scholarly journals Purification and characterization of SepII a new restriction endonuclease from Staphylococcus epidermidis

2012 ◽  
Vol 167 (2) ◽  
pp. 90-94 ◽  
Author(s):  
Abdelkarim Belkebir ◽  
Houssine Azeddoug
Gene ◽  
1995 ◽  
Vol 157 (1-2) ◽  
pp. 317-318
Author(s):  
Sylwia M. Rutkowska ◽  
Piotr M. Skowron ◽  
Anna J. Podhajska

1988 ◽  
Vol 251 (2) ◽  
pp. 461-466 ◽  
Author(s):  
I Vidal ◽  
J González ◽  
A Bernardo ◽  
R Martín

A method was developed to purify diacetyl-reducing enzymes from Staphylococcus aureus. Two enzymes capable of catalysing diacetyl reduction were isolated, neither of which turned out to be a specific diacetyl reductase. One of them is a lactate dehydrogenase similar to the one from Staphylococcus epidermidis, which accepts diacetyl, although poorly. The other one uses as coenzyme beta-NAD and reduces uncharged alpha-dicarbonyls with more than three carbon atoms (especially the alpha-diketones diacetyl and pentane-2,3-dione), producing the L(+) form of the corresponding alpha-hydroxycarbonyls. This enzyme has an Mr of 68,000 and is, most probably, a monomer. Its optimum pH is 6.0. Its shows a high affinity for NADH and a rather low one for diacetyl, which, at least in vitro, does not seem to be as good a substrate as pentane-2,3-dione. We propose for it the systematic name L-alpha-hydroxyketone: NAD+ oxidoreductase and the recommended name of alpha-diketone reductase (NAD). We also suggest that the diacetyl reductase entry in the I.U.B. classification be suppressed.


Gene ◽  
1988 ◽  
Vol 68 (1) ◽  
pp. 43-52 ◽  
Author(s):  
Patricia J. Greene ◽  
Barry T. Ballard ◽  
Frank Stephenson ◽  
William J. Kohr ◽  
Henry Rodriguez ◽  
...  

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