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Characterisation of Acetyl‐CoA Thiolase: The First Enzyme in the Biosynthesis of Terpenic Sex Pheromone Components in the Labial Gland of Bombus terrestris
Author(s) -
Brabcová Jana,
Demianová Zuzana,
Kindl Jiří,
Pichová Iva,
Valterová Irena,
Zarevúcka Marie
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402591
Subject(s) - thiolase , pheromone , sex pheromone , biology , enzyme , biochemistry , botany , dehydrogenase
Buff‐tailed bumblebees, Bombus terrestris , use a male sex pheromone for premating communication. Its main component is a sesquiterpene, 2,3‐dihydrofarnesol. This paper reports the isolation of a thiolase (acetyl‐CoA thiolase, AACT_BT), the first enzyme involved in the biosynthetic pathway leading to formation of isoprenoids in the B. terrestris male sex pheromone. Characterisation of AACT_BT might contribute to a better understanding of pheromonogenesis in the labial gland of B. terrestris males. The protein was purified to apparent homogeneity by column chromatography with subsequent stepwise treatment. AACT_BT showed optimum acetyltransferase activity at pH 7.1 and was strongly inhibited by iodoacetamide. The enzyme migrated as a band with an apparent mass of 42.9 kDa on SDS‐PAGE. MS analysis of an AACT_BT tryptic digest revealed high homology to representatives of the thiolase family. AACT_BT has 96 % amino acid sequence identity with the previously reported Bombus impatiens thiolase.