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Article

Identification of catalytically important residues in the active site of Escherichia coli transaldolase.

European journal of biochemistry - 1 Apr 2001

Schörken U, Thorell S, Schürmann M, Jia J, Sprenger G A, Schneider G

Abstract excerpt

The roles of invariant residues at the active site of transaldolase B from Escherichia coli have been probed by site-directed mutagenesis. The mutant enzymes D17A, N35A, E96A, T156A, and S176A were purified from a talB-deficient host and analyzed with respect to their 3D structure and kinetic behavior. X-ray analysis showed that side chain replacement did not induce unanticipated structural changes in the mutant...

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PMID: 11298760
DOI: 10.1046/j.1432-1327.2001.02128.x

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