期刊
PLANT MOLECULAR BIOLOGY REPORTER
卷 29, 期 3, 页码 745-752出版社
SPRINGER
DOI: 10.1007/s11105-010-0266-1
关键词
Auxin conjugate hydrolase; Enzyme activity.; Enzyme regulation; Indole-3-acetic acid; Indole-3-butyric acid; Medicago truncatula
资金
- Margaret and Herman Sokol Faculty [07A]
We have previously isolated and characterized a family of auxin amino acid conjugate hydrolases from the legume Medicago truncatula. All characterized members of this family possess a conserved second methionine within the predicted hydrolase domain. We therefore constructed 5'-truncated clones of the hydrolases to investigate whether this methionine could have a potential function. Overall, the hydrolases exhibited altered substrate specificities towards a variety of auxin conjugates tested, with a somewhat broadened substrate range. In vitro hydrolase activity increased over wild-type in several of the shortened proteins, but only for some substrates. The 5' head domain may be serving a regulatory function in the full-length versions of the enzymes or could provide a mechanism to broaden the substrate range in vivo.
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