Part:BBa_J45006

alcohol acetyltransferase I (ATF1)

Alcohol acetyltransferase I (ATFI) encodes the enzyme alcohol acetyltransferase I (AATase I), which produces acetate esters from acetyl CoA and alcohols. It was obtained from S. cerevisiae.

Usage and Biology

We will be interested in using AATase I to catalyze the reaction: isoamyl alcohol -> isoamyl acetate. Isoamyl acetate is a volatile ester with a strong banana-like scent. (The related enzyme AATase II, which is encoded by the gene ATF2, performs a similar function...but it is less efficient.)

According to studies done by [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12937998&query_hl=16&itool=pubmed_docsum Horton et al.], the addition of 10mM isoamyl alcohol to cultured E. coli expressing the ATF1 gene yields 1.8mM isoamyl acetate after 40 hours.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BglII site found at 99
  Illegal BamHI site found at 1426
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  INCOMPATIBLE WITH RFC[1000]

  Illegal SapI.rc site found at 526
  Illegal SapI.rc site found at 1534
  

Introduction

The acetyltransferase ATF1 one of three known S. cerevisiae alcohol acetyl transferases responsible for the synthesis of volatile esters. In this paper, ATF1 is proved to also acetylate alcohols to make various acetates, which are the main component of moth pheromones. Therefore, we could use this enzyme ATF1 to produce moth pheromone compounds biologically, which could be used in pest control.

Results

In this paper, They decided to determine whether this enzyme was responsible for the background formation of acetates when supplemented with long-chain fatty alcohols. First, They added 19 different fatty alcohol substrates to the atf1∆ knockout strain. The atf1∆ knockout strain produced barely detect- able quantities of any long-chain acetates, suggesting that ATF1 is the only yeast enzyme with significant activity towards fatty alcohols of C10 and longer (Fig. 2). To compare the capacity of ATF1 to that of EaDAcT to produce acetates, we expressed either enzyme in an atf1∆ knockout strain and incubated the cultures with the fatty alcohol sub- strates. Quantification of the acetates formation provided additional evidence that ATF1 can convert a wide range of fatty alcohols into their corresponding acetates (Fig. 2). Further, the levels of acetates formed in ATF1-expressing yeast were 10–40 times higher than those in yeast express- ing EaDAcT, except for 16:OH, 18:OH, and Z9-18:OH which were also poor substrates for ATF1 (Fig. 2).

Reference

Ding, Bao‑Jian, et al. “The Yeast ATF1 Acetyltransferase Efficiently Acetylates Insect Pheromone Alcohols: Implications for the Biological Production of Moth Pheromones.” Lipids, vol. 51, no. 4, 2016, pp. 469–475.