Sequence and Features
- 10COMPATIBLE WITH RFC
- 12COMPATIBLE WITH RFC
- 21COMPATIBLE WITH RFC
- 23COMPATIBLE WITH RFC
- 25INCOMPATIBLE WITH RFCIllegal NgoMIV site found at 1027
Illegal AgeI site found at 247
Illegal AgeI site found at 364
- 1000COMPATIBLE WITH RFC
MHET is dedicated to the role of PET degradation.
Like PETase, MHETase is also discovered from Ideonella sakaiensis 201-F6, it is a enzyme which can hydrolyze MHET, which is the main product of PETase when hydrolyzing PET.
Group: Austin UTexas
Summary: MHETase is essential for optimized PET degradation using PETase. An enzymatic synergy between PETase and MHETase exists. MHET, an intermediate in the PET degradation pathway, can be hydrolyzed by a number of PET-degrading cutinases. The form of PETase isolated from Ideonella sakaiensis, however, also requires the presence of MHETase for optimal degradation of PET into terepthalic acid (TPA) and ethylene glycol (EG), the pathway’s biodegradable products. Knot et al. showed that release rates of TPA and EG vary in samples containing different concentrations of PETase and MHETase over 96 hours at 30 °C. MHETase has no activity on PET on its own, while PETase has a moderate degradation rate of PET on its own. When MHETase and PETase are used in tandem, however, degradation rates increase. The amount of MHETase added need not be large, which suggests that presence of MHETase is more important than any particular concentration ratio to PETase.2
 Kohei Oda, Shosuke Yoshida, et al. A bacterium that degrades and assimilates poly(ethylene terephthalate)[J]. Science. Vol 351. MARCH 2016: 1196-1199
 Knott, B. C., Erickson, E., Allen, M. D., Gado, J. E., Graham, R., Kearns, F. L., Pardo, I., Topuzlu, E., Anderson, J. J., Austin, H. P., Dominick, G., Johnson, C. W., Rorrer, N. A., Szostkiewicz, C. J., Copié, V., Payne, C. M., Woodcock, H. L., Donohoe, B. S., Beckham, G. T., McGeehan, J, E. (2020). Characterization and engineering of a two-enzyme system for plastics depolymerization. Proceedings of the National Academy of Sciences
|biology||Ideonella sakaiensis 201-F6|