Busch, Florian and Rajendran, Chitra and Mayans, Olga and Loeffler, Patrick and Merkl, Rainer and Sterner, Reinhard (2014) TrpB2 Enzymes are O-Phospho-L-serine Dependent Tryptophan Synthases. BIOCHEMISTRY, 53 (38). pp. 6078-6083. ISSN 0006-2960,
Full text not available from this repository. (Request a copy)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 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | AEROPYRUM-PERNIX K1; ARCHAEON THERMOCOCCUS-KODAKARAENSIS; HYPERTHERMOPHILIC ARCHAEON; ESCHERICHIA-COLI; BIENZYME COMPLEX; BETA-SUBUNIT; ACETYLSERINE SULFHYDRYLASE; 3-DIMENSIONAL STRUCTURE; SALMONELLA-TYPHIMURIUM; MOLECULAR-GRAPHICS; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 13 Aug 2019 11:43 |
| Last Modified: | 13 Aug 2019 11:43 |
| URI: | https://pred.uni-regensburg.de/id/eprint/9525 |
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