CHARACTERIZATION OF THE ACTIVE SITE MUTANTS (C44S, C49S) OF ESCHERICHIA COLI LIPOAMIDE DEHYDROGENASE

1991 ◽  
pp. 581-584
Author(s):  
Nancy Hopkins ◽  
Charles H. Williams ◽  
George C. Russell ◽  
John R. Guest
2002 ◽  
Vol 269 (3) ◽  
pp. 893-901 ◽  
Author(s):  
Evert Bokma ◽  
Henriëtte J. Rozeboom ◽  
Mark Sibbald ◽  
Bauke W. Dijkstra ◽  
Jaap J. Beintema

1991 ◽  
pp. 525-528
Author(s):  
M. P. Deonarain ◽  
N. S. Scrutton ◽  
A. Berry ◽  
R. N. Perham

2006 ◽  
Vol 34 (1) ◽  
pp. 143-145 ◽  
Author(s):  
T.A. Clarke ◽  
A.M. Hemmings ◽  
B. Burlat ◽  
J.N. Butt ◽  
J.A. Cole ◽  
...  

The recent crystallographic characterization of NrfAs from Sulfurospirillum deleyianum, Wolinella succinogenes, Escherichia coli and Desulfovibrio desulfuricans allows structurally conserved regions to be identified. Comparison of nitrite and sulphite reductase activities from different bacteria shows that the relative activities vary according to organism. By comparison of both amino acid sequences and structures, differences can be identified in the monomer–monomer interface and the active-site channel; these differences could be responsible for the observed variance in substrate activity and indicate that subtle changes in the NrfA structure may optimize the enzyme for different roles.


2000 ◽  
Vol 267 (24) ◽  
pp. 7065-7074 ◽  
Author(s):  
Jacqueline Nairn ◽  
Doris Duncan ◽  
Naomi E. Price ◽  
Sharon M. Kelly ◽  
Linda A. Fothergill-Gilmore ◽  
...  

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