Purification and kinetic properties of ...



Title Purification and kinetic properties of elisabethatriene synthase from the coral Pseudopterogorgia elisabethae
Author(s) T. B. Bruck, Russell G. Kerr
Journal Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
Date 2006
Volume 143
Issue 3
Start page 269
End page 278
Abstract The Bahamian octocoral Pseudopterogorgia elisabethae is the source of pseudopterosins, diterpene glycosides with potent anti-inflammatory activity. The first committed step in pseudopterosin biosynthesis comprises the cyclisation of the universal diterpene precursor geranylgeranyl diphosphate to elisabethatriene. This reaction is catalysed by elisabethatriene synthase, which was purified to homogeneity from a crude coral extract. This represents the first purification to apparent homogeneity of a terpene cyclase from any marine source. The reaction kinetics of elisabethatriene synthase was examined using a steady state approach with (3)H-labelled isoprenyldiphosphates varying in carbon chain length (C(10), C(15), C(20)). For the reaction of elisabethatriene synthase with its natural substrate geranylgeranyl diphosphate, values of K(m) (2.3 x 10(-6) M), V(max) (3.4 x 10(4) nM elisabethatriene x s(-1)) and the specificity constant (k(cat)/K(m)= 1.8 x 10(-10) M(-1) x s(-1)) were comparable with diterpene cyclases from terrestrial plants. Elisabethatriene synthase also catalysed the conversion of C(15) and C(10) isoprenyldiphosphate analogues to monoterpene and sesquiterpene olefins, respectively. Kinetic parameters indicated that substrate specificity and K(m) of elisabethatriene synthase decreased with decreasing isoprenoid carbon chain length. Furthermore, GC-MS analysis showed increased product diversity with decreasing isoprenoid carbon chain length.
DOI 10.1016/j.cbpb.2005.11.016
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