scholarly journals Escherichia coli RNase D. Catalytic properties and substrate specificity.

1981 ◽  
Vol 256 (11) ◽  
pp. 5633-5637 ◽  
Author(s):  
H. Cudny ◽  
R. Zaniewski ◽  
M.P. Deutscher
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
Catalytic Properties

scholarly journals 4,4′-Diapophytoene Desaturase: Catalytic Properties of an Enzyme from the C30 Carotenoid Pathway ofStaphylococcus aureus

1999 ◽  
Vol 181 (19) ◽  
pp. 6184-6187 ◽  
Author(s):  
Axel Raisig ◽  
Gerhard Sandmann
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Substrate Specificity ◽  
Affinity Chromatography ◽  
Catalytic Properties ◽  
Ofstaphylococcus Aureus ◽  
Double Bonds ◽  
One Step ◽  
Single Enzyme ◽  
Carotenoid Pathway

ABSTRACT Staphylococcus aureus synthesizes C30carotenoids. Their formation involves the introduction of three double bonds, which is catalyzed by a single enzyme. This enzyme, 4,4′-diapophytoene desaturase from S. aureus, was overexpressed in Escherichia coli and purified in one step by affinity chromatography, and then the protein was characterized with respect to substrate specificity, cofactor requirement, and oligomerization.

scholarly journals Structural and catalytic properties of a deletion derivative (delta 133-157) of Escherichia coli adenylate kinase

1991 ◽  
Vol 266 (17) ◽  
pp. 10781-10786
Author(s):  
T. Rose ◽  
M. Brune ◽  
A. Wittinghofer ◽  
K. Le Blay ◽  
W.K. Surewicz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Adenylate Kinase ◽  
Catalytic Properties ◽  
Deletion Derivative
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