ChemInform Abstract: THE MITOGENIC PRINCIPLE OF ESCHERICHIA COLI LIPOPROTEIN: SYNTHESIS, SPECTROSCOPIC CHARACTERIZATION, AND MITOGENICITY OF N-PALMITOYL-S-((2R,S)-2,3-DIPALMITOYLOXYPROPYL)-(R)-CYSTEINE METHYL ESTER

1983 ◽  
Vol 14 (50) ◽  
Author(s):  
G. JUNG ◽  
C. CARRERA ◽  
H. BRUECKNER ◽  
W. G. BESSLER
Keyword(s):  
Escherichia Coli ◽  
Methyl Ester ◽  
Spectroscopic Characterization ◽  
Lipoprotein Synthesis

scholarly journals Functional expression of the eukaryotic proton pump rhodopsin OmR2 in Escherichia coli and its photochemical characterization

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Masuzu Kikuchi ◽  
Keiichi Kojima ◽  
Shin Nakao ◽  
Susumu Yoshizawa ◽  
Shiho Kawanishi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Proton Pump ◽  
Expression System ◽  
Spectroscopic Characterization ◽  
Functional Expression ◽  
Proton Pumping ◽  
E Coli ◽  
Oxyrrhis Marina ◽  
Domains Of Life

AbstractMicrobial rhodopsins are photoswitchable seven-transmembrane proteins that are widely distributed in three domains of life, archaea, bacteria and eukarya. Rhodopsins allow the transport of protons outwardly across the membrane and are indispensable for light-energy conversion in microorganisms. Archaeal and bacterial proton pump rhodopsins have been characterized using an Escherichia coli expression system because that enables the rapid production of large amounts of recombinant proteins, whereas no success has been reported for eukaryotic rhodopsins. Here, we report a phylogenetically distinct eukaryotic rhodopsin from the dinoflagellate Oxyrrhis marina (O. marina rhodopsin-2, OmR2) that can be expressed in E. coli cells. E. coli cells harboring the OmR2 gene showed an outward proton-pumping activity, indicating its functional expression. Spectroscopic characterization of the purified OmR2 protein revealed several features as follows: (1) an absorption maximum at 533 nm with all-trans retinal chromophore, (2) the possession of the deprotonated counterion (pKa = 3.0) of the protonated Schiff base and (3) a rapid photocycle through several distinct photointermediates. Those features are similar to those of known eukaryotic proton pump rhodopsins. Our successful characterization of OmR2 expressed in E. coli cells could build a basis for understanding and utilizing eukaryotic rhodopsins.

7-β-d-galactopyranosyloxycoumarin-4-acetic acid and its methyl ester as substrates for the β-d-galactosidase of Escherichia coli

1990 ◽  
Vol 197 ◽  
pp. 295-301 ◽  
Author(s):  
Neil Baggett ◽  
Martin A. Case ◽  
Paul R. Darby ◽  
Charles J. Gray
Keyword(s):  
Escherichia Coli ◽  
Acetic Acid ◽  
Methyl Ester

Lipopeptides of the N-terminus of Escherichia coli lipoprotein: synthesis, mitogenicity and properties in monolayer experiments

1987 ◽  
Vol 900 (1) ◽  
pp. 116-128 ◽  
Author(s):  
Werner Prass ◽  
Helmut Ringsdorf ◽  
Wolfgang Bessler ◽  
Karl-Heinz Wiesmüller ◽  
Günther Jung
Keyword(s):  
Escherichia Coli ◽  
N Terminus ◽  
Lipoprotein Synthesis

scholarly journals The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase

1990 ◽  
Vol 265 (3) ◽  
pp. 725-729 ◽  
Author(s):  
M J Warren ◽  
C A Roessner ◽  
P J Santander ◽  
A I Scott
Keyword(s):  
Escherichia Coli ◽  
Methyl Ester ◽  
Absorption Spectra ◽  
Uroporphyrinogen Iii Methylase

The Escherichia coli cysG gene was successfully subcloned and over-expressed to produce a 52 kDa protein that was purified to homogeneity. This protein was shown to catalyse the S-adenosylmethionine-dependent methylation of uroporphyrinogen III to give a product identified as sirohydrochlorin on the basis of its absorption spectra, incorporation of 14C label from S-adenosyl[Me-14C]methionine and mass and 1H-n.m.r. spectra of its octamethyl ester. Further confirmation of the structure was obtained from a 14C-n.m.r. spectrum of the methyl ester produced by incubation of the methylase with uroporphyrinogen III, derived from [4.6-13C2]porphobilinogen, and S-adenosyl[Me-13C]methionine.

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