Taxonomic group: plant / Streptophyta
(Phylum: Streptophyta)
Organ / tissue: leaf
Publication DOI: 10.1111/j.1365-313X.2007.03079.xJournal NLM ID: 9207397Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
Correspondence: cathie.martin
bbsrc.ac.uk
Institutions: John Innes Centre, Norwich Research Park, Colney, Norwich, NR4 7UH, UK, Graduate School of Pharmaceutical Sciences, Chiba University, Yayoi-cho 1-33, Inage-ku, Chiba 263-8522, Japan, Institute of Life Science, Ehime Women’s College, 421 Ibuki-cho Baba, Uwajima-shi, Ehime, 798-0025, Japan, Technologies for Systems Biology, Institute of Food Research, Norwich Research Park, Colney, Norwich, NR4 7UA, UK, Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, 3-15-1 Tokida, Ueda, Nagano 386-8567, Japan, Institute of Advanced Technology, Suntory Ltd., 1-1-1 Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka, 618-8503, Japan, RIKEN Plant Science Center, Suehiro-cho 1-7-22, Tsurumi-ku, Yokohama, 230-0045, Japan
Members of the BAHD family of plant acyl transferases are very versatile catalytically, and are thought to be able to evolve new substrate specificities rapidly. Acylation of anthocyanins occurs in many plant species and affects anthocyanin stability and light absorption in solution. The versatility of BAHD acyl transferases makes it difficult to identify genes encoding enzymes with defined substrate specificities on the basis of structural homology to genes of known catalytic function alone. Consequently, we have used a modification to standard functional genomics strategies, incorporating co-expression profiling with anthocyanin accumulation, to identify genes encoding three anthocyanin acyl transferases from Arabidopsis thaliana. We show that the activities of these enzymes influence the stability of anthocyanins at neutral pH, and some acylations also affect the anthocyanin absorption maxima. These properties make the BAHD acyl transferases suitable tools for engineering anthocyanins for an improved range of biotechnological applications.
anthocyanins, acyl transferases, convergent evolution, functional genomics
Structure type: oligomer
Location inside paper: Figure 1a
Trivial name: A11
Contained glycoepitopes: IEDB_114701,IEDB_116879,IEDB_142488,IEDB_146664,IEDB_167188,IEDB_174332,IEDB_983931,SB_192
Methods: ESI-MS, biological assays, HPLC, UV, LC-MS, enzymatic assay, genetic manipulations
Related record ID(s): 61092, 61093, 61094, 61095, 61096, 61097, 61098, 61099, 61100, 61101, 61103, 61104
NCBI Taxonomy refs (TaxIDs): 3702
Show glycosyltransferases
There is only one chemically distinct structure:
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