ArticleMolecular biology reports2000
The evolution of glutamate synthase.
Article in Molecular biology reports, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Identification and characterization of the glutamine synthetase gene family in oat (Frontiers in plant science · 2025Article
- Mechanism for nitrogen isotope fractionation during ammonium assimilation by Escherichia coli K12.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Quantitative analysis of cell-type specific gene expression in the green alga Volvox carteri.BMC genomics · 2006Article
- Crystallization and structural analysis of GADPH from Spinacia oleracea in a new form.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Semi-anaerobic growth conditions are favoured by some Escherichia coli strains during heterologous expression of some archaeal proteins.Molecular biology reports · 2006Article
- Glutamate synthase: structural, mechanistic and regulatory properties, and role in the amino acid metabolism.Photosynthesis research · 2005Review
- Glutamate synthase: an archaeal horizontal gene transfer?Journal of biosciences · 2001Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA coding for the ferredoxin-dependent glutamate synthase (EC 1.4.7.1) of spinach chloroplasts has been cloned and sequenced. It consists of 5015 bp and starts with the codon for the N-terminal cysteine of the mature protein. Ferredoxin-dependent glutamate synthase is one of the key enzymes in the early stages of ammonia assimilation in plants, algae and cyanobacteria. In addition to the ferredoxin-dependent enzyme, there are two other forms of glutamate synthase, one of which uses NADH as the electron donor and a second that uses NADPH. Although all three forms catalyze the reductive transamidation of the amido nitrogen from glutamine to 2-oxoglutarate to form two molecules of glutamate, ferredoxin-dependent glutamate synthases differ from the NADH and NADPH-dependent forms in subunit composition and amino acid sequence. The recent availability of sequence data for glutamate synthases from spinach and from two archael species has produced a clearer and more detailed picture of the evolution of this key enzyme in nitrogen metabolism and the origins of the two subunit/domain structure of the enzyme.
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