Literature summary for 2.5.1.47 extracted from

Benoni, R.; Beck, C.M.; Garza-Sanchez, F.; Bettati, S.; Mozzarelli, A.; Hayes, C.S.; Campanini, B.
Activation of an anti-bacterial toxin by the biosynthetic enzyme CysK mechanism of binding, interaction specificity and competition with cysteine synthase (2017), Sci. Rep., 7, 8817 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABK5	-	-
Escherichia coli K12	P0ABK5	-	-

General Information

General Information	Comment	Organism
physiological function	the binding interaction of CdiA-CT toxin from uropathogenic Escherichia coli 536 with CysK mimics the cysteine synthase complex of CysK:CysE. The C-terminal tails of CysE and CdiA-CT each insert into the CysK active-site cleft to anchor the respective complexes. The dissociation constant for CysK:CdiA-CT is comparable to that of the Escherichia coli cysteine synthase complex, and both complexes bind through a two-step mechanism with a slow isomerization phase after the initial encounter. CdiA-CT can effectively displace CysE from pre-formed cysteine synthase complexes, enabling toxin activation even in the presence of excess competing CysE	Escherichia coli

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Release 2023.1 (January 2023)