4eca | pdb_00004eca
ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE
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Overview
Escherichia coli asparaginase II catalyzes the hydrolysis of L-asparagine, to L-aspartate via a threonine-bound acyl-enzyme intermediate. A nearly, inactive mutant in which one of the active site threonines, Thr-89, was, replaced by valine was constructed, expressed, and crystallized. Its, structure, solved at 2.2 A resolution, shows high overall similarity to, the wild-type enzyme, but an aspartyl moiety is covalently bound to, Thr-12, resembling a reaction intermediate. Kinetic analysis confirms the, deacylation deficiency, which is also explained on a structural basis. The, previously identified oxyanion hole is described in more detail.
About this Structure
4ECA is a Single protein structure of sequence from Escherichia coli. Active as Asparaginase, with EC number 3.5.1.1 Known structural/functional Sites: AS, BS, CS and DS. Full crystallographic information is available from OCA.
Reference
A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant., Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A, FEBS Lett. 1996 Jul 22;390(2):211-6. PMID:8706862
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