Structural and functional analysis of hyper-thermostable ancestral L-amino acid oxidase that can convert Trp derivatives to D-forms by chemoenzymatic reaction
Abstract Production of D-amino acids (D-AAs) on a large-scale enables to provide precursors of peptide therapeutics. In this study, we designed a novel L-amino acid oxidase, HTAncLAAO2, by ancestral sequence reconstruction, exhibiting high thermostability and long-term stability. The crystal structu...
Main Authors: | Yui Kawamura, Chiharu Ishida, Ryo Miyata, Azusa Miyata, Seiichiro Hayashi, Daisuke Fujinami, Sohei Ito, Shogo Nakano |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2023-09-01
|
Series: | Communications Chemistry |
Online Access: | https://doi.org/10.1038/s42004-023-01005-1 |
Similar Items
-
Chemoenzymatic synthesis of 3-ethyl-2,5-dimethylpyrazine by L-threonine 3-dehydrogenase and 2-amino-3-ketobutyrate CoA ligase/L-threonine aldolase
by: Tomoharu Motoyama, et al.
Published: (2021-07-01) -
Structure Prediction and Genome Mining‐Aided Discovery of the Bacterial C‐Terminal Tryptophan Prenyltransferase PalQ
by: Azusa Miyata, et al.
Published: (2024-02-01) -
Comprehensive mutagenesis to identify amino acid residues contributing to the difference in thermostability between two originally thermostable ancestral proteins
by: Satoshi Akanuma, et al.
Published: (2021-01-01) -
Development of Enzymes for Chemoenzymatic Synthesis
by: Chi-Huey Wong
Published: (1993-04-01) -
Challenges and career consequences of internationally educated nurses: Empirical research qualitative
by: Chiharu Miyata
Published: (2023-11-01)