accepts a range of acyl-CoA esters
Products: -
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?
ATP + H2O + fatty acyl-CoA[side 1]
ADP + phosphate + fatty acyl-CoA[side 2]
Substrates: -
Products: -
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?
ATP + H2O + fatty acyl-CoA[side 1]
ADP + phosphate + fatty acyl-CoA[side 2]
-
Substrates: -
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?
ATP + H2O + fatty acyl-CoA[side 1]
ADP + phosphate + fatty acyl-CoA[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + heptadecanoyl-CoA/cis
ADP + phosphate + heptadecanoyl-CoA/trans
-
Substrates: -
Products: -
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?
ATP + H2O + heptadecanoyl-CoA/cis
ADP + phosphate + heptadecanoyl-CoA/trans
-
Substrates: -
Products: -
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?
ATP + H2O + lauroyl-CoA[side 1]
ADP + phosphate + lauroyl-CoA[side 2]
Substrates: -
Products: -
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?
ATP + H2O + lauroyl-CoA[side 1]
ADP + phosphate + lauroyl-CoA[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + octanoyl-CoA[side 1]
ADP + phosphate + octanoyl-CoA[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + octanoyl-CoA[side 1]
ADP + phosphate + octanoyl-CoA[side 2]
-
Substrates: -
Products: -
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?
ATP + H2O + very long-chain fatty acyl-CoA[side 1]
ADP + phosphate + very long-chain fatty acyl-CoA[side 2]
-
Substrates: -
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?
ATP + H2O + very long-chain fatty acyl-CoA[side 1]
ADP + phosphate + very long-chain fatty acyl-CoA[side 2]
Substrates: -
Products: -
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?
C18:1-CoA/out + ATP + H2O
C18:1-CoA/in + ADP + phosphate
-
Substrates: -
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?
C18:1-CoA/out + ATP + H2O
C18:1-CoA/in + ADP + phosphate
-
Substrates: -
Products: -
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?
additional information
?
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Substrates: best substrates for rescue of a yeast pxa1/pxa2 deletion mutant by ABCD1 are C24:0 and C26:0 fatty acids
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additional information
?
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Substrates: best substrates for rescue of a yeast pxa1/pxa2 deletion mutant by ABCD1 are C24:0 and C26:0 fatty acids
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additional information
?
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
?
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Substrates: activity measurement by malachite green phosphate determination assay. Enzyme hABCD2 possesses acyl-CoA thioesterase activity
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?
additional information
?
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Substrates: activity measurement by malachite green phosphate determination assay. Enzyme hABCD2 possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: activity measurement by malachite green phosphate determination assay. Enzyme hABCD2 possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: activity measurement by malachite green phosphate determination assay. Enzyme hABCD3 possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: activity measurement by malachite green phosphate determination assay. Enzyme hABCD3 possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: activity measurement by malachite green phosphate determination assay. Enzyme hABCD3 possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: the acyl-CoA thioesterase (ACOT) activity of enzyme ABCD1 is required for the transport of very long-chain acyl-CoA into peroxisomes. ATPase activity is not essential for ABCD1-catalyzed ACOT activity
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additional information
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Substrates: the enzyme does not use 7-nitro-2-1,3-benzoxadiazol-4-yl-hexadecanoyl-3'-dephospho-CoA and 7-nitro-2-1,3-benzoxadiazol-4-yl-hexanoyl-CoA as substrate
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?
additional information
?
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Substrates: isoform ABCD3 also possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: isoform ABCD3 also possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: isoform ABCD3 also possesses acyl-CoA thioesterase activity
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additional information
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Substrates: isoform ABCD1 also possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: isoform ABCD1 also possesses acyl-CoA thioesterase activity
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additional information
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Substrates: isoform ABCD1 also possesses acyl-CoA thioesterase activity
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additional information
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Substrates: isoform ABCD1+2+3 also possesses acyl-CoA thioesterase activity
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additional information
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Substrates: isoform ABCD1+2+3 also possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: isoform ABCD1+2+3 also possesses acyl-CoA thioesterase activity
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additional information
?
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Substrates: no activity with docosahexaenoyl-CoA or acetyl CoA
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additional information
?
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Substrates: acetyl-CoA is not a substrate
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: proton gradient across the peroxisomal membrane depends on enzyme activity
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additional information
?
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Substrates: the enzyme accepts medium, long and very long-chain acyl-CoA esters as substrates. The enzyme also has acyl-CoA thioesterase activity
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + C12-carnitine[side 1]
ADP + phosphate + C12-carnitine[side 2]
Substrates: -
Products: -
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ATP + H2O + C16-carnitine[side 1]
ADP + phosphate + C16-carnitine[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + lauroyl-CoA[side 1]
ADP + phosphate + lauroyl-CoA[side 2]
Substrates: -
Products: -
Products: -
?
ATP + H2O + long-chain dicarboxylic fatty acyl-CoA[side 1]
ADP + phosphate + long-chain dicarboxylic fatty acyl-CoA[side 2]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + long-chain fatty acyl CoA/cis
ADP + phosphate + long-chain fatty acyl CoA/trans
Substrates: -
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ATP + H2O + palmitoyl-CoA[side 1]
ADP + phosphate + palmitoyl-CoA[side 2]
Substrates: -
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ATP + H2O + very long chain fatty acyl-CoA[side 1]
ADP + phosphate + very long chain fatty acyl-CoA[side 2]
Substrates: -
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ATP + H2O + very long-chain fatty acyl-CoA[side 1]
ADP + phosphate + very long-chain fatty acyl-CoA[side 2]
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs into the organelle
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: the dysfunction of ALDP is responsible for X-linked adrenoleukodystrophy, a neurodegenerative disorder, loss of ALDP dimerization plays a role in pathogenesis
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: PMp70 is involved in metabolic transport of long chain acyl-CoASs across the peroxisomal membranes
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: 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
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: enzyme is involved in active transport across the peroxisomal membrane
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: 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
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: enzyme is involved in metabolite transport across the peroxisomal membrane
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: long-chain fatty acids are imported from the cytosolic pool of activated long-chain fatty acids via the peroxisomal membrane proteins Pat1p and Pat2p
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: enzyme is required for import of activated fatty acids into peroxisomes
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: C18:1-CoA enters the peroxisome via the peroxisomal ATP-binding-cassette transporter Pxa2p
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: -
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ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
Substrates: C18:1-CoA enters the peroxisome via the peroxisomal ATP-binding-cassette transporter Pxa2p
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ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
Substrates: -
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ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
Substrates: -
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ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
Substrates: -
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ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
Substrates: -
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ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
Substrates: specificity of the two different uptake routes in peroxisomal beta-oxidation of fatty acids, overview
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ATP + H2O + fatty acyl-CoA/cis
ADP + phosphate + fatty acyl-CoA/trans
-
Substrates: specificity of the two different uptake routes in peroxisomal beta-oxidation of fatty acids, overview
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ATP + H2O + fatty acyl-CoA[side 1]
ADP + phosphate + fatty acyl-CoA[side 2]
Substrates: -
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ATP + H2O + fatty acyl-CoA[side 1]
ADP + phosphate + fatty acyl-CoA[side 2]
-
Substrates: -
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ATP + H2O + fatty acyl-CoA[side 1]
ADP + phosphate + fatty acyl-CoA[side 2]
-
Substrates: -
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ATP + H2O + very long-chain fatty acyl-CoA[side 1]
ADP + phosphate + very long-chain fatty acyl-CoA[side 2]
-
Substrates: -
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ATP + H2O + very long-chain fatty acyl-CoA[side 1]
ADP + phosphate + very long-chain fatty acyl-CoA[side 2]
Substrates: -
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additional information
?
-
Substrates: 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
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additional information
?
-
-
Substrates: 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
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additional information
?
-
Substrates: 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
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additional information
?
-
-
Substrates: 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
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additional information
?
-
-
Substrates: proton gradient across the peroxisomal membrane depends on enzyme activity
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AlF3
moderate inhibition of the ATPase activity of liposome-reconstituted His-hABCD3; strong inhibition of the ATPase activity of liposome-reconstituted His-hABCD1; weak inhibition of the ATPase activity of liposome-reconstituted His-hABCD2
p-chloromercuribenzoic acid
the acyl?CoA thioesterase activity of ABCD1 is inhibited by 1 mM p-chloromercuribenzoic acid
siRNA
-
RNAi technique is used to knockdown the ABCD3 gene encoding PMP70
-
additional information
no inhibition of the ATPase activity of liposome-reconstituted His-hABCD1 by NaN3, EGTA or ouabain
-
additional information
no inhibition of the ATPase activity of liposome-reconstituted His-hABCD1 by NaN3, EGTA or ouabain
-
additional information
no inhibition of the ATPase activity of liposome-reconstituted His-hABCD1 by NaN3, EGTA or ouabain
-
additional information
-
the ATPase activity of ALDP-His is insensitive to oligomycin, azide and vanadate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Pex19p
-
protein required for the peroxisomal membrane synthesis, binds to PMP70 co-translationally and keeps PMP70 in a proper conformation for the localization to peroxisome, PMP70 forms 75% aggregates during translation in the absence of Pex19p
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0743
-
ALDRP-His, membrane fractions (about 10 mg of membrane protein) are incubated at 37°C in 0.1 ml of 40 mM Tris-HCl (pH 7.4) containing 0.1 mM EGTA, 1 mM dithiothreitol, 2mM ouabain and 15 mM MgSO4, and 5 mM NaATP
0.0774
-
ALDP-His, membrane fractions (about 10 mg of membrane protein) are incubated at 37°C in 0.1 ml of 40 mM Tris-HCl (pH 7.4) containing 0.1 mM EGTA, 1 mM dithiothreitol, 2mM ouabain and 15 mM MgSO4, and 5 mM NaATP
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Wistar rats, peroxisomal ABC transporters are encoded by the ABCD genes, ABCD1-ABCD3
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
SV40-transformed, from a patient with X-linked adrenoleukodystrophy missense mutation A626T
brenda
additional information
-
no expression is detected in embryos, neurons or glial-like cells
brenda
the microglial cells expressing ABCD2 chimeric homodimers (ABCD2-ABCD2 plus ABCD2-ABCD2-EGFP) also show tetramer formation of the proteins
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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
brenda
-
when the N-terminal 80-segment is fused to EGFP, the fusion protein is targeted to the outer mitochondrial membrane
brenda
the ABCD transporter contain six transmembrane helices (positions in sequence are analyzed) and a membrane peroxisomal targeting signal, direct involvement of this motif in peroxisomal targeting of ABCD1. The cytosolic helices form intracellular loops (ICLs), structure overview
brenda
the ABCD transporter contain six transmembrane helices (positions in sequence are analyzed) and a membrane peroxisomal targeting signal. The cytosolic helices form intracellular loops (ICLs), structure overview
brenda
the ABCD transporter contain six transmembrane helices (positions in sequence are analyzed) (TMH) and a membrane peroxisomal targeting signal, direct involvement of this motif in peroxisomal targeting of ABCD3. Peroxisomal targeting of ABCD3 seems to depend on the presence of this motif, the TMH 1 and 2, and also on several residues located in the first 60 amino acids (L21, L22, and L23) and near the TMH 5 (I307-L308). The cytosolic helices form intracellular loops (ICLs), structure overview
brenda
ABCD1 and its homologue ABCD2 exist mainly as homotetramers in the peroxisomal membrane, quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview
brenda
ABCD1 and its homologue ABCD2 exist mainly as homotetramers in the peroxisomal membrane, quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview
brenda
-
two peroxisomal half ABC transporters Pxa1p and Pxa2p form a heterodimeric complex in the peroxisomal membrane
brenda
-
two peroxisomal half ABC transporters Pxa1p and Pxa2p form a heterodimeric complex in the peroxisomal membrane
-
brenda
-
upon expression in Saccharomyces cerevisiae, CTS is correctly targeted to yeast peroxisomes, and assembled into the membrane with its nucleotide binding domains in the cytosol
brenda
-
when both the N-terminal 80-segment and the following TM1-TM2 region are present, the fusion protein locates exclusively to the peroxisome
brenda
-
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
brenda
-
transmembrane protein anchored in the peroxisomal membrane by its amino-terminal hydrophobic domain, possibly forming a channel, the ATP-binding domain is exposed to the cytosol
brenda
-
enzyme contains six membrane-spanning segments and a putative ATP-binding domain, the C-terminal hydrophilic domain of the enzyme is on the cytoplasmic surface of peroxisomes
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
physiological function
additional information
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)
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 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
ABCD1-3 belong to the ATP-binding cassette protein superfamily, subfamily D, membrane-bound proteins with highly conserved structure
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
malfunction
a patient with isoform ABCD3 defect exhibits hepatosplenomegaly and severe liver disease
malfunction
the export of cholesterol from lysosomes is reduced by the mutation of isoform ABCD1. Mutation of isoform ABCD1 causes X-linked adrenoleukodystrophy
malfunction
isoform ABCD1 dysfunction underlies toxic cytosolic accumulation of very long chain fatty acids, progressive demyelination, and neurological impairments including X-linked adrenoleukodystrophy
malfunction
-
enzyme loss induces lipid droplet accumulation and increases vulnerability to mitochondrial reactive oxygen species. Enzyme mutants show very long-chain fatty acids accumulation and impaired mitochondrial redox homeostasis, and axonal damage coupled to locomotor dysfunction
malfunction
-
the isoform Abcd3 knockout mouse presents with increased hepatic long-chain dicarboxylic fatty acids, increased urine medium-chain dicarboxylic fatty acids, lipodystrophy, enhanced hepatic cholesterol synthesis and decreased hepatic de novo lipogenesis
malfunction
enzyme dysfunction usually causes X-linked adrenoleukodystrophy
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
-
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
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
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
isoform ABCD3 plays a role in the import of bile acid intermediates, as well as pristanic acid and phytanic acid
physiological function
isoform ABCD1 is involved in the transport of saturated and unsaturated very long-chain fatty acid-CoA into peroxisomes
physiological function
isoform ABCD2 is involved in the transport of saturated and unsaturated very long-chain fatty acid-CoA into peroxisomes. Isoform ABCD2 has a central role in the metabolism of monounsaturated and polyunsaturated rather than saturated very long-chain fatty acids, and may be involved in the regulation of oxidative stress and synthesis of docosahexaenoic acid
physiological function
isoform ABCD1 is central to fatty acid catabolism and lipid biosynthesis
physiological function
-
the enzyme is important for the uptake of fatty acids and other beta-oxidation substrates into peroxisomes and provides an import pathway for free CoA in the peroxisomal lumen that controls peroxisomal CoA homeostasis
physiological function
-
the enzyme acting solely in the hypodermis rescues axonal and locomotion abnormalities, suggesting a myelin-like role for the hypodermis in providing essential peroxisomal functions for the nematode nervous system
physiological function
-
isoform ABCD3 plays a major role in hepatic dicarboxylic fatty acid metabolism and lipid homeostasis
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
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
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
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ABCD1_DROME
730
0
82639
Swiss-Prot
Mitochondrion (Reliability: 2)
ABCD3_HUMAN
659
0
75476
Swiss-Prot
Secretory Pathway (Reliability: 5)
PXA2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
853
0
97126
Swiss-Prot
-
PXA1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
870
0
100025
Swiss-Prot
other Location (Reliability: 5)
ABCD2_HUMAN
740
0
83233
Swiss-Prot
other Location (Reliability: 5)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
111000
monomer of EGFP-tagged ABCD2 protein, sucrose density sedimentation centrifugation analysis
215000 - 415000
tetramer of ABCD1 protein, sucrose density sedimentation centrifugation analysis
270000 - 515000
tetramer of EGFP-tagged ABCD2 protein, sucrose density sedimentation centrifugation analysis
300000 - 400000
-
PMP70, ALDP and ALDPR are found as large protein complexes upon sucrose density gradient centrifugation, since the sedimentation properties of a solubilized membrane protein also depend on its partial specific volume, shape and amount and type of protein-bound detergents/membrane lipids, no conclusions about regarding the true size of the observed protein complexes can be inferred
70000
75000
82000
monomer of ABCD1 protein, sucrose density sedimentation centrifugation analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
heterotetramer
homodimer
homotetramer
additional information
dimer
-
ALDP can form homodimers as well as heterodimers with the peroxisomal membrane protein PMP70
dimer
-
PMP70 can form homodimers as well as heterodimers with the adrenoleukodystrophy protein ALDP
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
-
ALDP can function as a homodimer and accepts a range of acyl-CoA esters
homodimer
-
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
-
ALDP, ALDRP and PMP70 have the structure of ABC half-transporters
additional information
-
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 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
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
-
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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
-
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
-
when the N-terminal 80-segment is fused to EGFP, the fusion protein is targeted to the outer mitochondrial membrane
additional information
-
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
-
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
-
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
-
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
-
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dimerization is considered as an obligatory step for stability and function of peroxisomal ABC transporters
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ALDP, preparative immunoprecipitation, PMP70, incubation in ATP-agarose and sucrose gradient centrifugation
-
anti-FLAG M2 affinity gel column chromatography and Superdex 200 gel filtration
recombinant His-tagged protein ABCD1 from Pichia pastoris strain SMD1168 by detergent solubilization and nickel affinity chromatography, evaluation of diverse detergents
recombinant His-tagged protein ABCD2 from Pichia pastoris strain SMD1168 by detergent solubilization and nickel affinity chromatography, evaluation of diverse detergents
recombinant His-tagged protein ABCD3 from Pichia pastoris strain SMD1168 by detergent solubilization and nickel affinity chromatography, evaluation of diverse detergents
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ABCD1, DNA and amino oacid sequence determination and analysis
-
gene ABCD1, recombinant expression of His-tagged protein ABCD1 in Pichia pastoris strain SMD1168
gene ABCD1, recombinant expression of the enzyme in COS-7 cells and in Rattus norvegicus H4IIEC3 hepatoma cell model
gene ABCD2, recombinant expression of protein ABCD2 in Pichia pastoris strain SMD1168
gene ABCD3, recombinant expression of protein ABCD3 in Pichia pastoris strain SMD1168
into the pMAM2-BSD, pEGFPN-1 and pcDNA4HisMax TOP vector for transfection of CHO cells, and as templates for the construction of mutant cDNAs
-
recombinant expression of EGFP-tagged enzyme in COS-7 cells and in Rattus norvegicus H4IIEC3 hepatoma cell model, microglial BV-2 cells expressing ABCD2 chimeric homodimers (ABCD2-ABCD2 plus ABCD2-ABCD2-EGFP) also show tetramer formation of the proteins
transfection of cDNA of rat PMP70 into Chineses hamster ovary cells and establishing of cell lines stably expressing PMP70
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged protein ABCD1 protein solubilization and reconstitution in proteoliposomes
recombinant His-tagged protein ABCD2 protein solubilization and reconstitution in proteoliposomes, the liposome-reconstituted His-hABCD1 shows ATPase activity
recombinant His-tagged protein ABCD3 protein solubilization and reconstitution in proteoliposomes
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
a correction of the biochemical defect of X-linked adrenoleukodystrophy could be possible by drug-induced overexpression or ectopic expression of adrenoleukodystrophy-related protein
medicine
-
a correction of the biochemical defect of X-linked adrenoleukodystrophy could be possible by drug-induced overexpression or ectopic expression of adrenoleukodystrophy-related protein
medicine
-
mutations in the gene encoding ALDP result in a devasting neurodegenerative disorder, X-linked adrenoleukodystrophy, X-ALD
medicine
-
mutations in the gene encoding ALDP result in a devasting neurodegenerative disorder, X-linked adrenoleukodystrophy, X-ALD
medicine
-
the finding that PMP70 over-expression partially corrected very long-chain fatty acid oxidation defects in fibroblasts of X-linked adrenoleukodystrophy patients, has unveiled its potential clinical relevance
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
265
4534-4540
1990
Rattus norvegicus
brenda
Hettema, E.H.; Tabak, H.F.
Transport of fatty acids and metabolites across the peroxisomal membrane
Biochim. Biophys. Acta
1486
18-27
2000
Saccharomyces cerevisiae
brenda
Contreras, M.; Sengupta, T.K.; Sheikh, F.; Aubourg, P.; Singh, I.
Topology of ATP-binding domain of adrenoleukodystrophy gene product in peroxisomes
Arch. Biochem. Biophys.
334
369-379
1996
Rattus norvegicus
brenda
Gartner, J.; Jimenez-Sanchez, G.; Roerig, P.; Valle, D.
Genomic organization of the 70-kDa peroxisomal membrane protein gene (PXMP1)
Genomics
48
203-208
1998
Homo sapiens
brenda
Hettema, E.H.; van Roermund, C.W.; Distel, B.; van den Berg, M.; Vilela, C.; Rodrigues-Pousada, C.; Wanders, R.J.; Tabak, H.F.
The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae
EMBO J.
15
3813-3822
1996
Saccharomyces cerevisiae
brenda
Imanaka, T.; Aihara, K.; Takano, T.; Yamashita, A.; Sato, R.; Suzuki, Y.; Yokota, S.; Osumi, T.
Characterization of the 70-kDa peroxisomal membrane protein, an ATP binding cassette transporter
J. Biol. Chem.
274
11968-11976
1999
Rattus norvegicus
brenda
Liu, L.X.; Janvier, K.; Berteaux-Lecellier, V.; Cartier, N.; Benarous, R.; Aubourg, P.
Homo- and heterodimerization of peroxisomal ATP-binding cassette half-transporters
J. Biol. Chem.
274
32738-32743
1999
Homo sapiens, Mus musculus
brenda
Netik, A.; Forss-Petter, S.; Holzinger, A.; Molzer, B.; Unterrainer, G.; Berger, J.
Adrenoleukodystrophy-related protein can compensate functionally for adrenoleukodystrophy protein deficiency (X-ALD): implications for therapy
Hum. Mol. Genet.
8
907-913
1999
Homo sapiens, Mus musculus
brenda
Shani, N.; Valle, D.
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
11901-11906
1996
Saccharomyces cerevisiae, Homo sapiens
brenda
Verleur, N.; Hettema, E.H.; van Roermund, C.W.; Tabak, H.F.; Wanders, R.J.
Transport of activated fatty acids by the peroxisomal ATP-binding-cassette transporter Pxa2 in a semi-intact yeast cell system
Eur. J. Biochem.
249
657-661
1997
Saccharomyces cerevisiae, Saccharomyces cerevisiae Pxa2p
brenda
Van Roermund, C.W.T.; de Jong, M.; Ijlst, L.; van Marle, J.; Dansen, T.B.; Wanders, R.J.A.; Waterham, H.R.
The peroxisomal lumen in Saccharomyces cerevisiae is alkaline
J. Cell Sci.
117
4231-4237
2004
Saccharomyces cerevisiae
brenda
Hayashi, M.; Nito, K.; Takei-Hoshi, R.; Yagi, M.; Kondo, M.; Suenaga, A.; Yamaya, T.; Nishimura, M.
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
Biochem. Biophys. Res. Commun.
341
150-157
2006
Rattus norvegicus
brenda
Guimaraes, C.P.; Domingues, P.; Aubourg, P.; Fouquet, F.; Pujol, A.; Jimenez-Sanchez, G.; Sa-Miranda, C.; Azevedo, J.E.
Mouse liver PMP70 and ALDP: homomeric interactions prevail in vivo
Biochim. Biophys. Acta
1689
235-243
2004
Mus musculus
brenda
Kashiwayama, Y.; Asahina, K.; Shibata, H.; Morita, M.; Muntau, A.C.; Roscher, A.A.; Wanders, R.J.; Shimozawa, N.; Sakaguchi, M.; Kato, H.; Imanaka, T.
Role of Pex19p in the targeting of PMP70 to peroxisome
Biochim. Biophys. Acta
1746
116-128
2005
Homo sapiens
brenda
Morita, M.; Kurisu, M.; Kashiwayama, Y.; Yokota, S.; Imanaka, T.
ATP-binding and -hydrolysis activities of ALDP (ABCD1) and ALDRP (ABCD2), human peroxisomal ABC proteins, overexpressed in Sf21 cells
Biol. Pharm. Bull.
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
26997-27005
2007
Homo sapiens
brenda
Takahashi, N.; Morita, M.; Maeda, T.; Harayama, Y.; Shimozawa, N.; Suzuki, Y.; Furuya, H.; Sato, R.; Kashiwayama, Y.; Imanaka, T.
Adrenoleukodystrophy: subcellular localization and degradation of adrenoleukodystrophy protein (ALDP/ABCD1) with naturally occurring missense mutations
J. Neurochem.
101
1632-1643
2007
Homo sapiens
brenda
Kemp, S.; Wanders, R.J.
X-linked adrenoleukodystrophy: very long-chain fatty acid metabolism, ABC half-transporters and the complicated route to treatment
Mol. Genet. Metab.
90
268-276
2007
Mammalia, Saccharomyces cerevisiae
brenda
Di Benedetto, R.; Denti, M.A.; Salvati, S.; Sanchez, M.; Attorri, L.; David, G.; Di Biase, A.
RNAi-mediated silencing of ABCD3 gene expression in rat C6 glial cells: a model system to study PMP70 function
Neurochem. Int.
52
1106-1113
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
FASEB J.
22
4201-4208
2008
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
Fungal Genet. Biol.
46
55-66
2009
Podospora anserina, Podospora anserina (Q7Z9L6)
brenda
Iwashita, S.; Tsuchida, M.; Tsukuda, M.; Yamashita, Y.; Emi, Y.; Kida, Y.; Komori, M.; Kashiwayama, Y.; Imanaka, T.; Sakaguchi, M.
Multiple organelle-targeting signals in the N-terminal portion of peroxisomal membrane protein PMP70
J. Biochem.
147
581-590
2010
Homo sapiens
brenda
Kanai, M.; Nishimura, M.; Hayashi, M.
A peroxisomal ABC transporter promotes seed germination by inducing pectin degradation under the control of ABI5
Plant J.
62
936-947
2010
Arabidopsis thaliana
brenda
van Roermund, C.W.; Visser, W.F.; Ijlst, L.; Waterham, H.R.; Wanders, R.J.
Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid ?-oxidation
Biochim. Biophys. Acta
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
J. Biol. Chem.
285
29892-29902
2010
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
J. Biol. Chem.
287
20144-20153
2012
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.
Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane
J. Biol. Chem.
287
210-221
2012
Homo sapiens
brenda
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 (P33897), Homo sapiens (P28288), 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.
Peroxisomes can oxidize medium- and long-chain fatty acids through a pathway involving ABCD3 and HSD17B4
FASEB J.
33
4355-4364
2019
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
2017
Homo sapiens (P33897), Homo sapiens (P28288), 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
2017
Mus musculus (P48410), Mus musculus (Q61285)
brenda
Imanaka, T.
Biogenesis and function of peroxisomes in human disease with a focus on the ABC transporter
Biol. Pharm. Bull.
42
649-665
2019
Homo sapiens (P33897), Homo sapiens (P28288), Homo sapiens (Q9UBJ2)
brenda
Le, L.T.M.; Thompson, J.R.; Dang, P.X.; Bhandari, J.; Alam, A.
Structures of the human peroxisomal fatty acid transporter ABCD1 in a lipid environment
Commun. Biol.
5
7-7
2022
Homo sapiens (P33897)
brenda
van Roermund, C.W.T.; IJlst, L.; Baker, A.; Wanders, R.J.A.; Theodoulou, F.L.; Waterham, H.R.
The Saccharomyces cerevisiae ABC subfamily D transporter Pxa1/Pxa2p co-imports CoASH into the peroxisome
FEBS Lett.
595
763-772
2021
Saccharomyces cerevisiae
brenda
Coppa, A.; Guha, S.; Fourcade, S.; Parameswaran, J.; Ruiz, M.; Moser, A.B.; Schlueter, A.; Murphy, M.P.; Lizcano, J.M.; Miranda-Vizuete, A.; Dalfo, E.; Pujol, A.
The peroxisomal fatty acid transporter ABCD1/PMP-4 is required in the C. elegans hypodermis for axonal maintenance A worm model for adrenoleukodystrophy
Free Radic. Biol. Med.
152
797-809
2020
Caenorhabditis elegans
brenda
van Roermund, C.W.T.; IJlst, L.; Linka, N.; Wanders, R.J.A.; Waterham, H.R.
Peroxisomal ATP uptake is provided by two adenine nucleotide transporters and the ABCD transporters
Front. Cell Dev. Biol.
9
788921
2021
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ1991
brenda
Ranea-Robles, P.; Chen, H.; Stauffer, B.; Yu, C.; Bhattacharya, D.; Friedman, S.L.; Puchowicz, M.; Houten, S.M.
The peroxisomal transporter ABCD3 plays a major role in hepatic dicarboxylic fatty acid metabolism and lipid homeostasis
J. Inherit. Metab. Dis.
44
1419-1433
2021
Mus musculus
brenda
Chen, Z.P.; Xu, D.; Wang, L.; Mao, Y.X.; Li, Y.; Cheng, M.T.; Zhou, C.Z.; Hou, W.T.; Chen, Y.
Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1
Nat. Commun.
13
3299
2022
Homo sapiens (P33897)
brenda
Kawaguchi, K.; Mukai, E.; Watanabe, S.; Yamashita, A.; Morita, M.; So, T.; Imanaka, T.
Acyl-CoA thioesterase activity of peroxisomal ABC protein ABCD1 is required for the transport of very long-chain acyl-CoA into peroxisomes
Sci. Rep.
11
2192
2021
Homo sapiens (P33897)
brenda
EXTERNAL LINKS (specific for EC-Number 7.6.2.4)
Transporter Classification Database (TCDB): 3.A.1.203.5
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