Any feedback?
Literature summary extracted from
- Peroxisomal ATP-binding cassette transporters form mainly tetramers (2017), J. Biol. Chem., 292, 6965-6977 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.6.2.4 | gene ABCD1, recombinant expression of the enzyme in COS-7 cells and in Rattus norvegicus H4IIEC3 hepatoma cell model | Mus musculus |
| 7.6.2.4 | 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 | Mus musculus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.6.2.4 | peroxisomal membrane | ABCD1 and its homologue ABCD2 exist mainly as homotetramers in the peroxisomal membrane, quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview | Mus musculus | 5778 | - |
| 7.6.2.4 | peroxisomal membrane | ABCD1 and its homologue ABCD2 exist mainly as homotetramers in the peroxisomal membrane, quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview | Mus musculus | 5778 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.6.2.4 | Mg2+ | required | Mus musculus |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.4 | 82000 | - |
monomer of ABCD1 protein, sucrose density sedimentation centrifugation analysis | Mus musculus |
| 7.6.2.4 | 111000 | - |
monomer of EGFP-tagged ABCD2 protein, sucrose density sedimentation centrifugation analysis | Mus musculus |
| 7.6.2.4 | 215000 | 415000 | tetramer of ABCD1 protein, sucrose density sedimentation centrifugation analysis | Mus musculus |
| 7.6.2.4 | 270000 | 515000 | tetramer of EGFP-tagged ABCD2 protein, sucrose density sedimentation centrifugation analysis | Mus musculus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.6.2.4 | ATP + H2O + fatty acyl CoA[side 1] | Mus musculus | - |
ADP + phosphate + fatty acyl CoA[side 2] | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.6.2.4 | Mus musculus | P48410 | - |
- |
| 7.6.2.4 | Mus musculus | Q61285 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 7.6.2.4 | BV-2 cell | - |
Mus musculus | - |
| 7.6.2.4 | BV-2 cell | the microglial cells expressing ABCD2 chimeric homodimers (ABCD2-ABCD2 plus ABCD2-ABCD2-EGFP) also show tetramer formation of the proteins | Mus musculus | - |
| 7.6.2.4 | microglial cell line | - |
Mus musculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.6.2.4 | ATP + H2O + fatty acyl CoA[side 1] | - |
Mus musculus | ADP + phosphate + fatty acyl CoA[side 2] | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.6.2.4 | heterotetramer | quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview | Mus musculus |
| 7.6.2.4 | heterotetramer | quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview | Mus musculus |
| 7.6.2.4 | homodimer | quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview | Mus musculus |
| 7.6.2.4 | homodimer | quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview | Mus musculus |
| 7.6.2.4 | homotetramer | quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview | Mus musculus |
| 7.6.2.4 | homotetramer | quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview | Mus musculus |
| 7.6.2.4 | More | 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 | Mus musculus |
| 7.6.2.4 | More | 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 | Mus musculus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.6.2.4 | ABCD1 | - |
Mus musculus |
| 7.6.2.4 | ABCD2 | - |
Mus musculus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.6.2.4 | ATP | - |
Mus musculus | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.6.2.4 | 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 | Mus musculus |
| 7.6.2.4 | 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 | Mus musculus |
| 7.6.2.4 | 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 | Mus musculus |
| 7.6.2.4 | 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 | Mus musculus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
