Properties of Malic Enzyme from the Aerobic Methanotroph Methylosinus trichosporium.
Journal
Biochemistry. Biokhimiia
ISSN: 1608-3040
Titre abrégé: Biochemistry (Mosc)
Pays: United States
ID NLM: 0376536
Informations de publication
Date de publication:
Apr 2019
Apr 2019
Historique:
entrez:
24
6
2019
pubmed:
24
6
2019
medline:
27
6
2019
Statut:
ppublish
Résumé
Recombinant malic enzyme from the aerobic methanotroph Methylosinus trichosporium was obtained by heterologous expression in Escherichia coli and purified by affinity metal-chelating chromatography. The homohexameric enzyme of 6×80 kDa catalyzed the reversible reaction of oxidative decarboxylation of malate to pyruvate in the presence of mono- and divalent cations and NADP+ as a cofactor. The k
Identifiants
pubmed: 31228930
pii: BCM84040532
doi: 10.1134/S0006297919040060
doi:
Substances chimiques
Recombinant Proteins
0
NADP
53-59-8
Pyruvic Acid
8558G7RUTR
Malate Dehydrogenase
EC 1.1.1.37
malate dehydrogenase (decarboxylating)
EC 1.1.1.39
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM