Ghrelin O-acyltransferase (GOAT) has a preference for n-hexanoyl-CoA over n-octanoyl-CoA as an acyl donor

Biochemical and Biophysical Research Communications

Volumn 386, Issue 1, 2009, Pages 153-158

  Ohgusu, Hideko ^a   Shirouzu, Kaori ^a   Nakamura, Yuki ^a   Nakashima, Yoshiki ^a   Ida, Takanori ^a   Sato, Takahiro ^a   Kojima, Masayasu ^a  

^a KURUME UNIVERSITY   (Japan)

Author keywords

Acyl modification; Ghrelin; Ghrelin O acyltransferase (GOAT); n Hexanoyl CoA; n Octanoyl CoA

Indexed keywords

ACYLTRANSFERASE; COENZYME A; COPPER; GHRELIN; GHRELIN O ACYLTRANSFERASE; HEXANOYL COENZYME A; IRON; OCTANOIC ACID; OCTANOYL COENZYME A; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN MOTIF; TEMPERATURE;

ACYL COENZYME A; ACYLTRANSFERASES; AMINO ACID SEQUENCE; ANIMALS; GHRELIN; HYDROGEN-ION CONCENTRATION; MICE; PEPTIDES; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 67649210216     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.06.001     Document Type: Article

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