Abstract: raw data from activity assays for different variant of an ω-transaminase with different substrates and their pH- and temperature optimum, as well as their temperature stability. Structural prediction of the enzyme variants, performed with AlphaFold are also included.
License: CC0 1.0 Universal (Creative Commons Public Domain Dedication)
DOI: 10.5447/ipk/2023/12
| N70E | |
| S17P | |
| S17PN70E | |
| S17PT38V | |
| S17PT38VN70E | |
| S17PT38VY47T | |
| S17PY47T | |
| S17PY47TN70E | |
| T317V | |
| T38V | |
| T38VN70E | |
| T38VY47T | |
| T38VY47TN70E | |
| WT | |
| Y47T | |
| Y47TN70E | |
| raw data.ods | 77.8 KB |
| readme.txt | 5 KB |
| CONTRIBUTOR: |
Nicolaus von Wirén,
Marion Rauter,
Gotthard Kunze
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| CREATOR: |
Uwe Wegner
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| PUBLISHER: | e!DAL - Plant Genomics and Phenomics Research Data Repository (PGP), IPK Gatersleben, Seeland OT Gatersleben, Corrensstraße 3, 06466, Germany |
| SIZE: | 0 B |
| SUBJECT: | ω-transaminase, Sphaerobacter thermophilus, ß- and γ-amino acids, kinetic resolution |