Reaction participants Show >> << Hide
- Name help_outline 3-methyl-(2E)-butenoyl-CoA Identifier CHEBI:57344 Charge -4 Formula C26H38N7O17P3S InChIKeyhelp_outline BXIPALATIYNHJN-ZMHDXICWSA-J SMILEShelp_outline CC(C)=CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6-carboxybiotinyl-L-lysyl-[protein]
Identifier
RHEA-COMP:10506
Reactive part
help_outline
- Name help_outline carboxybiotinyl-L-lysine residue Identifier CHEBI:83145 Charge -1 Formula C17H25N4O5S SMILEShelp_outline [O-]C(=O)N1[C@H]2CS[C@@H](CCCCC(=O)NCCCC[C@H](N-*)C(-*)=O)[C@H]2NC1=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-methyl-(2E)-glutaconyl-CoA Identifier CHEBI:57346 Charge -5 Formula C27H37N7O19P3S InChIKeyhelp_outline GXKSHRDAHFLWPN-RKYLSHMCSA-I SMILEShelp_outline C\C(CC([O-])=O)=C/C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)N1C=NC2=C1N=CN=C2N 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6-biotinyl-L-lysyl-[protein]
Identifier
RHEA-COMP:10505
Reactive part
help_outline
- Name help_outline N6-biotinyl-L-lysine residue Identifier CHEBI:83144 Charge 0 Formula C16H26N4O3S SMILEShelp_outline *-N[C@@H](CCCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13025 | RHEA:13026 | RHEA:13027 | RHEA:13028 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Characterization of the mycobacterial acyl-CoA carboxylase holo complexes reveals their functional expansion into amino acid catabolism.
Ehebauer M.T., Zimmermann M., Jakobi A.J., Noens E.E., Laubitz D., Cichocki B., Marrakchi H., Laneelle M.A., Daffe M., Sachse C., Dziembowski A., Sauer U., Wilmanns M.
Biotin-mediated carboxylation of short-chain fatty acid coenzyme A esters is a key step in lipid biosynthesis that is carried out by multienzyme complexes to extend fatty acids by one methylene group. Pathogenic mycobacteria have an unusually high redundancy of carboxyltransferase genes and biotin ... >> More
Biotin-mediated carboxylation of short-chain fatty acid coenzyme A esters is a key step in lipid biosynthesis that is carried out by multienzyme complexes to extend fatty acids by one methylene group. Pathogenic mycobacteria have an unusually high redundancy of carboxyltransferase genes and biotin carboxylase genes, creating multiple combinations of protein/protein complexes of unknown overall composition and functional readout. By combining pull-down assays with mass spectrometry, we identified nine binary protein/protein interactions and four validated holo acyl-coenzyme A carboxylase complexes. We investigated one of these--the AccD1-AccA1 complex from Mycobacterium tuberculosis with hitherto unknown physiological function. Using genetics, metabolomics and biochemistry we found that this complex is involved in branched amino-acid catabolism with methylcrotonyl coenzyme A as the substrate. We then determined its overall architecture by electron microscopy and found it to be a four-layered dodecameric arrangement that matches the overall dimensions of a distantly related methylcrotonyl coenzyme A holo complex. Our data argue in favor of distinct structural requirements for biotin-mediated γ-carboxylation of α-β unsaturated acid esters and will advance the categorization of acyl-coenzyme A carboxylase complexes. Knowledge about the underlying structural/functional relationships will be crucial to make the target category amenable for future biomedical applications. << Less
PLoS Pathog. 11:e1004623-e1004623(2015) [PubMed] [EuropePMC]