Characterisation of Acetyl-CoA Thiolase: The First Enzyme in the Biosynthesis of Terpenic Sex Pheromone Components in the Labial Gland of Bombus terrestris

0444344 - ÚOCHB 2016 RIV DE eng J - Článek v odborném periodiku
Brabcová, Jana - Demianová, Z. - Kindl, Jiří - Pichová, Iva - Valterová, Irena - Zarevúcka, Marie
Characterisation of Acetyl-CoA Thiolase: The First Enzyme in the Biosynthesis of Terpenic Sex Pheromone Components in the Labial Gland of Bombus terrestris.
Chembiochem. Roč. 16, č. 7 (2015), s. 1047-1051. ISSN 1439-4227. E-ISSN 1439-7633
Grant CEP: GA TA ČR TA01020969
Institucionální podpora: RVO:61388963
Klíčová slova: acetyl-CoA thiolase * biosynthesis * Bombus terrestris * labial gland * pheromones * terpenoids
Kód oboru RIV: CE - Biochemie
Impakt faktor: 2.850, rok: 2015

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.
Trvalý link: http://hdl.handle.net/11104/0246996