Literature summary for 3.5.1.1 extracted from

Jaskolski, M.; Kozak, M.; Lubkowski, J.; Palm, G.; Wlodawer, A.
Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups (2001), Acta Crystallogr. Sect. D, D57, 369-377.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant enzyme Y25F, untreated crystals and crystals soaked with L-hydroxylysine. Comparison with previously reported structures. The loop acting as a gate over the active site is very flexible. Its structure in the native enzyme is primarily controlled by the occupancy of the active site	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00805	-	-

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Release 2023.1 (January 2023)