ArticleMolecular biology reports2014
Expression, purification, and characterization of recombinant mangrove glutamine synthetase.
Article in Molecular biology reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 9 citations in OpenAlex.
- Article
- Functional Analysis of a Glutamine Biosynthesis Protein from a Psychrotrophic Bacterium,Indian journal of microbiology · 2020Article
- Light intensity affects the uptake and metabolism of glycine by pakchoi (Brassica chinensis L.).Scientific reports · 2016Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
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Abstract
To expand our knowledge about the relationship of nitrogen use efficiency and glutamine synthetase (GS) activity in the mangrove plant, a cytosolic GS gene from Avicennia marina has been heterologously expressed in and purified from Escherichia coli. Synthesis of the mangrove GS enzyme in E. coli was demonstrated by functional genetic complementation of a GS deficient mutant. The subunit molecular mass of GSI was ~40 kDa. Optimal conditions for biosynthetic activity were found to be 35 °C at pH 7.5. The Mg(2+)-dependent biosynthetic activity was strongly inhibited by Ni(2+), Zn(2+), and Al(3+), whereas was enhanced by Co(2+). The apparent K m values of AmGLN1 for the substrates in the biosynthetic assay were 3.15 mM for glutamate, and 2.54 mM for ATP, 2.80 mM for NH4 (+) respectively. The low affinity kinetics of AmGLN1 apparently participates in glutamine synthesis under the ammonium excess conditions.
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