Ghrelin O-acyltransferase decanoylates Proghrelin

Stable Identifier
R-HSA-422017
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Proghrelin is decanoylated by ghrelin O-acyltransferase (GOAT/MBOAT4), an enzyme present in the endoplasmic reticulum membrane which both transports the decanoic acid substrate and condenses it on the hydroxyl group of serine-3 of the mature protein. The most common acylated form of ghrelin is octanoyl ghrelin but decanoyl ghrelin is also detected in plasma. GOAT is able to use substrates up to tetradecanoic acid. Ghrelin is the only protein known to undergo such a modification.

Literature References
PubMed ID Title Journal Year
19280057 Ghrelin fluctuation, what determines its production?

Yin, X, Li, Y, Zhang, W, An, W, Xu, G

Acta Biochim Biophys Sin (Shanghai) 2009
18396350 Ghrelin, des-acyl ghrelin and obestatin: three pieces of the same puzzle

Soares, JB, Leite-Moreira, AF

Peptides 2008
12414809 Structural divergence of human ghrelin. Identification of multiple ghrelin-derived molecules produced by post-translational processing

Kangawa, K, Hosoda, H, Mizushima, T, Shimizu, S, Kojima, M

J Biol Chem 2003
19628676 Production of n-octanoyl-modified ghrelin in cultured cells requires prohormone processing protease and ghrelin O-acyltransferase, as well as n-octanoic acid

Nakamura, Y, Ida, T, Tsuji, A, Sato, T, Takahashi, T, Nakashima, Y, Kojima, M

J Biochem 2009
18443287 Ghrelin octanoylation mediated by an orphan lipid transferase

Knierman, MD, Luo, S, Hale, JE, Jin, Z, Onyia, JE, Witcher, DR, Willency, JA, Perkins, DR, Solenberg, PJ, Gutierrez, JA

Proc Natl Acad Sci U S A 2008
Participants
Participates
Catalyst Activity

O-acyltransferase activity of MBOAT4 [endoplasmic reticulum membrane]

Orthologous Events
Authored
Reviewed
Created
Cite Us!