Substrate specificity of an archaeal thioesterase from Thermococcus kodakarensis
Clicks: 3
ID: 315933
2026
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This
article has not been analysed, so there is no overall score —
reader engagement is measured and shown alongside.
Reader Engagement
Steady Performance
0.6
/100
3 views
0 readers
AI Quality Assessment
Not analyzed
Readership in this journal
SteadyRanked #19 of 36 articles by views in The Journal of Biochemistry
Most read
Least read
Bar heights use a square-root scale.
Mint this article as an NFT
Not yet mintedCreate a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.
5
SUSD
one-off · no wallet required
Abstract
Thioesterases catalyze the hydrolysis of thioester bonds and are responsible for reactions such as the release of fatty acids from acyl-ACP in fatty acid biosynthesis. Although enzymes from bacteria and eukaryotes have been studied, identification and characterization of thioesterases from archaea have not been reported. Here we searched the genome of the hyperthermophilic archaeon Thermococcus kodakarensis for candidate genes that might encode a thioesterase. Among these, the TK1652 protein contained a HotDog fold and shared ~ 20% identity with TE8 and TE13 family thioesterases. Active site residues proposed for TE8 and TE13 enzymes were partially conserved in the TK1652 protein. The recombinant TK1652 protein produced in Escherichia coli was purified to apparent homogeneity. Although TE8 and TE13 family enzymes assemble as tetramers, the TK1652 protein formed a homodimer. The protein displayed thioesterase activity toward acetyl-CoA, and to a much lower extent, propionyl-CoA. The TK1652 protein did not recognize phenylacetyl-CoA, n-decanoyl-CoA, lauroyl-CoA and myristoyl-CoA, substrates utilized by TE8/TE13 family thioesterases. Differences in active site residues, quaternary structure, and substrate specificity suggested that the TK1652 protein represents a new family of thioesterases. Acetyl-CoA thioesterase activity was detected in cell-free extracts of T. kodakarensis, and the metabolic roles of this activity are discussed.
| Reference Key |
openalex_W7163583081
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
|---|---|
| Authors | Yu Su, Jianqiang Jin, Yuta Michimori, Haruyuki Atomi |
| Journal | The Journal of Biochemistry |
| Year | 2026 |
| DOI |
10.1093/jb/mvag037
|
| URL | |
| Keywords | Keywords not found |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.