Enzymes
| UniProtKB help_outline | 1,442 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 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine Identifier CHEBI:149697 Charge -1 Formula C23H36NO4 InChIKeyhelp_outline FQUVPTVNRMUOPO-UPQKDGGNSA-M SMILEShelp_outline C(CCC)C/C=C\C/C=C\C/C=C\C/C=C\CCCC(N[C@H](C(=O)[O-])CO)=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 (5Z,8Z,11Z,14Z)-eicosatetraenoate Identifier CHEBI:32395 (Beilstein: 5439048) help_outline Charge -1 Formula C20H31O2 InChIKeyhelp_outline YZXBAPSDXZZRGB-DOFZRALJSA-M SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 83 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-serine Identifier CHEBI:33384 Charge 0 Formula C3H7NO3 InChIKeyhelp_outline MTCFGRXMJLQNBG-REOHCLBHSA-N SMILEShelp_outline [NH3+][C@@H](CO)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 78 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:64116 | RHEA:64117 | RHEA:64118 | RHEA:64119 | |
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| 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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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.