2004
DOI: 10.1074/jbc.m309532200
|View full text |Cite
|
Sign up to set email alerts
|

Biochemical and Molecular Characterization of ACH2, an Acyl-CoA Thioesterase from Arabidopsis thaliana

Abstract: By using computer-based homology searches of the Arabidopsis genome, we identified the gene for ACH2, a putative acyl-CoA thioesterase. With the exception of a unique 129-amino acid N-terminal extension, the ACH2 protein is 17-36% identical to members of a family of acyl-CoA thioesterases that are found in both prokaryotes and eukaryotes. The eukaryotic homologs of ACH2 are peroxisomal acyl-CoA thioesterases that are up-regulated during times of increased fatty acid oxidation, suggesting potential roles in per… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

3
36
0
1

Year Published

2004
2004
2020
2020

Publication Types

Select...
7
2

Relationship

0
9

Authors

Journals

citations
Cited by 57 publications
(45 citation statements)
references
References 42 publications
3
36
0
1
Order By: Relevance
“…Information on plant acyl-CoA thioesterases is limited. One Arabidopsis peroxisomal acyl-CoA thioesterase, ACH2, has been cloned and biochemically characterized, and the data suggest that this enzyme is unlikely to be involved in fatty acid oxidation, but its function is unclear (Tilton et al, 2004). A thioesterase activity was previously reported for mammalian iPLA 2 b, which is also a patatin domain-containing enzyme (Jenkins et al, 2006).…”
Section: Discussionmentioning
confidence: 95%
See 1 more Smart Citation
“…Information on plant acyl-CoA thioesterases is limited. One Arabidopsis peroxisomal acyl-CoA thioesterase, ACH2, has been cloned and biochemically characterized, and the data suggest that this enzyme is unlikely to be involved in fatty acid oxidation, but its function is unclear (Tilton et al, 2004). A thioesterase activity was previously reported for mammalian iPLA 2 b, which is also a patatin domain-containing enzyme (Jenkins et al, 2006).…”
Section: Discussionmentioning
confidence: 95%
“…However, the physiological roles of acyl-CoA thioesterases remain unclear. One role suggested for peroxisomal acyl-CoA thioesterases is in fatty acid oxidation (Tilton et al, 2004). Information on plant acyl-CoA thioesterases is limited.…”
Section: Discussionmentioning
confidence: 99%
“…The final step of JA biosynthesis is that jasmonyl-CoA releases free acid by jasmonyl-thioesterase. There is no report of cloning of jasmonyl-thioesterase in plant so far except that in Arabidopsis two peroxyisomal acyl-thioesterases, ACH1 and ACH2 have showed thioesterase activity of hydrolyzing both medium and long-chain fatty acylCoAs but not jasmonyl-CoA (Tilton et al, 2004).…”
Section: β-Oxidation Enzymesmentioning
confidence: 99%
“…In addition, peroxisomes contain another structurally unrelated acyl-CoA thioesterase, called PTE-2. This enzyme was initially identified as an HIV-1 Nefbinding protein (21,22) and subsequently further characterized as an acyl-CoA thioesterase in mouse, human, yeast, and rat (19,20,23,38). Characterization of PTE-2 in mouse showed it to be the major acyl-CoA thioesterase in peroxisomes, hydrolyzing a broad range of acyl-CoA esters.…”
Section: Discussionmentioning
confidence: 99%