An activity stain for dihydroxy-acid dehydratase

1987 ◽  
Vol 164 (2) ◽  
pp. 526-530 ◽  
Author(s):  
Che Fu Kuo ◽  
Tadahiko Mashino ◽  
Irwin Fridovich
1990 ◽  
pp. 617-621
Author(s):  
Dietmar Schomburg ◽  
Margit Salzmann

1993 ◽  
Vol 21 (4) ◽  
pp. 367-385 ◽  
Author(s):  
D.H. Flint ◽  
A. Nudelman

1996 ◽  
Vol 49 (3) ◽  
pp. 349 ◽  
Author(s):  
G Limberg ◽  
G Limberg ◽  
J Thiem ◽  
J Thiem

Modified aldopentonic and aldohexonic acids were synthesized in order to study the electronic requirements for a successful enzymatic conversion into their corresponding 2-keto 3-deoxy analogues by dihydroxy acid dehydratase (DHAD), an enzyme from the biosynthetic pathway of branched chain amino acids. Analytical tests with the novel artificial substrates (18)-(21) and (27) provided evidence that the amount of conversion could be enhanced by replacement of the hydroxy group at C4 of L-arabinonic acid (21) with less electron-withdrawing, ambivalent or electron-donating substituents. Modified aldohexonic acids were no substrates for DHAD, perhaps due to less perfect binding to the active site presumably for steric reasons. For 4-deoxy-L-threo-pentonic acid (18) the enzymatic conversion into 3,4-dideoxy-2-ketopentonic acid (29) by DHAD could be achieved on a preparative scale.


1966 ◽  
Vol 241 (9) ◽  
pp. 2042-2046 ◽  
Author(s):  
Kazuyoshi Kiritani ◽  
Sumiko Narise ◽  
R.P. Wagner

1993 ◽  
Vol 268 (20) ◽  
pp. 14732-14742
Author(s):  
D.H. Flint ◽  
M.H. Emptage ◽  
M.G. Finnegan ◽  
W. Fu ◽  
M.K. Johnson

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