Structure of glyoxysomal malate dehydrogenase (MDH3) from Saccharomyces cerevisiae

Mizushima, Tsunehiro ; Nishio, Kazuya ; et al.

In: Acta crystallographica. Section F, Structural biology communications, Jg. 74 (2018-03-19), Heft Pt 10

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Malate dehydrogenase (MDH), a carbohydrate and energy metabolism enzyme in eukaryotes, catalyzes the interconversion of malate to oxaloacetate (OAA) in conjunction with that of nicotinamide adenine dinucleotide (NAD+) to NADH. Three isozymes of MDH have been reported inSaccharomyces cerevisiae: MDH1, MDH2 and MDH3. MDH1 is a mitochondrial enzyme and a member of the tricarboxylic acid cycle, whereas MDH2 is a cytosolic enzyme that functions in the glyoxylate cycle. MDH3 is a glyoxysomal enzyme that is involved in the reoxidation of NADH, which is produced during fatty-acid β-oxidation. The affinity of MDH3 for OAA is lower than those of MDH1 and MDH2. Here, the crystal structures of yeast apo MDH3, the MDH3–NAD+complex and the MDH3–NAD+–OAA ternary complex were determined. The structure of the ternary complex suggests that the active-site loop is in the open conformation, differing from the closed conformations in mitochondrial and cytosolic malate dehydrogenases.

Structure of glyoxysomal malate dehydrogenase (MDH3) from Saccharomyces cerevisiae

Malate dehydrogenase (MDH), a carbohydrate and energy metabolism enzyme in eukaryotes, catalyzes the interconversion of malate to oxaloacetate (OAA) in conjunction with that of nicotinamide adenine dinucleotide (NAD⁺) to NADH. Three isozymes of MDH have been reported in Saccharomyces cerevisiae: MDH1, MDH2 and MDH3. MDH1 is a mitochondrial enzyme and a member of the tricarboxylic acid cycle, whereas MDH2 is a cytosolic enzyme that functions in the glyoxylate cycle. MDH3 is a glyoxysomal enzyme that is involved in the reoxidation of NADH, which is produced during fatty‐acid β‐oxidation. The affinity of MDH3 for OAA is lower than those of MDH1 and MDH2. Here, the crystal structures of yeast apo MDH3, the MDH3–NAD⁺ complex and the MDH3–NAD⁺–OAA ternary complex were determined. The structure of the ternary complex suggests that the active‐site loop is in the open conformation, differing from the closed conformations in mitochondrial and cytosolic malate dehydrogenases.

malate dehydrogenase; glyoxysome; fatty‐acid β‐oxidation; X‐ray crystallography; MDH3; Saccharomyces cerevisiae

The full text for this article, hosted at http://journals.iucr.org, is unavailable due to technical difficulties.

Supporting Information

Supporting information for this article can be found http://scripts.iucr.org/cgi-bin/paper?nw5076

By Shu Moriyama; Kazuya Nishio and Tsunehiro Mizushima

Titel:	Structure of glyoxysomal malate dehydrogenase (MDH3) from Saccharomyces cerevisiae
Autor/in / Beteiligte Person:	Mizushima, Tsunehiro ; Nishio, Kazuya ; Moriyama, Shu
Link:	Volltext (PDF) View record in OpenAIRE (Volltext) https://pubmed.ncbi.nlm.nih.gov/30279312
Zeitschrift:	Acta crystallographica. Section F, Structural biology communications, Jg. 74 (2018-03-19), Heft Pt 10
Veröffentlichung:	2018
Medientyp:	unknown
ISSN:	2053-230X (print)
Schlagwort:	0301 basic medicine Models, Molecular Oxaloacetic Acid Protein Conformation, alpha-Helical Malates Gene Expression Nicotinamide adenine dinucleotide Crystallography, X-Ray Biochemistry Substrate Specificity Research Communications chemistry.chemical_compound Apoenzymes Structural Biology Malate Dehydrogenase Catalytic Domain Citrate synthase Cloning, Molecular Ternary complex chemistry.chemical_classification biology Chemistry Condensed Matter Physics Recombinant Proteins Isoenzymes Protein Binding Saccharomyces cerevisiae Proteins Genetic Vectors Biophysics Glyoxylate cycle Saccharomyces cerevisiae Malate dehydrogenase 03 medical and health sciences Oxidoreductase Genetics Escherichia coli Protein Interaction Domains and Motifs Amino Acid Sequence 030102 biochemistry & molecular biology Sequence Homology, Amino Acid NAD Citric acid cycle 030104 developmental biology Glyoxysomes biology.protein Protein Conformation, beta-Strand NAD+ kinase Protein Multimerization Sequence Alignment
Sonstiges:	Nachgewiesen in: OpenAIRE Rights: OPEN

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