Abstract 1794 Artificial and Disease-Causing Mutations of Opa1 Modify Enzyme Kinetics

Dynamin Superfamily Proteins (DSPs) are members of a diverse class of enzymes involved in the remodeling of cellular membranes. All DSPs are characterized by the inclusion of 1) an N-terminal GTPase domain (G-domain) responsible for transforming chemical into conformational energy and dimerization, 2) a Middle domain responsible for oligomerization, and 3) a lipid-interacting domain (LID). One such DSP, Opa1, is involved in the fusion of the inner membrane of the mitochondria, relying on interactions with the anionic lipid cardiolipin.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109149
Primary Topic
Biochemical and Molecular Research
Type
article
Field-Weighted Citation Impact
0.00
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Abstract 1794 Artificial and Disease-Causing Mutations of Opa1 Modify Enzyme Kinetics

Andrew D. Kehr, Joyce C. Lockhart, Nathaniel Roethler, Alian Leon-Jaramillo et al.
Journal of Biological Chemistry
Biochemical and Molecular Research
article

Abstract 1794 Artificial and Disease-Causing Mutations of Opa1 Modify Enzyme Kinetics

Andrew D. Kehr, Joyce C. Lockhart, Nathaniel Roethler, Alian Leon-Jaramillo, Arturo Perez-Dolores
article en

Abstract

Dynamin Superfamily Proteins (DSPs) are members of a diverse class of enzymes involved in the remodeling of cellular membranes. All DSPs are characterized by the inclusion of 1) an N-terminal GTPase domain (G-domain) responsible for transforming chemical into conformational energy and dimerization, 2) a Middle domain responsible for oligomerization, and 3) a lipid-interacting domain (LID). One such DSP, Opa1, is involved in the fusion of the inner membrane of the mitochondria, relying on interactions with the anionic lipid cardiolipin.

Journal of Biological ChemistryVol. 301(5)
Washburn University (US), Auburn University (US)
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Biochemical and Molecular Research
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