Reaction participants Show >> << Hide
- Name help_outline (13Z)-docosenoate Identifier CHEBI:32393 Charge -1 Formula C22H41O2 InChIKeyhelp_outline DPUOLQHDNGRHBS-KTKRTIGZSA-M SMILEShelp_outline CCCCCCCC\C=C/CCCCCCCCCCCC([O-])=O 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
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,355 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(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)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,623 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (13Z)-docosenoyl-CoA Identifier CHEBI:74068 Charge -4 Formula C43H72N7O17P3S InChIKeyhelp_outline OWGHRDKRIGXBJM-SPZFTOIUSA-J SMILEShelp_outline CCCCCCCC\C=C/CCCCCCCCCCCC(=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 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AMP Identifier CHEBI:456215 Charge -2 Formula C10H12N5O7P InChIKeyhelp_outline UDMBCSSLTHHNCD-KQYNXXCUSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 545 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,211 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:83111 | RHEA:83112 | RHEA:83113 | RHEA:83114 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Acyl-CoA synthetase activity of rat liver microsomes. Substrate specificity with special reference to very-long-chain and isomeric fatty acids.
Normann P.T., Thomassen M.S., Christiansen E.N., Flatmark T.
1. A fatty acid-depleted rat liver microsomal fraction has been used for the measurement of acyl-CoA synthetase (acid : CoA ligase (AMP-forming), EC 6.2.1.3) activity. The assay was based on measurement of the reaction product AMP by high-performance liquid chromatography (HPLC). The synthetase ac ... >> More
1. A fatty acid-depleted rat liver microsomal fraction has been used for the measurement of acyl-CoA synthetase (acid : CoA ligase (AMP-forming), EC 6.2.1.3) activity. The assay was based on measurement of the reaction product AMP by high-performance liquid chromatography (HPLC). The synthetase activity (V') revealed an optimum at 12 : 0 with saturated fatty acids as substrate, and at 14 : 1 with mono-unsaturated fatty acids. The apparent Michaelis constant, on the other hand, showed no systematic dependence on the fatty acid chain-length. 2. The mono-unsaturated fatty acids from 14 : 1 to 22 : 1 gave higher activities than the corresponding saturated fatty acids, and the relative differences were greatest with the very-long-chain fatty acids eicosaenoic (20 : 1 (11) (cis)) and docosaenoic acid (22 : 1 (11) (cis)). The synthetase activity with saturated and mono-unsaturated fatty acids was found to correlate to their capacity factor (k') on reversed phase chromatography (HPLC). This finding may indicate that the observed chain-length dependence of the activity largely reflects the partition of the fatty acids between a hydrophobic and a hydrophilic phase. In general, the position of the double bond and the cis/trans configuration had little effect on the V' values except for 22 : 1 (11)(cis) which revealed a 2-fold higher activity tha 22 : 1 (13) (cis). 3. The polyunsaturated fatty acid 22 : 6 (all cis) ;was notably found to be a much better substrate than other C22 fatty acids. 4. The present study does not support the idea of more than a single ATP-dependent acyl-CoA synthetase in the rat liver microsomal fraction. << Less
-
The oxidation of erucic acid by rat heart mitochondria.
Swarttouw M.A.
-
In vitro conversion of erucic acid by microsomes and mitochondria from liver, kidneys and heart of rats.
Clouet P., Bezard J.
Microsomes and mitochondria of liver, kidneys, and heart were incubated with [14-(14)C] erucic acid in three assay media: one favorable for chain elongation (NADPH + KCN), another favorable for beta-oxidation and the last one for shortening (NADP + KCN). Elongating reactions occurred mainly in mic ... >> More
Microsomes and mitochondria of liver, kidneys, and heart were incubated with [14-(14)C] erucic acid in three assay media: one favorable for chain elongation (NADPH + KCN), another favorable for beta-oxidation and the last one for shortening (NADP + KCN). Elongating reactions occurred mainly in microsomes, those of kidneys being very active; the mitochondria also showed some activity, heart mitochondria being, however, more active than the microsomes, when considering the amount of erucic acid activated. In the medium for beta-oxidation, practically no shortened fatty acids were found. On the contrary, when beta-oxidation was inhibited, and in the presence of NADP, the formation of shorter monoenes, probably in the outer membrane of the mitochondria, was observed, namely eicosenoic acid in high amount, oleic acid and hexadecenoic acid. Mitochondria from liver were very active as were those of heart, when compared with the quantity of activated erucic acid. In heart, the mitochondria shortened erucic acid into oleic acid and hexadecenoic acid, which were then probably used as energy substrates. With carnitine and without NADP, shortened fatty acids were formed in the mitochondria of liver, probably by the first reactions of beta-oxidation. In this case, the proportions of oleic acid and hexadecenoic acid were higher than with NADP alone. In the presence of carnitine and NADP, the level of the chain-shortening reaction did not differ from that observed with NADP alone. It appears, therefore, that the activated erucic acid is mainly directed towards shortening reactions and not towards transfer reactions across the mitochondrial membranes. << Less
Comments
Activity catalyzed by enzymes such as ACSL1, ACSL3 and ACSL5, and even though not proven experimentally with this particular substrate, we can infer it would catalyze this reaction.