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Literature summary for 2.3.2.2 extracted from

  • Wada, K.; Hiratake, J.; Irie, M.; Okada, T.; Yamada, C.; Kumagai, H.; Suzuki, H.; Fukuyama, K.
    Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists (2008), J. Mol. Biol., 380, 361-372.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with azaserine and acivicin, at 1.65 A resolution. Both inhibitors bind to the substrate-binding pocketand form a covalent bond with the Ogamma atom of residue T391. The two amido nitrogen atoms of Gly483 and Gly484, which form the oxyanion hole, interact with the inhibitors directly or via a water molecule. In the azaserine complex the carbon atom that forms a covalent bond with Thr391 is sp3-hybridized Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P18956
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