Publikation: TrpB2 Enzymes are O-Phospho-l-serine Dependent Tryptophan Synthases
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2014
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Biochemistry. 2014, 53(38), pp. 6078-6083. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi500977y
Zusammenfassung
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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570 Biowissenschaften, Biologie
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BUSCH, Florian, Chitra RAJENDRAN, Olga MAYANS, Patrick LÖFFLER, Rainer MERKL, Reinhard STERNER, 2014. TrpB2 Enzymes are O-Phospho-l-serine Dependent Tryptophan Synthases. In: Biochemistry. 2014, 53(38), pp. 6078-6083. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi500977yBibTex
@article{Busch2014-09-30TrpB2-38702,
year={2014},
doi={10.1021/bi500977y},
title={TrpB2 Enzymes are O-Phospho-l-serine Dependent Tryptophan Synthases},
number={38},
volume={53},
issn={0006-2960},
journal={Biochemistry},
pages={6078--6083},
author={Busch, Florian and Rajendran, Chitra and Mayans, Olga and Löffler, Patrick and Merkl, Rainer and Sterner, Reinhard}
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<dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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