Enzymes
| UniProtKB help_outline | 1,400 proteins |
Reaction participants Show >> << Hide
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-octadecanoyl-L-phenylalanine Identifier CHEBI:149700 Charge -1 Formula C27H44NO3 InChIKeyhelp_outline PHZQULSGYVCYNC-VWLOTQADSA-M SMILEShelp_outline N([C@H](C([O-])=O)CC1=CC=CC=C1)C(CCCCCCCCCCCCCCCCC)=O 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 L-phenylalanine Identifier CHEBI:58095 Charge 0 Formula C9H11NO2 InChIKeyhelp_outline COLNVLDHVKWLRT-QMMMGPOBSA-N SMILEShelp_outline [NH3+][C@@H](Cc1ccccc1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 72 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline octadecanoate Identifier CHEBI:25629 (Beilstein: 3590530; CAS: 646-29-7) help_outline Charge -1 Formula C18H35O2 InChIKeyhelp_outline QIQXTHQIDYTFRH-UHFFFAOYSA-M SMILEShelp_outline C(CCCCCCCCCC)CCCCCCC(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 38 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:64128 | RHEA:64129 | RHEA:64130 | RHEA:64131 | |
|---|---|---|---|---|
| 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
-
Cooperative enzymatic control of N-acyl amino acids by PM20D1 and FAAH.
Kim J.T., Terrell S.M., Li V.L., Wei W., Fischer C.R., Long J.Z.
The N-acyl amino acids are a family of bioactive lipids with pleiotropic physiologic functions, including in energy homeostasis. Their endogenous levels are regulated by an extracellular mammalian N-acyl amino acid synthase/hydrolase called PM20D1 (peptidase M20 domain containing 1). Using an acti ... >> More
The N-acyl amino acids are a family of bioactive lipids with pleiotropic physiologic functions, including in energy homeostasis. Their endogenous levels are regulated by an extracellular mammalian N-acyl amino acid synthase/hydrolase called PM20D1 (peptidase M20 domain containing 1). Using an activity-guided biochemical approach, we report the molecular identification of fatty acid amide hydrolase (FAAH) as a second intracellular N-acyl amino acid synthase/hydrolase. In vitro, FAAH exhibits a more restricted substrate scope compared to PM20D1. In mice, genetic ablation or selective pharmacological inhibition of FAAH bidirectionally dysregulates intracellular, but not circulating, N-acyl amino acids. Dual blockade of both PM20D1 and FAAH reveals a dramatic and non-additive biochemical engagement of these two enzymatic pathways. These data establish FAAH as a second intracellular pathway for N-acyl amino acid metabolism and underscore enzymatic division of labor as an enabling strategy for the regulation of a structurally diverse bioactive lipid family. << Less
Elife 9:0-0(2020) [PubMed] [EuropePMC]
This publication is cited by 22 other entries.