Literature summary for 3.4.22.71 extracted from

Maresso, A.W.; Wu, R.; Kern, J.W.; Zhang, R.; Janik, D.; Missiakas, D.M.; Duban, M.; Joachimiak, A.; Schneewind, O.
Activation of inhibitors by sortase triggers irreversible modification of the active site (2007), J. Biol. Chem., 282, 23129-23139.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
SrtB in complex with aryl (beta-amino)ethyl ketone inhibitors. Analysis of the three-dimensional structure ofBacillusanthracissortaseBwithandwithoutinhibitorprovidesinsights into the mechanism of inhibition	Bacillus anthracis

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	aryl (beta-amino)ethyl ketones inhibit sortase enzymes. Inhibition of sortases occurs through an irreversible, covalent modification of their active site cysteine. Sortases specifically activate this class of molecules via beta-elimination, generating a reactive olefin intermediate that covalently modifies the cysteine thiol	Bacillus anthracis

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	-	-	-

Synonyms

Synonyms	Comment	Organism
SrtB	-	Bacillus anthracis

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Release 2023.1 (January 2023)