ArticleBioorganic chemistry2015
Mechanistic analysis of ghrelin-O-acyltransferase using substrate analogs.
Article in Bioorganic chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Acyltransferases that Modify Cell Surface Polymers Across the Membrane.Biochemistry · 2025Review
- Therapeutic potential of ghrelin/GOAT/GHSR system in gastrointestinal disorders.Frontiers in nutrition · 2024Review
- Combined Computational-Biochemical Approach Offers an Accelerated Path to Membrane Protein Solubilization.Journal of chemical information and modeling · 2023Article
- Cellular Uptake of a Fluorescent Ligand Reveals GhrelinACS chemical biology · 2023Article
- Discovery of novel inhibitors of ghrelin O-acyltransferase enzyme: anResearch in pharmaceutical sciences · 2022Article
- Ghrelin octanoylation by ghrelinOpen biology · 2021Review
- Ghrelin Signaling: GOAT and GHS-R1a Take a LEAP in Complexity.Trends in endocrinology and metabolism: TEM · 2020Review
- The ghrelinThe Journal of biological chemistry · 2019Article
- Article
- Characterization of Ghrelin O-Acyltransferase (GOAT) in goldfish (Carassius auratus).PloS one · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Ghrelin-O-Acyltransferase (GOAT) is an 11-transmembrane integral membrane protein that octanoylates the metabolism-regulating peptide hormone ghrelin at Ser3 and may represent an attractive target for the treatment of type II diabetes and the metabolic syndrome. Protein octanoylation is unique to ghrelin in humans, and little is known about the mechanism of GOAT or of related protein-O-acyltransferases HHAT or PORC. In this study, we explored an in vitro microsomal ghrelin octanoylation assay to analyze its enzymologic features. Measurement of Km for 10-mer, 27-mer, and synthetic Tat-peptide-containing ghrelin substrates provided evidence for a role of charge interactions in substrate binding. Ghrelin substrates with amino-alanine in place of Ser3 demonstrated that GOAT can catalyze the formation of an octanoyl-amide bond at a similar rate compared with the natural reaction. A pH-rate comparison of these substrates revealed minimal differences in acyltransferase activity across pH 6.0-9.0, providing evidence that these reactions may be relatively insensitive to the basicity of the substrate nucleophile. The conserved His338 residue was required both for Ser3 and amino-Ala3 ghrelin substrates, suggesting that His338 may have a key catalytic role beyond that of a general base.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.