E. coli L-asparaginase II mutant (K162M) in complex with L-Asp at pH 5.6

Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.

Expressed variant contains 8 additional N-terminal residues MDHHHHHH (affinity tag) and mutation (K162M) in mature protein

L-asparaginase II,L-ASNase II,L-asparagine amidohydrolase II

Crystals were grown in 0.17 M NH4-citrate, pH 5.6, 17-18% PEG3350, 10 mM L-Asp

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY

inactive mutant, hydrolysis of L-asparagine, HYDROLASE