期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 386, 期 1, 页码 153-158出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.06.001
关键词
Ghrelin; Ghrelin O-acyltransferase (GOAT); Acyl-modification; n-Octanoyl-CoA; n-Hexanoyl-CoA
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Health and Labour Sciences Research
- Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry
Ghrelin is a peptide hormone in which serine 3 is modified by n-octanoic acid through GOAT (ghrelin O-acyltransferase). However, the enzymological properties of GOAT remain to be elucidated. We analyzed the in vitro activity of GOAT using the recombinant enzyme. Unexpectedly, although the main active form of ghrelin is modified by n-octanoic acid, GOAT had a strong preference for n-hexanoyl-CoA over n-octanoyl-CoA as an acyl donor. Moreover, a four-amino acid peptide derived from the N-terminal sequence of ghrelin can be modified by GOAT, indicating that these four amino acids constitute the core motif for substrate recognition by the enzyme. (C) 2009 Elsevier Inc. All rights reserved.
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