N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 1. A substrate analog binds to two different binding sites on the bifunctional enzyme from Escherichia coli

Biochemistry ◽  
1979 ◽  
Vol 18 (26) ◽  
pp. 5946-5953 ◽  
Author(s):  
Hans Bisswanger ◽  
Kasper Kirschner ◽  
Willy Cohn ◽  
Vreni Hager ◽  
Elisabeth Hansson
2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Jinghui Xiong ◽  
Hefeng Chen ◽  
Ran Liu ◽  
Hao Yu ◽  
Min Zhuo ◽  
...  

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 ◽  
1999 ◽  
Vol 7 (7) ◽  
pp. 865-875 ◽  
Author(s):  
Igor A Shumilin ◽  
Robert H Kretsinger ◽  
Ronald H Bauerle

2013 ◽  
Vol 8 (5) ◽  
pp. 958-966 ◽  
Author(s):  
Pamela A. Barendt ◽  
Najaf A. Shah ◽  
Gregory A. Barendt ◽  
Parth A. Kothari ◽  
Casim A. Sarkar

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