Sulfate Acts as Phosphate Analog on the Monomeric Catalytic Fragment of the CPx-ATPase CopB from Sulfolobus solfataricus

2007 ◽  
Vol 369 (2) ◽  
pp. 368-385 ◽  
Author(s):  
Mathias Lübben ◽  
Jörn Güldenhaupt ◽  
Martin Zoltner ◽  
Katrin Deigweiher ◽  
Peter Haebel ◽  
...  
2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity

2007 ◽  
Vol 367 (1) ◽  
pp. 224-233 ◽  
Author(s):  
Vengadesan Krishnan ◽  
Yuanyuan Xu ◽  
Kevin Macon ◽  
John E. Volanakis ◽  
Sthanam V.L. Narayana

2021 ◽  
Vol 11 (11) ◽  
pp. 4877
Author(s):  
Ravneet Mandair ◽  
Pinar Karagoz ◽  
Roslyn M. Bill

A triple mutant of NADP(H)-dependent malate dehydrogenase from thermotolerant Thermococcus kodakarensis has an altered cofactor preference for NAD+, as well as improved malate production compared to wildtype malate dehydrogenase. By combining mutant malate dehydrogenase with glucose dehydrogenase from Sulfolobus solfataricus and NAD+/NADH in a closed reaction environment, gluconate and malate could be produced from pyruvate and glucose. After 3 h, the yield of malate was 15.96 mM. These data demonstrate the feasibility of a closed system capable of cofactor regeneration in the production of platform chemicals.


1993 ◽  
Vol 268 (9) ◽  
pp. 6505-6510
Author(s):  
P.J. Kennelly ◽  
K.A. Oxenrider ◽  
J. Leng ◽  
J.S. Cantwell ◽  
N. Zhao

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