GhrelinO-acyltransferase (GOAT), a specific enzyme that modifies ghrelin with a medium-chain fatty acid
Author(s) -
Masayasu Kojima,
Akie Hamamoto,
Takahiro Sato
Publication year - 2016
Publication title -
the journal of biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 115
eISSN - 1756-2651
pISSN - 0021-924X
DOI - 10.1093/jb/mvw046
Subject(s) - ghrelin , threonine , serine , enzyme , chemistry , endocrinology , medicine , biochemistry , hormone , biology
In the gastric peptide hormone ghrelin, serine 3 (threonine 3 in frogs) is modified, primarily by n-octanoic acid; this modification is essential for ghrelin's activity. The enzyme that transfers n-octanoic acid to Ser3 of ghrelin is ghrelin O-acyltransferase (GOAT). GOAT, the only enzyme known to catalyze acyl modification of ghrelin, specifically modifies serine (or threonine) at the third position and does not modify other serine residues in ghrelin peptides. GOAT prefers n-hexanoyl-CoA over n-octanoyl-CoA as the acyl donor, although in the stomach the n-octanoyl form is the predominant form of acyl-modified ghrelin. GOAT is a promising target for drug development to treat metabolic diseases and eating disorders.
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