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Novel inhibitory function of the rhizomucor miehei lipase propeptide and three-dimensional structures of its complexes with the enzyme

DOI: 10.1021/acsomega.9b00612 DOI Help

Authors: Olga V. Moroz (University of York) , Elena Blagova (University of York) , Verena Reiser (Novozymes A/S) , Rakhi Saikia (Novozymes A/S) , Sohel Dalal (Novozymes A/S) , Christian Isak Jørgensen (Novozymes A/S) , Vikram K. Bhatia (Novozymes A/S) , Lone Baunsgaard (Novozymes A/S) , Birgitte Andersen (Novozymes A/S) , Allan Svendsen (Novozymes A/S) , Keith S. Wilson (University of York)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Acs Omega , VOL 4 , PAGES 9964 - 9975

State: Published (Approved)
Published: June 2019
Diamond Proposal Number(s): 7864 , 9948

Open Access Open Access

Abstract: Many proteins are synthesized as precursors, with propeptides playing a variety of roles such as assisting in folding or preventing them from being active within the cell. While the precise role of the propeptide in fungal lipases is not completely understood, it was previously reported that mutations in the propeptide region of the Rhizomucor miehei lipase have an influence on the activity of the mature enzyme, stressing the importance of the amino acid composition of this region. We here report two structures of this enzyme in complex with its propeptide, which suggests that the latter plays a role in the correct maturation of the enzyme. Most importantly, we demonstrate that the propeptide shows inhibition of lipase activity in standard lipase assays and propose that an important role of the propeptide is to ensure that the enzyme is not active during its expression pathway in the original host.

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength)

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