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1: FEBS Lett. 1991 Jul 8;285(1):55-8.Click here to read Links

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

Harms E, Wehner A, Aung HP, Röhm KH.

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.

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.

PMID: 1906013 [PubMed - indexed for MEDLINE]

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