Enzymes
| UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol Identifier CHEBI:144774 Charge 0 Formula C23H36O6R2 SMILEShelp_outline O(C[C@@](COC(*)=O)(OC(=O)*)[H])C(*)=O 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
- Name help_outline N-(32-hydroxydotriacontanoyl)-sphing-4-enine Identifier CHEBI:157644 Charge 0 Formula C50H99NO4 InChIKeyhelp_outline KTUFFKGQVWCEJY-FUEXHLDUSA-N SMILEShelp_outline C(CCCCCCCCCC)CC\C=C\[C@@H](O)[C@@H](NC(=O)CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCO)CO 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a diacylglycerol Identifier CHEBI:18035 Charge 0 Formula C5H6O5R2 SMILEShelp_outline [*]OCC(CO[*])O[*] 2D coordinates Mol file for the small molecule Search links Involved in 378 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-(32-(9Z,12Z-octadecadienoyloxy)-dotricontanoyl)-sphing-4-enine Identifier CHEBI:157653 Charge 0 Formula C68H129NO5 InChIKeyhelp_outline NKZDGPMKCOVGRH-ARKMRHPDSA-N SMILEShelp_outline [C@H]([C@@H](/C=C/CCCCCCCCCCCCC)O)(NC(=O)CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCOC(CCCCCCC/C=C\C/C=C\CCCCC)=O)CO 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:65652 | RHEA:65653 | RHEA:65654 | RHEA:65655 | |
|---|---|---|---|---|
| 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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PNPLA1 has a crucial role in skin barrier function by directing acylceramide biosynthesis.
Hirabayashi T., Anjo T., Kaneko A., Senoo Y., Shibata A., Takama H., Yokoyama K., Nishito Y., Ono T., Taya C., Muramatsu K., Fukami K., Munoz-Garcia A., Brash A.R., Ikeda K., Arita M., Akiyama M., Murakami M.
Mutations in patatin-like phospholipase domain-containing 1 (PNPLA1) cause autosomal recessive congenital ichthyosis, but the mechanism involved remains unclear. Here we show that PNPLA1, an enzyme expressed in differentiated keratinocytes, plays a crucial role in the biosynthesis of ω-O-acylceram ... >> More
Mutations in patatin-like phospholipase domain-containing 1 (PNPLA1) cause autosomal recessive congenital ichthyosis, but the mechanism involved remains unclear. Here we show that PNPLA1, an enzyme expressed in differentiated keratinocytes, plays a crucial role in the biosynthesis of ω-O-acylceramide, a lipid component essential for skin barrier. Global or keratinocyte-specific Pnpla1-deficient neonates die due to epidermal permeability barrier defects with severe transepidermal water loss, decreased intercellular lipid lamellae in the stratum corneum, and aberrant keratinocyte differentiation. In Pnpla1<sup>-/-</sup> epidermis, unique linoleate-containing lipids including acylceramides, acylglucosylceramides and (O-acyl)-ω-hydroxy fatty acids are almost absent with reciprocal increases in their putative precursors, indicating that PNPLA1 catalyses the ω-O-esterification with linoleic acid to form acylceramides. Moreover, acylceramide supplementation partially rescues the altered differentiation of Pnpla1<sup>-/-</sup> keratinocytes. Our findings provide valuable insight into the skin barrier formation and ichthyosis development, and may contribute to novel therapeutic strategies for treatment of epidermal barrier defects. << Less
Nat. Commun. 8:14609-14609(2017) [PubMed] [EuropePMC]
This publication is cited by 9 other entries.