Norris, Andrew and Busch, Florian and Schupfner, Michael and Sterner, Reinhard and Wysocki, Vicki H. (2020) Quaternary Structure of the Tryptophan Synthase alpha-Subunit Homolog BX1 from Zea mays. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 31 (2). pp. 227-233. ISSN 1044-0305, 1879-1123
Full text not available from this repository. (Request a copy)Abstract
BX1 from Zea mays (zmBX1) is an enzyme of plant secondary metabolism that generates indole for the synthesis of plant defensins. It is a homologue of the tryptophan synthase alpha-subunit, TrpA. Whereas TrpA itself is a monomer in solution, zmBX1 is dimeric, confirmed in our work by native MS. Using cross-linking and mutagenesis, we identified the physiological dimerization interface of zmBX1. We found that homodimerization has only minor effects on catalysis and stability. A comparison of the zmBX1 zmBX1 homodimer and zmTrpA-zmTrpB heterodimer interfaces suggest that homodimerization in zmBX1 might, at an early point in evolution, have served as a mechanism to exclude the interaction with the tryptophan synthase beta-subunit (zmTrpB), marking its transition from primary to secondary metabolism.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ALLOSTERIC REGULATION; CROSS-LINKING; ASSEMBLIES; MECHANISM; CRYSTALS; COMPLEX; MASS; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 31 Mar 2021 07:15 |
| Last Modified: | 31 Mar 2021 07:15 |
| URI: | https://pred.uni-regensburg.de/id/eprint/45251 |
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