Optimal enzyme utilization suggests that concentrations and thermodynamics determine binding mechanisms and enzyme saturations.

Bibliographic Details
Title: Optimal enzyme utilization suggests that concentrations and thermodynamics determine binding mechanisms and enzyme saturations.
Authors: Sahin A; Laboratory of Computational Systems Biotechnology, Ecole Polytechnique Federale de Lausanne (EPFL), 1015, Lausanne, Switzerland., Weilandt DR; Laboratory of Computational Systems Biotechnology, Ecole Polytechnique Federale de Lausanne (EPFL), 1015, Lausanne, Switzerland.; Department of Chemistry and Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ, USA., Hatzimanikatis V; Laboratory of Computational Systems Biotechnology, Ecole Polytechnique Federale de Lausanne (EPFL), 1015, Lausanne, Switzerland. vassily.hatzimanikatis@epfl.ch.
Source: Nature communications [Nat Commun] 2023 May 05; Vol. 14 (1), pp. 2618. Date of Electronic Publication: 2023 May 05.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
Database: MEDLINE Complete
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Description
ISSN:2041-1723
DOI:10.1038/s41467-023-38159-4