IN VITRO BIOSYNTHESIS OF AN AI-2 LIKE BACTERIAL AUTOINDUCER BY RECOMBINANT ESCHERICHIA COLI ENZYMES

Author(s):  
Michael Ramm ◽  
Silke Steinbach ◽  
Volker Schroeckh
Biochemistry ◽  
1977 ◽  
Vol 16 (16) ◽  
pp. 3608-3618 ◽  
Author(s):  
Maurille J. Fournier ◽  
Elizabeth Webb ◽  
Shirley Tang

2015 ◽  
Vol 46 (1) ◽  
Author(s):  
Katharina Kerner ◽  
Philip S Bridger ◽  
Gabriele Köpf ◽  
Julia Fröhlich ◽  
Stefanie Barth ◽  
...  

2005 ◽  
Vol 69 (3) ◽  
pp. 286-292 ◽  
Author(s):  
Qun Ren ◽  
Guy de Roo ◽  
Jan B. van Beilen ◽  
Manfred Zinn ◽  
Birgit Kessler ◽  
...  

2007 ◽  
Vol 79 (12) ◽  
pp. 2179-2188 ◽  
Author(s):  
A. Ian Scott ◽  
Charles A. Roessner

The genetic engineering of Escherichia coli for the over-expression of enzymes of the aerobic and anaerobic pathways to cobalamin has resulted in the in vivo and in vitro biosynthesis of new intermediates and other products that were isolated and characterized using a combination of bioorganic chemistry and high-resolution NMR. Analyses of these products were used to deduct the functions of the enzymes that catalyze their synthesis. CobZ, another enzyme for the synthesis of precorrin-3B of the aerobic pathway, has recently been described, as has been BluB, the enzyme responsible for the oxygen-dependent biosynthesis of dimethylbenzimidazole. In the anaerobic pathway, functions have recently been experimentally confirmed for or assigned to the CbiMNOQ cobalt transport complex, CbiA (a,c side chain amidation), CbiD (C-1 methylation), CbiF (C-11 methylation), CbiG (lactone opening, deacylation), CbiP (b,d,e,g side chain amidation), and CbiT (C-15 methylation, C-12 side chain decarboxylation). The dephosphorylation of adenosylcobalamin-phosphate, catalyzed by CobC, has been proposed as the final step in the biosynthesis of adenosylcobalamin.


1987 ◽  
Vol 262 (18) ◽  
pp. 8834-8839
Author(s):  
C A Lingwood ◽  
H Law ◽  
S Richardson ◽  
M Petric ◽  
J L Brunton ◽  
...  

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