Purification of (+)-gamma-cadinene synthase, a sesquiterpene cyclase from bacteria-inoculated cotton foliar tissue

A sesquiterpene cyclase whose activity is induced in a glandless, bacterial blight-resistant line of cotton (Gossypium hirsutum L.) catalyses the conversion of (E, E)-farnesyl diphosphate to (+)-delta-cadinene. This enzyme was purified by a combination of salt-induced phase separation, hydroxylapati...

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Bibliographic Details
Published in:Phytochemistry (Oxford) 1996, Vol.41 (4), p.1047-1055
Main Authors: Davis, E.M, Tsuji, J, Davis, G.D, Pierce, M.L, Essenberg, M
Format: Article
Language:English
Subjects:
amino acid sequences
biosynthesis
chemical structure
cotyledons
disease resistance
enzyme activity
Gossypium hirsutum
leaves
ligases
molecular conformation
molecular sequence data
molecular weight
pathogenicity
phytoalexins
purification
sesquiterpenoids
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Summary:A sesquiterpene cyclase whose activity is induced in a glandless, bacterial blight-resistant line of cotton (Gossypium hirsutum L.) catalyses the conversion of (E, E)-farnesyl diphosphate to (+)-delta-cadinene. This enzyme was purified by a combination of salt-induced phase separation, hydroxylapatite fractionation, hydrophobic interaction and strong anion-exchange chromatography, and denaturing polyacrylamide gel electrophoresis, followed by renaturation with Tween 80. The purified enzyme has a molecular weight of 64-65 kDa, and exhibited a single silver-staining band fo11owing electrophoresis in analytical denaturing polyacrylamide gels. Amino acid sequences of three tryptic peptides from the enzyme have been determined and are similar to known sequences in other terpene cyclases from plants.
ISSN:0031-9422
1873-3700