Chaperonin GroEL hydrolyses ortho -nitrophenyl β-galactoside

We serendipitously found that chaperonin GroEL can hydrolyze -nitrophenyl β-galactoside (ONPG), a well-known substrate of the enzyme β-galactosidase. The ONPG hydrolysis by GroEL follows typical enzyme kinetics. Our experiments and molecular docking studies suggest ONPG binding at the ATP binding si...

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Veröffentlicht in:	Organic & biomolecular chemistry 2023-08, Vol.21 (30), p.6120-6123
Hauptverfasser:	Hashim, P K, Dokainish, Hisham M, Tamaoki, Nobuyuki
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Binding Sites Chaperonins - metabolism Galactosidase Galactosides Hydrolysis Molecular docking Molecular Docking Simulation Protein Folding Substrates β-Galactosidase
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Zusammenfassung:	We serendipitously found that chaperonin GroEL can hydrolyze -nitrophenyl β-galactoside (ONPG), a well-known substrate of the enzyme β-galactosidase. The ONPG hydrolysis by GroEL follows typical enzyme kinetics. Our experiments and molecular docking studies suggest ONPG binding at the ATP binding site of GroEL.
ISSN:	1477-0520 1477-0539
DOI:	10.1039/d3ob00989k