Difference between revisions of "Part:BBa K4378999"
| Line 7: | Line 7: | ||
The designation of the gene TphB is used interchangeably with the name of its product’s function, decarboxylating cis-dihydrodiol dehydrogenase (DCDDH). TphB is unique in its capacity to decarboxylate the reaction product from the TphA1, A2, and A3 actions. | The designation of the gene TphB is used interchangeably with the name of its product’s function, decarboxylating cis-dihydrodiol dehydrogenase (DCDDH). TphB is unique in its capacity to decarboxylate the reaction product from the TphA1, A2, and A3 actions. | ||
| − | Bains et al. structurally characterized the 3-dimensional structure of DCDDH at 1. | + | Bains et al. structurally characterized the 3-dimensional structure of DCDDH at 1.85Å (Bains, 2012). The method used for structural characterization was iodide single wavelength anomalous dispersion. Computational modeling yielded information about how DCDDH acts on its substrate (Bains, 2012). |
No genetic engineering has been carried out to improve catalytic activity of DCDDH. All published efforts outline characterizations of either mechanistic or structural interest. Similarly, little information exists as to the kinetics of the above catalysis accomplished by TphB. A comprehensive report on kinetics of phthalate ester metabolism is available from Kluwe et al. (Kluwe, 1982). Apart from the publication from Bains, no experiment has to date provided insight into how TphB accomplishes its reaction. | No genetic engineering has been carried out to improve catalytic activity of DCDDH. All published efforts outline characterizations of either mechanistic or structural interest. Similarly, little information exists as to the kinetics of the above catalysis accomplished by TphB. A comprehensive report on kinetics of phthalate ester metabolism is available from Kluwe et al. (Kluwe, 1982). Apart from the publication from Bains, no experiment has to date provided insight into how TphB accomplishes its reaction. | ||
Revision as of 09:50, 1 October 2022
TphB with His-Tag
The first documented degradation of phthalates in soil bacteria comes from a paper published 1995. Researchers sampled sediment from the riverbed of the Passaic River in New Jersey (Wang, 1995). Samples were then exposed to various phthalates and their respective microbial populations and metabolites characterized thereafter. C. testosteroni emerged from a sample with a microbiota capable of growing on two different phthalate isomers. These were terephthalate (Tph), isophthalate, and p-hydroxybenzoate.
The designation of the gene TphB is used interchangeably with the name of its product’s function, decarboxylating cis-dihydrodiol dehydrogenase (DCDDH). TphB is unique in its capacity to decarboxylate the reaction product from the TphA1, A2, and A3 actions.
Bains et al. structurally characterized the 3-dimensional structure of DCDDH at 1.85Å (Bains, 2012). The method used for structural characterization was iodide single wavelength anomalous dispersion. Computational modeling yielded information about how DCDDH acts on its substrate (Bains, 2012).
No genetic engineering has been carried out to improve catalytic activity of DCDDH. All published efforts outline characterizations of either mechanistic or structural interest. Similarly, little information exists as to the kinetics of the above catalysis accomplished by TphB. A comprehensive report on kinetics of phthalate ester metabolism is available from Kluwe et al. (Kluwe, 1982). Apart from the publication from Bains, no experiment has to date provided insight into how TphB accomplishes its reaction.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 219
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 340
References
Bains J, Wulff JE, Boulanger MJ. 2012. Investigating Terephthalate Biodegradation: Structural Characterization of a Putative Decarboxylating cis-Dihydrodiol Dehydrogenase. Journal of Molecular Biology 423: 284–293.
Wang YZ, Zhou Y, Zylstra GJ. 1995. Molecular analysis of isophthalate and terephthalate degradation by Comamonas testosteroni YZW-D. Environmental Health Perspectives 103: 9–12.