scholarly journals Light Induction of Phosphoenolpyruvate Carboxylase in Etiolated Maize Leaf Tissue

1981 ◽  
Vol 67 (1) ◽  
pp. 133-138 ◽  
Author(s):  
Shinobu Hayakawa ◽  
Kazumi Matsunaga ◽  
Tatsuo Sugiyama
1974 ◽  
Vol 53 (6) ◽  
pp. 829-834 ◽  
Author(s):  
S. K. Mukerji ◽  
S. F. Yang

1988 ◽  
Vol 253 (1) ◽  
pp. 217-222 ◽  
Author(s):  
D H Gonzalez ◽  
C S Andreo

The analogue (Z)-phosphoenol-3-fluoropyruvate [(Z)-3-fluoro-2-(phosphono-oxy)propenoic acid] was tested as substrate of maize leaf phosphoenolpyruvate carboxylase. Studies with NaH14CO3 indicate that the analogue is carboxylated by the enzyme. However, this reaction accounts for only one-tenth of the activity measured by Pi liberation. The rest of the analogue is merely dephosphorylated. This is the first analogue for which both carboxylation and dephosphorylation have been observed.


Biochemistry ◽  
1995 ◽  
Vol 34 (2) ◽  
pp. 472-480 ◽  
Author(s):  
Wayne A. Jensen ◽  
John McD. Armstrong ◽  
Joe DeGiorgio ◽  
Milton T. W. Hearn

1988 ◽  
Vol 18 (3) ◽  
pp. 317-325 ◽  
Author(s):  
K. Angelopoulos ◽  
K. Stamatakis ◽  
Y. Manetas ◽  
N. A. Gavalas

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