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Literature summary for 6.3.4.4 extracted from

  • Bouyoub, A.; Barbier, G.; Forterre, P.; Labedan, B.
    The adenylosuccinate synthetase from the hyperthermophilic archaeon Pyrococcus species displays unusual structural features (1996), J. Mol. Biol., 261, 144-154.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli. The archaeal adenylosuccinate synthetase has a significant number of substitutions in residues that are conserved in all other homologous enzymes from bacteria to man. Despite theses differences the purA-like archaeal gene seems to be normally expressed and its product functions in vivo in bacteria, since it complements an Escherichia coli purA auxotroph Pyrococcus sp.
the archaeal adenylosuccinate synthase has a significant number of substitutions in residues that are conserved in all other homologous enzymes from bacteria to human. In Escherichia coli, the conserved residues are essential for catalytic activity and/or for the folded structure of the homodimer. Despite these drastic differences, the purA-like archaeal gene is normally expressed and its product functions in vivo in bacteria, since it complements an Escherichia coli purA auxotroph Pyrococcus sp.

Organism

Organism UniProt Comment Textmining
Pyrococcus sp. Q59726
-
-
Pyrococcus sp. ST700 Q59726
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-

Synonyms

Synonyms Comment Organism
purA
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Pyrococcus sp.