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Literature summary for 6.3.4.2 extracted from

  • Endrizzi, J.A.; Kim, H.; Anderson, P.M.; Baldwin, E.P.
    Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets (2004), Biochemistry, 43, 6447-6463.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
2.3 A resolution crystal structure of apoenzyme using Hg-multiwavelength anomalous dispersion phasing, vapor diffusion method, crystals belong to space group P2(1)2(1)2(1), in which each bifunctional monomer contains a dethiobiotin synthetase-like amidoligase N-terminal domain and a type 1 glutamine amidotransferase C-terminal domain Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A7E5
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Synonyms

Synonyms Comment Organism
CTPS
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Escherichia coli