ArticleApplied and environmental microbiology1997
Characterization of recombinant glutamine synthetase from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1.
Article in Applied and environmental microbiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 24 citations in OpenAlex.
- Differences in regulation mechanisms of glutamine synthetases from methanogenic archaea unveiled by structural investigations.Communications biology · 2024Article
- Feruloyl esterase immobilization in mesoporous silica particles and characterization in hydrolysis and transesterification.BMC biochemistry · 2018Article
- Genetic examination of initial amino acid oxidation and glutamate catabolism in the hyperthermophilic archaeon Thermococcus kodakarensis.Journal of bacteriology · 2013Article
- Genetic studies on the virus-like regions in the genome of hyperthermophilic archaeon, Thermococcus kodakarensis.Extremophiles : life under extreme conditions · 2013Article
- Nitrogen metabolism in haloarchaea.Saline systems · 2008Article
- beta-Glutamate as a substrate for glutamine synthetase.Applied and environmental microbiology · 2001Article
- A DNA ligase from a hyperthermophilic archaeon with unique cofactor specificity.Journal of bacteriology · 2000Article
- Characterization of DNA polymerase from Pyrococcus sp. strain KOD1 and its application to PCR.Applied and environmental microbiology · 1997Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glnA gene encoding glutamine synthetase was cloned from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1, and its nucleotide sequence was determined. The glnA gene was expressed in Escherichia coli ME8459 (glnA mutant strain), and the protein was purified to homogeneity and shown to be functional in a dodecameric from (637,000 Da), exhibiting both transferase and synthetase activities. However, kinetic studies indicated that the enzyme possessed low biosynthetic activity, suggesting that the reaction was biased towards glutamate production. The optimum temperature for both activities was 60 degrees C, which was lower than the optimal growth temperature of KOD1. Recombinant KOD1 GlnA exhibited different optimum pHs depending on the reaction employed (pH 7.8 for the synthetase reaction and pH 7.2 for the transferase reaction). Of the various nucleoside triphosphates tested, GTP as well as ATP was involved in the synthetase reaction.
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