Diterpene cyclase and methods of use
AssigneeFlorida Atlantic University
InventorsRussell Kerr, Amber Kohl, Jose Lopez
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Abstract
An enzyme having diterpene cyclase activity has been purified from P. elisabethae using a series of chromatography steps. The purified enzyme has an apparent molecular weight of about 47 kilodaltons and an isoelectric point of about 5.1. The purifed enzyme catalyzed the cyclization of geranyl geranyl diphosphate to elisabethatriene.
Claims16
Purified elisabethatriene cyclase.
A purified protein isolatable from a coral sample comprising Pseudopterogorgia elisabethae or a purified fragment of the protein capable of catalyzing the formation of elisabethatriene from geranyl geranyl diphosphate, the purified protein having the following characteristics:
- (A) an apparent molecular weight of about 47,000 Da;
- (B) an isoelectric point of about 5.1;
- and
- (C) the ability to cyclize geranyl geranyl diphosphate.
A method of purifying an elisabethatriene cyclase from a Pseudopterogorgia elisabethae sample, the method comprising the steps of:
- (A) preparing a cell free extract from a Pseudopterogorgia elisabethae sample;
- (B) separating the cell free extract into at least one fraction that exhibits elisabethatriene cyclase activity and at least one fraction that does not exhibit elisabethatriene cyclase activity;
- and
- (C) collecting the at least one fraction that exhibits elisabethatriene cyclase activity.
Dependencies are inferred from the claim text.