Structural highlights
Function
RDPA_SPHHM Involved in the degradation of the phenoxypropionate herbicides. Catalyzes the enantiospecific cleavage of the ether bond in the herbicid R-dichlorprop ((R)-2-(2,4-dichlorophenoxy)propionate)(R-2,4-DP) and R-mecoprop ((R)-2-(4-chloro-2-methylphenoxy)propionate)(R-2,4-MCPP). It can also accept (RS)-4-chlorophenoxypropanoate, however it can only accept 2-oxoglutarate as oxygen acceptor.[1] [2] [3]
References
- ↑ Muller TA, Zavodszky MI, Feig M, Kuhn LA, Hausinger RP. Structural basis for the enantiospecificities of R- and S-specific phenoxypropionate/alpha-ketoglutarate dioxygenases. Protein Sci. 2006 Jun;15(6):1356-68. doi: 10.1110/ps.052059406. PMID:16731970 doi:http://dx.doi.org/10.1110/ps.052059406
- ↑ Muller TA, Fleischmann T, van der Meer JR, Kohler HP. Purification and characterization of two enantioselective alpha-ketoglutarate-dependent dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH. Appl Environ Microbiol. 2006 Jul;72(7):4853-61. doi: 10.1128/AEM.02758-05. PMID:16820480 doi:http://dx.doi.org/10.1128/AEM.02758-05
- ↑ Kohler HP. Sphingomonas herbicidovorans MH: a versatile phenoxyalkanoic acid herbicide degrader. J Ind Microbiol Biotechnol. 1999 Oct;23(4-5):336-340. doi:, 10.1038/sj/jim/2900751. PMID:11423952 doi:http://dx.doi.org/10.1038/sj/jim/2900751
