Exploring the Active Site ofTrypanosoma bruceiPhosphofructokinase by Inhibition Studies:  Specific Irreversible Inhibition†

Biochemistry ◽  
2002 ◽  
Vol 41 (32) ◽  
pp. 10183-10193 ◽  
Author(s):  
Samantha Claustre ◽  
Colette Denier ◽  
Faouzi Lakhdar-Ghazal ◽  
Andrée Lougare ◽  
Claudia Lopez ◽  
...  
Keyword(s):  
Active Site ◽  
Irreversible Inhibition ◽  
Inhibition Studies

Active site directed irreversible inhibition of thermolysin

Biochemistry ◽  
1978 ◽  
Vol 17 (21) ◽  
pp. 4363-4369 ◽  
Author(s):  
David Rasnick ◽  
James C. Powers
Keyword(s):  
Active Site ◽  
Irreversible Inhibition

Access to the Active Site of Periplasmic Nitrate Reductase:  Insights from Site-Directed Mutagenesis and Zinc Inhibition Studies†

Biochemistry ◽  
2007 ◽  
Vol 46 (34) ◽  
pp. 9713-9721 ◽  
Author(s):  
Sébastien Dementin ◽  
Pascal Arnoux ◽  
Bettina Frangioni ◽  
Sandrine Grosse ◽  
Christophe Léger ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Periplasmic Nitrate Reductase ◽  
Zinc Inhibition ◽  
Inhibition Studies

scholarly journals Isolation and characterization of glyoxylate dehydrogenase from the fungus Sclerotium rolfsii

1984 ◽  
Vol 218 (1) ◽  
pp. 113-118 ◽  
Author(s):  
A J Balmforth ◽  
A Thomson
Keyword(s):  
Affinity Chromatography ◽  
Active Site ◽  
Sclerotium Rolfsii ◽  
Thiol Group ◽  
Isolation And Characterization ◽  
Crude Extracts ◽  
Nad Oxidoreductase ◽  
Inhibition Studies ◽  
Dye Affinity Chromatography

Glyoxylate dehydrogenase (glyoxylate: NAD+ oxidoreductase) was purified 600-fold in three steps from crude extracts of the fungus Sclerotium rolfsii (Corticium rolfsii Curzi). Two of the purification steps involved dye-affinity chromatography. The enzyme is a tetramer of Mr 250 000, with identical subunits of Mr 57 000. Inhibition studies suggest that there is one essential thiol group per active site.

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