TrpB2 Enzymes are O-Phospho-l-serine Dependent Tryptophan Synthases | Zendy

Florian Büsch | Zendy; Chitra Rajendran | Zendy; Olga Mayans | Zendy; Patrick Löffler | Zendy; Rainer Merkl | Zendy; Reinhard Sterner | Zendy

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TrpB2 Enzymes are O-Phospho-l-serine Dependent Tryptophan Synthases

Author(s) -

Florian Büsch,

Chitra Rajendran,

Olga Mayans,

Patrick Löffler,

Rainer Merkl,

Reinhard Sterner

Publication year - 2014

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi500977y

Subject(s) - serine , tryptophan synthase , enzyme , tryptophan , biochemistry , chemistry , residue (chemistry) , mutagenesis , stereochemistry , biology , amino acid , gene , mutation

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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