Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement

2003 ◽  
Vol 61 (2) ◽  
pp. 163-178 ◽  
Author(s):  
L. Peng ◽  
K. Shimizu
Keyword(s):  
Escherichia Coli ◽  
Enzyme Activity ◽  
Protein Expression ◽  
Metabolic Regulation ◽  
Activity Measurement ◽  
Escherichia Coli K12 ◽  
Dimensional Electrophoresis

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.

Mutations that alter the pore function of the ompF porin of Escherichia coli K12

1988 ◽  
Vol 203 (4) ◽  
pp. 961-970 ◽  
Author(s):  
S.A. Benson ◽  
J.L.L. Occi ◽  
B.A. Sampson
Keyword(s):  
Escherichia Coli ◽  
Ompf Porin ◽  
Escherichia Coli K12
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