Enzymes
| UniProtKB help_outline | 4 proteins |
Reaction participants Show >> << Hide
- Name help_outline 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine Identifier CHEBI:72999 (CAS: 63-89-8,2644-64-6) help_outline Charge 0 Formula C40H80NO8P InChIKeyhelp_outline KILNVBDSWZSGLL-KXQOOQHDSA-N SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCCCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 23 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
all-trans-retinol--[retinol-binding protein]
Identifier
RHEA-COMP:14428
Reactive part
help_outline
- Name help_outline all-trans-retinol Identifier CHEBI:17336 (Beilstein: 403040; CAS: 11103-57-4,68-26-8) help_outline Charge 0 Formula C20H30O InChIKeyhelp_outline FPIPGXGPPPQFEQ-OVSJKPMPSA-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 29 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an L-α amino acid residue Identifier CHEBI:83228 Charge 0 Formula C2H2NOR SMILEShelp_outline [*][C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 551 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-hexadecanoyl-sn-glycero-3-phosphocholine Identifier CHEBI:76078 Charge 0 Formula C24H50NO7P InChIKeyhelp_outline NEGQHKSYEYVFTD-HSZRJFAPSA-N SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)O[C@H](CO)COP([O-])(=O)OCC[N+](C)(C)C 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline all-trans-retinyl hexadecanoate Identifier CHEBI:17616 (CAS: 79-81-2) help_outline Charge 0 Formula C36H60O2 InChIKeyhelp_outline VYGQUTWHTHXGQB-FFHKNEKCSA-N SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)OC\C=C(C)\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 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
apo--[retinol-binding protein]
Identifier
RHEA-COMP:14426
Reactive part
help_outline
- Name help_outline an L-α amino acid residue Identifier CHEBI:83228 Charge 0 Formula C2H2NOR SMILEShelp_outline [*][C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 551 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:56244 | RHEA:56245 | RHEA:56246 | RHEA:56247 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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An acyl-covalent enzyme intermediate of lecithin:retinol acyltransferase.
Golczak M., Palczewski K.
Synthesis of fatty acid retinyl esters determines systemic vitamin A levels and provides substrate for production of visual chromophore (11-cis-retinal) in vertebrates. Lecithin:retinol acyltransferase (LRAT), the main enzyme responsible for retinyl ester formation, catalyzes the transfer of an ac ... >> More
Synthesis of fatty acid retinyl esters determines systemic vitamin A levels and provides substrate for production of visual chromophore (11-cis-retinal) in vertebrates. Lecithin:retinol acyltransferase (LRAT), the main enzyme responsible for retinyl ester formation, catalyzes the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol. To delineate the catalytic mechanism of this reaction, we expressed and purified a fully active, soluble form of this enzyme and used it to examine the possible formation of a transient acyl-enzyme intermediate. Detailed mass spectrometry analyses revealed that LRAT undergoes spontaneous, covalent modification upon incubation with a variety of phosphatidylcholine substrates. The addition of an acyl chain occurs at the Cys(161) residue, indicating formation of a thioester intermediate. This observation provides the first direct experimental evidence of thioester intermediate formation that constitutes the initial step in the proposed LRAT catalytic reaction. Additionally, we examined the effect of increasing fatty acyl side chain length in phosphatidylcholine on substrate accessibility in this reaction, which provided insights into the function of the single membrane-spanning domain of LRAT. These observations are critical to understanding the catalytic mechanism of LRAT protein family members as well as other lecithin:acyltransferases wherein Cys residues are required for catalysis. << Less
J. Biol. Chem. 285:29217-29222(2010) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.