NDLI: Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum

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Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum

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Characterization of malate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum

Content Provider	Springer Nature Link
Author	Yennaco, Lynda J. Hu, Yajing Holden, James F.
Copyright Year	2007
Abstract	Native and recombinant malate dehydrogenase (MDH) was characterized from the hyperthermophilic, facultatively autotrophic archaeon Pyrobaculum islandicum. The enzyme is a homotetramer with a subunit mass of 33 kDa. The activity kinetics of the native and recombinant proteins are the same. The apparent K m values of the recombinant protein for oxaloacetate (OAA) and NADH (at 80°C and pH 8.0) were 15 and 86 μM, respectively, with specific activity as high as 470 U mg−1. Activity decreased more than 90% when NADPH was used. The catalytic efficiency of OAA reduction by P. islandicum MDH using NADH was significantly higher than that reported for any other archaeal MDH. Unlike other archaeal MDHs, specific activity of the P. islandicum MDH back-reaction also decreased more than 90% when malate and NAD+ were used as substrates and was not detected with NADP+. A phylogenetic tree of 31 archaeal MDHs shows that they fall into 5 distinct groups separated largely along taxonomic lines suggesting minimal lateral mdh transfer between Archaea.
Starting Page	741
Ending Page	746
Page Count	6
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	11
Issue Number	5
e-ISSN	14334909
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-05-09
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Malate dehydrogenase Pyrobaculum islandicum Archaea Citric acid cycle Autotrophy Ecology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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