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Literature summary for 2.4.2.14 extracted from

  • Wang, X.S.; Roitberg, A.E.; Richards, N.G.
    Computational studies of ammonia channel function in glutamine 5-phosphoribosylpyrophosphate amidotransferase (2009), Biochemistry, 48, 12272-12282.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
L415A mutant has reduced transfer efficiency. The L415A GPATase mutant-thioester-5'-phosphoribosylpyrophosphate complex after 39 ps, shows the leakage of ammonia into bulk solution Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AG16
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information GPATase-thioester-5'-phosphoribosylpyrophosphate complex model demonstrates the ammonia transfer between the active sites of GPATase in its active conformation. The ammonia channel in GPATase is a transient structural element, a pipe through which ammonia travels in the absence of an external driving potential. The ammonia tunnel in GPATase discriminates against ammonium ion Escherichia coli ?
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Synonyms

Synonyms Comment Organism
glutamine 5-phosphoribosylpyrophosphate amidotransferase
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Escherichia coli
GPATase
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Escherichia coli