Literature summary for 3.4.19.13 extracted from

Ida, T.; Suzuki, H.; Fukuyama, K.; Hiratake, J.; Wada, K.
Structure of Bacillus subtilis ?-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue. (2014), Acta Crystallogr. Sect. D, 70, 607-614.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with acivicin, to 1.8 A resolution. Acivicin is bound covalently through its C3 atom with sp2 hybridization to Thr403 Ogamma, the catalytic nucleophile of the enzyme	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P54422	enzyme displays both glutathione hydrolase and gamma-glutamyl transpeptidase activity, EC 2.3.2.2	-
Bacillus subtilis 168	P54422	enzyme displays both glutathione hydrolase and gamma-glutamyl transpeptidase activity, EC 2.3.2.2	-

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Release 2023.1 (January 2023)