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Harms, E. et al.

A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis.

A threonine-12 to alanine mutant of E. coli asparaginase II (EC 3.5.1.1) has less than 0.01% of the activity of wild-type enzyme. Both tertiary and quaternary structure of the enzyme are essentially unaffected by the mutation; thus the activity loss seems to be the result of a direct impairment of catalytic function. As aspartate is still bound by the mutant enzyme, Thr-12 appears not be involved in substrate binding.[1]

References

A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis. Harms, E., Wehner, A., Aung, H.P., Röhm, K.H. FEBS Lett. (1991) [Pubmed]

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