Structure of glyoxysomal malate dehydrogenase (MDH3) from Saccharomyces cerevisiae.
Acta Crystallogr F Struct Biol Commun
; 74(Pt 10): 617-624, 2018 Oct 01.
Article
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| MEDLINE
| ID: mdl-30279312
ABSTRACT
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 ß-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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
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Ácido Oxaloacético
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Proteínas de Saccharomyces cerevisiae
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Malato Deshidrogenasa
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Malatos
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NAD
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Año:
2018
Tipo del documento:
Article
País de afiliación:
Japón