Enzymes
UniProtKB help_outline | 6 proteins |
Reaction participants Show >> << Hide
- Name help_outline 1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine Identifier CHEBI:138218 Charge 0 Formula C39H78NO8P InChIKeyhelp_outline YSFFAUPDXKTJMR-DIPNUNPCSA-N SMILEShelp_outline P(OC[C@@H](COC(CCCCCCCCCCCCCCCC)=O)OC(CCCCCCCCCCCCCCCC)=O)(=O)(OCC[NH3+])[O-] 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine Identifier CHEBI:74667 (CAS: 6753-55-5) help_outline Charge 0 Formula C42H82NO8P InChIKeyhelp_outline RRVPPYNAZJRZFR-VYOBOKEXSA-N SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC\C=C/CCCCCCCC)COP([O-])(=O)OCC[N+](C)(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 1,2-diheptadecanoyl-sn-glycero-3-phospho-N-(9Z-octadecenoyl)-ethanolamine Identifier CHEBI:138222 Charge -1 Formula C57H109NO9P InChIKeyhelp_outline PCUGWEAIXCPPIT-JRTFMWKKSA-M SMILEShelp_outline N(CCOP(OC[C@@H](COC(CCCCCCCCCCCCCCCC)=O)OC(CCCCCCCCCCCCCCCC)=O)(=O)[O-])C(=O)CCCCCCC/C=C\CCCCCCCC 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 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 H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:53528 | RHEA:53529 | RHEA:53530 | RHEA:53531 | |
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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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Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins.
Golczak M., Kiser P.D., Sears A.E., Lodowski D.T., Blaner W.S., Palczewski K.
Lecithin:retinol acyltransferase-like proteins, also referred to as HRAS-like tumor suppressors, comprise a vertebrate subfamily of papain-like or NlpC/P60 thiol proteases that function as phospholipid-metabolizing enzymes. HRAS-like tumor suppressor 3, a representative member of this group, plays ... >> More
Lecithin:retinol acyltransferase-like proteins, also referred to as HRAS-like tumor suppressors, comprise a vertebrate subfamily of papain-like or NlpC/P60 thiol proteases that function as phospholipid-metabolizing enzymes. HRAS-like tumor suppressor 3, a representative member of this group, plays a key role in regulating triglyceride accumulation and energy expenditure in adipocytes and therefore constitutes a novel pharmacological target for treatment of metabolic disorders causing obesity. Here, we delineate a catalytic mechanism common to lecithin:retinol acyltransferase-like proteins and provide evidence for their alternative robust lipid-dependent acyltransferase enzymatic activity. We also determined high resolution crystal structures of HRAS-like tumor suppressor 2 and 3 to gain insight into their active site architecture. Based on this structural analysis, two conformational states of the catalytic Cys-113 were identified that differ in reactivity and thus could define the catalytic properties of these two proteins. Finally, these structures provide a model for the topology of these enzymes and allow identification of the protein-lipid bilayer interface. This study contributes to the enzymatic and structural understanding of HRAS-like tumor suppressor enzymes. << Less
J. Biol. Chem. 287:23790-23807(2012) [PubMed] [EuropePMC]
This publication is cited by 9 other entries.