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Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity.

Schneider, Birgit ; Knöchel, Thorsten ; Darimont, Beatrice ; Hennig, Michael ; Dietrich, Susanne ; Babinger, Karin ; Kirschner, Kasper ; Sterner, Reinhard



Abstract

Indole-3-glycerol phosphate synthase (IGPS) catalyzes the fifth step in the biosynthesis of tryptophan. It belongs to the large and versatile family of (betaalpha)(8)-barrel enzymes but has an unusual N-terminal extension of about 40 residues. Limited proteolysis with trypsin of IGPS from both Sulfolobus solfataricus (sIGPS) and Thermotoga maritima (tIGPS) removes about 25 N-terminal residues and ...

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