Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline 9-cis-retinol Identifier CHEBI:78272 (CAS: 22737-97-9) help_outline Charge 0 Formula C20H30O InChIKeyhelp_outline FPIPGXGPPPQFEQ-MKOSUFFBSA-N SMILEShelp_outline C\C(=C/CO)\C=C\C=C(\C)/C=C/C1=C(C)CCCC1(C)C 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a fatty acyl-CoA Identifier CHEBI:77636 Charge -4 Formula C22H31N7O17P3SR 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)NCCSC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,243 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 9-cis-retinyl ester Identifier CHEBI:195360 Charge 0 Formula C21H29O2R SMILEShelp_outline C1CCC(=C(\C=C\C(=C/C=C/C(=C/COC(*)=O)/C)\C)C1(C)C)C 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 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 1,468 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:78263 | RHEA:78264 | RHEA:78265 | RHEA:78266 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Allosteric modulation of the substrate specificity of acyl-CoA wax alcohol acyltransferase 2.
Arne J.M., Widjaja-Adhi M.A., Hughes T., Huynh K.W., Silvaroli J.A., Chelstowska S., Moiseenkova-Bell V.Y., Golczak M.
The esterification of alcohols with fatty acids is a universal mechanism to form inert storage forms of sterols, di- and triacylglycerols, and retinoids. In ocular tissues, formation of retinyl esters is an essential step in the enzymatic regeneration of the visual chromophore (11-<i>cis</i>-retin ... >> More
The esterification of alcohols with fatty acids is a universal mechanism to form inert storage forms of sterols, di- and triacylglycerols, and retinoids. In ocular tissues, formation of retinyl esters is an essential step in the enzymatic regeneration of the visual chromophore (11-<i>cis</i>-retinal). Acyl-CoA wax alcohol acyltransferase 2 (AWAT2), also known as multifunctional <i>O</i>-acyltransferase (MFAT), is an integral membrane enzyme with a broad substrate specificity that has been shown to preferentially esterify 11-<i>cis</i>-retinol and thus contribute to formation of a readily available pool of <i>cis</i> retinoids in the eye. However, the mechanism by which this promiscuous enzyme can gain substrate specificity is unknown. Here, we provide evidence for an allosteric modulation of the enzymatic activity by 11-<i>cis</i> retinoids. This regulation is independent from cellular retinaldehyde-binding protein (CRALBP), the major <i>cis</i>-retinoid binding protein. This positive-feedback regulation leads to decreased esterification rates for 9-<i>cis</i>, 13-<i>cis</i>, or all-<i>trans</i> retinols and thus enables preferential synthesis of 11-<i>cis</i>-retinyl esters. Finally, electron microscopy analyses of the purified enzyme indicate that this allosteric effect does not result from formation of functional oligomers. Altogether, these data provide the experimental basis for understanding regulation of AWAT2 substrate specificity. << Less
J. Lipid Res. 58:719-730(2017) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.