Topology of Binding Sites for Carbamyl Phosphate in Aspartate Transcarbamylase from Escherichia coli. The Use of Pyridoxal Phosphate as Covalent Probe

1975 ◽  
Vol 54 (1) ◽  
pp. 293-299 ◽  
Author(s):  
Peter SUTER ◽  
Jurg P. ROSENBUSCH
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Pyridoxal Phosphate ◽  
Aspartate Transcarbamylase ◽  
Carbamyl Phosphate

The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate

Biochemistry ◽  
1990 ◽  
Vol 29 (36) ◽  
pp. 8491-8498 ◽  
Author(s):  
Xu Guang Xi ◽  
Francoise Van Vliet ◽  
Moncef M. Ladjimi ◽  
Raymond Cunin ◽  
Guy Herve
Keyword(s):  
Escherichia Coli ◽  
Carbonyl Group ◽  
Catalytic Site ◽  
Aspartate Transcarbamylase ◽  
Carbamyl Phosphate

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.

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