Structural highlights
Function
[TRPB2_SULSO] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Publication Abstract from PubMed
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 beta chain/beta 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.
TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases.,Busch F, Rajendran C, Mayans O, Loffler P, Merkl R, Sterner R Biochemistry. 2014 Sep 30;53(38):6078-83. doi: 10.1021/bi500977y. Epub 2014 Sep, 17. PMID:25184516[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Busch F, Rajendran C, Mayans O, Loffler P, Merkl R, Sterner R. TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases. Biochemistry. 2014 Sep 30;53(38):6078-83. doi: 10.1021/bi500977y. Epub 2014 Sep, 17. PMID:25184516 doi:http://dx.doi.org/10.1021/bi500977y
