The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction

10.1042/BJ20140679

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Main Authors:	Ceh-Pavia, E, Ang, S.K, Spiller, M.P, Lu, H
Other Authors:	BIOLOGICAL SCIENCES
Format:	Article
Published:	Portland Press 2020
Subjects:	cytochrome c dimer fungal enzyme histidine mutant protein oligomer tetramer thiol oxidase tryptophan coenzyme cytochrome reductase GFER protein, human protein binding Article autosomal recessive disorder catalysis circular dichroism denaturation enzyme activity essential for respiration and viability 1 gene fluorescence spectroscopy fungal gene fungal strain gel filtration chromatography gene mutation hydrogen bond light scattering melting point molecular weight multiangle laser light scattering myopathy nonhuman oligomerization oxidation reduction reaction oxidation reduction state oxygen consumption pH protein conformation protein quaternary structure protein tertiary structure protein unfolding proton transport respiratory chain site directed mutagenesis temperature dependence thermostability ultraviolet spectroscopy wild type yeast amino acid sequence amino acid substitution chemical structure chemistry enzyme active site genetics human metabolism missense mutation molecular genetics muscle disease sequence homology Amino Acid Sequence Amino Acid Substitution Catalysis Catalytic Domain Coenzymes Cytochrome Reductases Humans Models, Molecular Molecular Sequence Data Muscular Diseases Mutation, Missense Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/183892
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1838922024-04-03T10:35:32Z The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction Ceh-Pavia, E Ang, S.K Spiller, M.P Lu, H BIOLOGICAL SCIENCES cytochrome c dimer fungal enzyme histidine mutant protein oligomer tetramer thiol oxidase tryptophan coenzyme cytochrome reductase GFER protein, human protein binding Article autosomal recessive disorder catalysis circular dichroism denaturation enzyme activity essential for respiration and viability 1 gene fluorescence spectroscopy fungal gene fungal strain gel filtration chromatography gene mutation hydrogen bond light scattering melting point molecular weight multiangle laser light scattering myopathy nonhuman oligomerization oxidation reduction reaction oxidation reduction state oxygen consumption pH protein conformation protein quaternary structure protein tertiary structure protein unfolding proton transport respiratory chain site directed mutagenesis temperature dependence thermostability ultraviolet spectroscopy wild type yeast amino acid sequence amino acid substitution catalysis chemical structure chemistry coenzyme enzyme active site genetics human metabolism missense mutation molecular genetics muscle disease sequence homology Amino Acid Sequence Amino Acid Substitution Catalysis Catalytic Domain Coenzymes Cytochrome Reductases Humans Models, Molecular Molecular Sequence Data Muscular Diseases Mutation, Missense Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid 10.1042/BJ20140679 Biochemical Journal 464 3 449-459 2020-11-23T08:56:41Z 2020-11-23T08:56:41Z 2014 Article Ceh-Pavia, E, Ang, S.K, Spiller, M.P, Lu, H (2014). The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction. Biochemical Journal 464 (3) : 449-459. ScholarBank@NUS Repository. https://doi.org/10.1042/BJ20140679 0264-6021 https://scholarbank.nus.edu.sg/handle/10635/183892 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Portland Press Unpaywall 20201031
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	cytochrome c dimer fungal enzyme histidine mutant protein oligomer tetramer thiol oxidase tryptophan coenzyme cytochrome reductase GFER protein, human protein binding Article autosomal recessive disorder catalysis circular dichroism denaturation enzyme activity essential for respiration and viability 1 gene fluorescence spectroscopy fungal gene fungal strain gel filtration chromatography gene mutation hydrogen bond light scattering melting point molecular weight multiangle laser light scattering myopathy nonhuman oligomerization oxidation reduction reaction oxidation reduction state oxygen consumption pH protein conformation protein quaternary structure protein tertiary structure protein unfolding proton transport respiratory chain site directed mutagenesis temperature dependence thermostability ultraviolet spectroscopy wild type yeast amino acid sequence amino acid substitution catalysis chemical structure chemistry coenzyme enzyme active site genetics human metabolism missense mutation molecular genetics muscle disease sequence homology Amino Acid Sequence Amino Acid Substitution Catalysis Catalytic Domain Coenzymes Cytochrome Reductases Humans Models, Molecular Molecular Sequence Data Muscular Diseases Mutation, Missense Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid
spellingShingle	cytochrome c dimer fungal enzyme histidine mutant protein oligomer tetramer thiol oxidase tryptophan coenzyme cytochrome reductase GFER protein, human protein binding Article autosomal recessive disorder catalysis circular dichroism denaturation enzyme activity essential for respiration and viability 1 gene fluorescence spectroscopy fungal gene fungal strain gel filtration chromatography gene mutation hydrogen bond light scattering melting point molecular weight multiangle laser light scattering myopathy nonhuman oligomerization oxidation reduction reaction oxidation reduction state oxygen consumption pH protein conformation protein quaternary structure protein tertiary structure protein unfolding proton transport respiratory chain site directed mutagenesis temperature dependence thermostability ultraviolet spectroscopy wild type yeast amino acid sequence amino acid substitution catalysis chemical structure chemistry coenzyme enzyme active site genetics human metabolism missense mutation molecular genetics muscle disease sequence homology Amino Acid Sequence Amino Acid Substitution Catalysis Catalytic Domain Coenzymes Cytochrome Reductases Humans Models, Molecular Molecular Sequence Data Muscular Diseases Mutation, Missense Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid Ceh-Pavia, E Ang, S.K Spiller, M.P Lu, H The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction
description	10.1042/BJ20140679
author2	BIOLOGICAL SCIENCES
author_facet	BIOLOGICAL SCIENCES Ceh-Pavia, E Ang, S.K Spiller, M.P Lu, H
format	Article
author	Ceh-Pavia, E Ang, S.K Spiller, M.P Lu, H
author_sort	Ceh-Pavia, E
title	The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction
title_short	The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction
title_full	The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction
title_fullStr	The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction
title_full_unstemmed	The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction
title_sort	disease-associated mutation of the mitochondrial thiol oxidase erv1 impairs cofactor binding during its catalytic reaction
publisher	Portland Press
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/183892
_version_	1795374614171353088

The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction

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