Enzymes
| UniProtKB help_outline | 4 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
L-seryl-[protein]
Identifier
RHEA-COMP:9863
Reactive part
help_outline
- Name help_outline L-serine residue Identifier CHEBI:29999 Charge 0 Formula C3H5NO2 SMILEShelp_outline C([C@H](CO)N*)(=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 butanoyl-CoA Identifier CHEBI:57371 Charge -4 Formula C25H38N7O17P3S InChIKeyhelp_outline CRFNGMNYKDXRTN-CITAKDKDSA-J SMILEShelp_outline CCCC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 37 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
O-butanoyl-L-seryl-[protein]
Identifier
RHEA-COMP:17461
Reactive part
help_outline
- Name help_outline O-butanoyl-L-serine residue Identifier CHEBI:177287 Charge 0 Formula C7H11NO3 SMILEShelp_outline C(CCC)(OC[C@@H](C(*)=O)N*)=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 CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,567 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:68276 | RHEA:68277 | RHEA:68278 | RHEA:68279 | |
|---|---|---|---|---|
| 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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Ghrelin octanoylation mediated by an orphan lipid transferase.
Gutierrez J.A., Solenberg P.J., Perkins D.R., Willency J.A., Knierman M.D., Jin Z., Witcher D.R., Luo S., Onyia J.E., Hale J.E.
The peptide hormone ghrelin is the only known protein modified with an O-linked octanoyl side group, which occurs on its third serine residue. This modification is crucial for ghrelin's physiological effects including regulation of feeding, adiposity, and insulin secretion. Despite the crucial rol ... >> More
The peptide hormone ghrelin is the only known protein modified with an O-linked octanoyl side group, which occurs on its third serine residue. This modification is crucial for ghrelin's physiological effects including regulation of feeding, adiposity, and insulin secretion. Despite the crucial role for octanoylation in the physiology of ghrelin, the lipid transferase that mediates this novel modification has remained unknown. Here we report the identification and characterization of human GOAT, the ghrelin O-acyl transferase. GOAT is a conserved orphan membrane-bound O-acyl transferase (MBOAT) that specifically octanoylates serine-3 of the ghrelin peptide. Transcripts for both GOAT and ghrelin occur predominantly in stomach and pancreas. GOAT is conserved across vertebrates, and genetic disruption of the GOAT gene in mice leads to complete absence of acylated ghrelin in circulation. The occurrence of ghrelin and GOAT in stomach and pancreas tissues demonstrates the relevance of GOAT in the acylation of ghrelin and further implicates acylated ghrelin in pancreatic function. << Less
Proc. Natl. Acad. Sci. U.S.A. 105:6320-6325(2008) [PubMed] [EuropePMC]
This publication is cited by 9 other entries.