scholarly journals Glutamine Induces the N-Dependent Accumulation of mRNAs Encoding Phosphoenolpyruvate Carboxylase and Carbonic Anhydrase in Detached Maize Leaf Tissue

1992 ◽  
Vol 100 (4) ◽  
pp. 2066-2070 ◽  
Author(s):  
Bambang Sugiharto ◽  
Iwane Suzuki ◽  
James N. Burnell ◽  
Tatsuo Sugiyama
Keyword(s):  
Carbonic Anhydrase ◽  
Phosphoenolpyruvate Carboxylase ◽  
Leaf Tissue ◽  
Maize Leaf

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
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Leaf Tissue ◽  
Light Induction ◽  
Maize Leaf

scholarly journals Phosphoenolpyruvate Carboxylase from Spinach Leaf Tissue

1974 ◽  
Vol 53 (6) ◽  
pp. 829-834 ◽  
Author(s):  
S. K. Mukerji ◽  
S. F. Yang
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Leaf Tissue ◽  
Spinach Leaf

scholarly journals Carboxylation and dephosphorylation of phosphoenol-3-fluoropyruvate by maize leaf phosphoenolpyruvate carboxylase

1988 ◽  
Vol 253 (1) ◽  
pp. 217-222 ◽  
Author(s):  
D H Gonzalez ◽  
C S Andreo
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Maize Leaf ◽  
Propenoic Acid

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.

Stability Studies on Maize Leaf Phosphoenolpyruvate Carboxylase: The Effect of Salts

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

Carbon dioxide, the substrate for phosphoenolpyruvate carboxylase from leaves of maize

1969 ◽  
Vol 47 (9) ◽  
pp. 1455-1458 ◽  
Author(s):  
E. R. Waygood ◽  
Regis Mache ◽  
C. K. Tan
Keyword(s):  
Carbon Dioxide ◽  
Zea Mays ◽  
Carbonic Anhydrase ◽  
Phosphoenolpyruvate Carboxylase ◽  
Spinacea Oleracea ◽  
Natural Photosynthesis

Using a spectrophotometric technique it has been shown that CO2 is the substrate for phosphoenolpyruvate carboxylase (EC 4.1.1.31) from leaves of Zea mays. The Km (CO2) is approximately 7.5 × 10−6 M, which is the order of the half saturation value for CO2 in natural photosynthesis. Studies indicate also that carbonic anhydrase is localized in chloroplasts, isolated by the 'laceration technique' from leaves of Spinacea oleracea, but is absent from leaves of Zea mays. It is speculated that carbonic anhydrase catalyses a 'trap' for the CO2 escaping into the environment via photorespiration.

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