Disease relevance of ACP3

• This difference most likely results from the presence of sufficient substrate pools of C(14) and C(16) acyl-ACPs but a relative lack of C(18) acyl-ACP pools in E. coli to support the activities of the plant fatty acid desaturase [1].

High impact information on ACP3

• These results imply that both 12:0- and 14:0-ACP can bind to the two proteins equally well, but in the case of the triple mutant, the hydrolysis of 12:0-ACP is severely impaired [2].
• When the FatB1 cDNA encoding a 12:0-ACP TE (Uc FatB1) from California bay, Umbellularia californica (Uc) was expressed in Escherichia coli and in developing oilseeds of the plants Arabidopsis thaliana and Brassica napus, large amounts of laurate (12:0) and small amounts of myristate (14:0) were accumulated [2].
• ACP2, ACP3, and ACP4 mRNA levels were also examined in Arabidopsis cell suspension culture and were found to be differentially controlled by metabolic and/or growth derived signals [3].
• The substrate specificity of ATP A2 was analysed by X-ray crystallography and docking of lignin precursors [4].
• The analysis indicates that the precursors p-coumaryl and coniferyl alcohols are preferred by ATP A2, while the oxidation of sinapyl alcohol will be sterically hindered in ATP A2 as well as in all other plant peroxidases due to an overlap with the conserved Pro-139 [4].

Biological context of ACP3

• This element contains a characteristic telomeric sequence (AACCCTAA) which is also found in the promoters of the A2 and A4 genes as well as in the promoters of the Drosophila EF-1 alpha F1 gene and of several highly expressed plant genes [5].
• Based upon both their physical separation and a comparison of their sequences, it is suggested that the A4 gene and the A1, A2, and A3 genes constitute two distinct subfamilies within the genome [5].
• Characterization of substrate specificity of plant FatA and FatB acyl-ACP thioesterases [6].
• The deduced amino acid sequence is 51% identical to the lauroyl-ACP thioesterase but only 39% identical to safflower oleoyl-ACP thioesterase [7].
• Here we show that the Atp A2 promoter directs GUS reporter gene expression in lignified tissues of transgenic plants [4].

Anatomical context of ACP3

• We suggest ATP A2 is involved in a complex regulation of the covalent cross-linking in the plant cell wall [4].

Associations of ACP3 with chemical compounds

• Acylation of fatty acids to hydroxy groups in cells generally require activation to a thioester (ACP or CoA) or transacylation from another oxygen ester [8].

References