Busch, Florian and Rajendran, Chitra and Heyn, Kristina and Schlee, Sandra and Merkl, Rainer and Sterner, Reinhard (2016) Ancestral Tryptophan Synthase Reveals Functional Sophistication of Primordial Enzyme Complexes. CELL CHEMICAL BIOLOGY, 23 (6). pp. 709-715. ISSN 2451-9448,
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Modern enzyme complexes are characterized by a high catalytic efficiency and allosteric communication between the constituting protein subunits. We were interested in whether primordial enzyme complexes from extinct species displayed a similar degree of functional sophistication. To this end, we used ancestral sequence reconstruction to resurrect the alpha and beta subunits of the tryptophan synthase (TS) complex from the last bacterial common ancestor (LBCA), which presumably existed more than 3.4 billion years ago. We show that the LBCA TS subunits are thermostable and exhibit high catalytic activity. Moreover, they form a complex with abba stoichiometry whose crystal structure is similar to that of modern TS. Kinetic analysis revealed that the reaction intermediate indole is channeled from the a to the b subunits and suggests that allosteric communication already occurred in LBCA TS.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ALLOSTERIC REGULATION; MULTIENZYME COMPLEX; MOLECULAR-GRAPHICS; SEQUENCE ALIGNMENT; ESCHERICHIA-COLI; BIENZYME COMPLEX; RECONSTRUCTION; MECHANISM; EVOLUTION; SOFTWARE; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Rainer Merkl |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 08 Apr 2019 08:57 |
| Last Modified: | 08 Apr 2019 08:57 |
| URI: | https://pred.uni-regensburg.de/id/eprint/3750 |
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