From Proteopedia

proteopedia linkproteopedia link

Revision as of 00:41, 11 April 2025 (edit) Anjali Rabindran (Talk | contribs) ← Previous diff		Revision as of 00:45, 11 April 2025 (edit) (undo) Anjali Rabindran (Talk | contribs) Next diff →
Line 9:		Line 9:
	<scene name='10/1075190/F243_wt/5'>WT F243 Residue</scene>		<scene name='10/1075190/F243_wt/5'>WT F243 Residue</scene>
-	<br /><scene name='10/1075190/F243w_mutant/4'>F243W</scene>	+	<br /><scene name='10/1075190/F243w_mutant/5'>F243W</scene>
	<scene name='10/1075190/F243i/3'>F234I</scene>		<scene name='10/1075190/F243i/3'>F234I</scene>

---

Revision as of 00:45, 11 April 2025

Contents 1 PET Hydrolase!!!!!😁😁😁😊😊😊😊😊 1.1 Structure 1.2 Results 1.3 Mechanism 1.4 References

PET Hydrolase!!!!!😁😁😁😊😊😊😊😊

Structure

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Researchers have been investigating various mutations of PET hydrolase to enhance is catalytic ability. One group of researchers, Tournier et. al., have made mutations in the PET hydrolase active site. They identified the key residues involved in the catalytic mechanism by using a model of the onto the enzyme. The site, mainly a hydrophobic pocket, contained 11 residues targeted for mutagenesis. From this, they identified that the majority of enzymes specific activity went down, however, the mutation of the F243 to either isoleucine or tryptophan actually increased specific activity.

Results

Table 1. Specific activity and rate of wild-type, WCCG, and ICCG mutants. Initial rate was measured by the calculated rate of reaction by NaOH consumption. Specific activity was measured via pf-PET-depolymerization assay.^[1]

	Enzyme		Initial rate (ghydrolyzed PET•L-1•h-1)		Specific activity (mgTAeqh-1•mgenzyme-1) ± SD
	Wild-Type		25.7		81.9 ± 5.6
	WCCG		30.3		75.9 ± 5.9
	ICCG		31.0		82.0 ± 3.9

Mechanism

References

1. ↑ Tournier V, Topham CM, Gilles A, David B, Folgoas C, Moya-Leclair E, Kamionka E, Desrousseaux ML, Texier H, Gavalda S, Cot M, Guemard E, Dalibey M, Nomme J, Cioci G, Barbe S, Chateau M, Andre I, Duquesne S, Marty A. An engineered PET depolymerase to break down and recycle plastic bottles. Nature. 2020 Apr;580(7802):216-219. doi: 10.1038/s41586-020-2149-4. Epub 2020 Apr, 8. PMID:32269349 doi:http://dx.doi.org/10.1038/s41586-020-2149-4