Ghrelin O-acyltransferase (GOAT) has a preference for n-hexanoyl-CoA over n-octanoyl-CoA as an acyl donor.
Ghrelin O-acyltransferase (GOAT) has a preference for n-hexanoyl-CoA over n-octanoyl-CoA as an acyl donor.
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DOI：
10.1016/j.bbrc.2009.06.001
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发表时间：
2009-08
影响因子：
3.1
通讯作者：
H. Ohgusu;Kaori Shirouzu;Yuki Nakamura;Yoshiki Nakashima;T. Ida;Takahiro Sato;M. Kojima
中科院分区：
文献类型：
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作者：
H. Ohgusu;Kaori Shirouzu;Yuki Nakamura;Yoshiki Nakashima;T. Ida;Takahiro Sato;M. Kojima
Ghrelin是一种肽激素，其中丝氨酸3被正辛酸通过GOAT （Ghrelin o -酰基转移酶）修饰。然而，GOAT的酶学特性仍有待阐明。我们利用重组酶分析了GOAT的体外活性。出乎意料的是，尽管胃饥饿素的主要活性形式是由正辛酸修饰的，但作为酰基供体，山羊对正己醇辅酶a的偏好强于正辛醇辅酶a。此外，从ghrelin的n端序列衍生的一个4个氨基酸的肽可以被GOAT修饰，这表明这4个氨基酸构成了该酶识别底物的核心基序。
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.