Renaturation of 1-Aminocyclopropane-1-carboxylate Synthase Expressed inEscherichia coliin the Form of Inclusion Bodies into a Dimeric and Catalytically Active Enzyme

1998 ◽  
Vol 12 (3) ◽  
pp. 305-314 ◽  
Author(s):  
Susan Huxtable ◽  
Huiqing Zhou ◽  
Susanna Wong ◽  
Ning Li
Keyword(s):  
Inclusion Bodies ◽  
Active Enzyme ◽  
Catalytically Active

Fusion of a Coiled-Coil Domain Facilitates the High-Level Production of Catalytically Active Enzyme Inclusion Bodies

ChemCatChem ◽  
2015 ◽  
Vol 8 (1) ◽  
pp. 142-152 ◽  
Author(s):  
Martin Diener ◽  
Benita Kopka ◽  
Martina Pohl ◽  
Karl-Erich Jaeger ◽  
Ulrich Krauss
Keyword(s):  
Inclusion Bodies ◽  
Coiled Coil ◽  
Active Enzyme ◽  
Coiled Coil Domain ◽  
Catalytically Active ◽  
High Level ◽  
Level Production

Catalytically-active inclusion bodies—Carrier-free protein immobilizates for application in biotechnology and biomedicine

2017 ◽  
Vol 258 ◽  
pp. 136-147 ◽  
Author(s):  
Ulrich Krauss ◽  
Vera D. Jäger ◽  
Martin Diener ◽  
Martina Pohl ◽  
Karl-Erich Jaeger
Keyword(s):  
Inclusion Bodies ◽  
Free Protein ◽  
Active Inclusion Bodies ◽  
Carrier Free ◽  
Catalytically Active

High-level synthesis of recombinant HIV-1 protease and the recovery of active enzyme from inclusion bodies

Gene ◽  
1990 ◽  
Vol 87 (2) ◽  
pp. 243-248 ◽  
Author(s):  
Yih-Shyun E. Cheng ◽  
Michell H. McGowan ◽  
Charles A. Kettner ◽  
John V. Schloss ◽  
Susan Erickson-Viitanen ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Active Enzyme ◽  
High Level Synthesis ◽  
High Level ◽  
Hiv 1

scholarly journals Catalytically-active inclusion bodies for biotechnology—general concepts, optimization, and application

2020 ◽  
Vol 104 (17) ◽  
pp. 7313-7329
Author(s):  
Vera D. Jäger ◽  
Robin Lamm ◽  
Kira Küsters ◽  
Gizem Ölçücü ◽  
Marco Oldiges ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Active Inclusion Bodies ◽  
Catalytically Active

scholarly journals Function of the N-terminal propeptide of an aminopeptidase from Vibrio proteolyticus

2000 ◽  
Vol 350 (3) ◽  
pp. 671-676 ◽  
Author(s):  
Zhen-Zhong ZHANG ◽  
Satoru NIRASAWA ◽  
Yoshiaki NAKAJIMA ◽  
Michiteru YOSHIDA ◽  
Kiyoshi HAYASHI
Keyword(s):  
Escherichia Coli ◽  
Enzyme Activity ◽  
Active Region ◽  
Protein Expression ◽  
Inclusion Bodies ◽  
Active Enzyme ◽  
Vibrio Proteolyticus ◽  
Show Evidence ◽  
Inhibited Enzyme

An aminopeptidase from Vibrio proteolyticus was translated as a preproprotein consisting of four domains: a signal peptide, an N-terminal propeptide, a mature region and a C-terminal propeptide. Protein expression and analysis of the activity results demonstrated that the N-terminal propeptide was essential to the formation of the active enzyme in Escherichia coli. Urea dissolution of inclusion bodies and dialysis indicated that the N-terminal propeptide could facilitate the correct folding of the enzyme in vitro. Using l-Leu-p-nitroanilide as the substrate, the kinetic parameters (kcat and Km) of the pro-aminopeptidase and processed aminopeptidases were analysed. The results suggested that the N-terminal propeptide inhibited enzyme activity of the mature region. In contrast, the C-terminal propeptide did not show evidence of forming an active enzyme, of correctly folding in vitro or of inhibiting the active region.

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