Thermococcus sp. KS-1 PPIase as a fusion partner improving soluble production of aromatic amino acid decarboxylase

Thermococcus sp. KS-1 PPIase as a fusion partner improving soluble production of aromatic amino acid decarboxylase

Abstract Peptidyl-prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) catalyzes the racemization reaction of proline residues on a polypeptide chain. This enzyme is also known to function as a molecular chaperon to stabilize protein conformation during the folding process. In this study, we noted FK506...

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Bibliographic Details
Main Authors: Takashi Koyanagi, Ayumi Hara, Kanako Kobayashi, Yuji Habara, Akira Nakagawa, Hiromichi Minami, Takane Katayama, Norihiko Misawa
Format: Article
Language:English
Published: SpringerOpen 2021-12-01
Series:AMB Express
Subjects:
Peptidyl-prolyl cis-trans isomerase (PPIase)
Molecular chaperon
Thermococcus sp. strain KS-1
Aromatic amino acid decarboxylase
Escherichia coli
Online Access:https://doi.org/10.1186/s13568-021-01340-3

Internet

https://doi.org/10.1186/s13568-021-01340-3

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