Substrate-and Antibiotic-Binding Sites at the Peptidyl-Transferase Centre of Escherichia coli Ribosomes. Studies on the Chloramphenicol, Lincomycin and Erythromycin Sites

1971 ◽  
Vol 23 (1) ◽  
pp. 185-193 ◽  
Author(s):  
Rafael Fernandez-Munoz ◽  
Robin E. Monro ◽  
David Vazquez ◽  
Ramon Torres-Pinedo
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Peptidyl Transferase ◽  
Peptidyl Transferase Centre

Affinity labelling the acceptor site of the peptidyl transferase centre of the Escherichia coli ribosome

Nature ◽  
1974 ◽  
Vol 250 (5466) ◽  
pp. 514-516 ◽  
Author(s):  
DAN EILAT ◽  
MARIA PELLEGRINI ◽  
HELEN OEN ◽  
NATHAN DE GROOT ◽  
YEHUDA LAPIDOT ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acceptor Site ◽  
Peptidyl Transferase ◽  
Affinity Labelling ◽  
Peptidyl Transferase Centre

scholarly journals Tuning a bi-enzymatic cascade reaction in Escherichia coli to facilitate NADPH regeneration for ε-caprolactone production

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Jinghui Xiong ◽  
Hefeng Chen ◽  
Ran Liu ◽  
Hao Yu ◽  
Min Zhuo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Regeneration System ◽  
Nadph Regeneration ◽  
Whole Cell ◽  
Cyclohexanone Monooxygenase ◽  
Ribosome Binding ◽  
Ribosome Binding Sites ◽  
Whole Cell Biocatalyst ◽  
Substrate Tolerance

Abstractε-Caprolactone is a monomer of poly(ε-caprolactone) which has been widely used in tissue engineering due to its biodegradability and biocompatibility. To meet the massive demand for this monomer, an efficient whole-cell biocatalytic approach was constructed to boost the ε-caprolactone production using cyclohexanol as substrate. Combining an alcohol dehydrogenase (ADH) with a cyclohexanone monooxygenase (CHMO) in Escherichia coli, a self-sufficient NADPH-cofactor regeneration system was obtained. Furthermore, some improved variants with the better substrate tolerance and higher catalytic ability to ε-caprolactone production were designed by regulating the ribosome binding sites. The best mutant strain exhibited an ε-caprolactone yield of 0.80 mol/mol using 60 mM cyclohexanol as substrate, while the starting strain only got a conversion of 0.38 mol/mol when 20 mM cyclohexanol was supplemented. The engineered whole-cell biocatalyst was used in four sequential batches to achieve a production of 126 mM ε-caprolactone with a high molar yield of 0.78 mol/mol.

Structure of a conserved RNA component of the peptidyl transferase centre

1997 ◽  
Vol 4 (10) ◽  
pp. 775-778 ◽  
Author(s):  
Elisabetta Viani Puglisi ◽  
Rachel Green ◽  
Harry F. Noller ◽  
Joseph D. Puglisi
Keyword(s):  
Peptidyl Transferase ◽  
Peptidyl Transferase Centre
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