Title : Engineering of Escherichia coli L-serine O-acetyltransferase on the basis of crystal structure: desensitization to feedback inhibition by L-cysteine.

Pub. Date : 2006 Apr

PMID : 16459339






3 Functional Relationships(s)
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1 The crystal structure and the reaction mechanism of SAT from E.coli have shown that the substrate L-serine and the inhibitor L-cysteine bind to the identical region in the SAT protein. Serine streptothricin acetyltransferase Escherichia coli
2 The crystal structure and the reaction mechanism of SAT from E.coli have shown that the substrate L-serine and the inhibitor L-cysteine bind to the identical region in the SAT protein. Serine streptothricin acetyltransferase Escherichia coli
3 To decrease the affinity for only L-cysteine, we first built the structure model of L-serine-binding SAT on the basis of the crystal structure with bound L-cysteine and compared these two structures. Serine streptothricin acetyltransferase Escherichia coli