TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases
Florian Busch1, Chitra Rajendran, Olga Mayans
1Institute of Biophysics and Physical Biochemistry, University of Regensburg , Universitätsstrasse 31, D-93053 Regensburg, Germany.
Abstract:
The rapid increase of the number of sequenced genomes asks for the functional annotation of the encoded enzymes. We used a combined computational-structural approach to determine the function of the TrpB2 subgroup of the tryptophan synthase β chain/β chain-like TrpB1-TrpB2 family (IPR023026). The results showed that TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases, whereas TrpB1 enzymes catalyze the l-serine dependent synthesis of tryptophan. We found a single residue being responsible for the different substrate specificities of TrpB1 and TrpB2 and confirmed this finding by mutagenesis studies and crystallographic analysis of a TrpB2 enzyme with bound O-phospho-l-serine.
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