| Structural highlights
Function
DDDQ_RUELI Able to cleave dimethlysulfonioproprionate (DMSP) in vitro, releasing dimethyl sulfide (DMS). DMS is the principal form by which sulfur is transported from oceans to the atmosphere (PubMed:24395783, PubMed:24967457). The real activity of the protein is however subject to debate and it is unclear whether it constitutes a real dimethlysulfonioproprionate lyase in vivo: the very low activity with DMSP as substrate suggests that DMSP is not its native substrate (PubMed:24760823).[1] [2] [3]
References
- ↑ Li CY, Wei TD, Zhang SH, Chen XL, Gao X, Wang P, Xie BB, Su HN, Qin QL, Zhang XY, Yu J, Zhang HH, Zhou BC, Yang GP, Zhang YZ. Molecular insight into bacterial cleavage of oceanic dimethylsulfoniopropionate into dimethyl sulfide. Proc Natl Acad Sci U S A. 2014 Jan 21;111(3):1026-31. doi:, 10.1073/pnas.1312354111. Epub 2014 Jan 6. PMID:24395783 doi:http://dx.doi.org/10.1073/pnas.1312354111
- ↑ Alcolombri U, Elias M, Vardi A, Tawfik DS. Ambiguous evidence for assigning DddQ as a dimethylsulfoniopropionate lyase and oceanic dimethylsulfide producer. Proc Natl Acad Sci U S A. 2014 May 20;111(20):E2078-9. doi:, 10.1073/pnas.1401685111. Epub 2014 Apr 23. PMID:24760823 doi:http://dx.doi.org/10.1073/pnas.1401685111
- ↑ Li CY, Chen XL, Xie BB, Su HN, Qin QL, Zhang YZ. Reply to Tawfik et al.: DddQ is a dimethylsulfoniopropionate lyase involved in dimethylsulfoniopropionate catabolism in marine bacterial cells. Proc Natl Acad Sci U S A. 2014 May 20;111(20):E2080. PMID:24967457
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