Part:BBa_K4275009
MHETase
As the second enzyme of the PET degradation two-enzyme system found in Ideonella sakaiensis, the MHETase catalyzes the cleavage of the ester bond in MHET(Monohydroxyethyl terephthalate) and liberates the final products of PET degradation - EG(ethylene glycol) and TPA(terephthalic acid) into the solution[1]. The MHETase amino acid sequence used in this experiment is the same with the wild-type MHETase (GenBank Accession number: GAP38911.1). The enzyme MHETase works in synergy with PETase, the first enzyme in the two-enzyme PET degradation system found in Ideonella sakaiensis - a PET-degrading and assimilating strain of bacteria isolated from a water treatment plant.
Figure 1 The 3D structure of the protein predicted by Alphafold2.
Usage and Biology
The 3D structure of MHETase consists of a catalytic domain and an extensive lid domain[1]. The catalytic domain adopts the α/β-hydrolase fold typical of a serine hydrolase, with an active site consist the catalytic triad Ser225, Asp492, and His528, which shows significant structural conservation compared to PETase. The lid domain partially covers the active site, hinders its capability to bind with PET fiber, and harbors a well-coordinated calcium cation[1].
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 123
Illegal NgoMIV site found at 237
Illegal NgoMIV site found at 693
Illegal AgeI site found at 190
Illegal AgeI site found at 307 - 1000COMPATIBLE WITH RFC[1000]
References
1. Knott, Brandon C. et al. "Characterization And Engineering Of A Two-Enzyme System For Plastics Depolymerization". Proceedings Of The National Academy Of Sciences, vol 117, no. 41, 2020, pp. 25476-25485. Proceedings Of The National Academy Of Sciences, https://doi.org/10.1073/pnas.2006753117.
| None |