A study on the inactivation of maize leaves nadp-malic enzyme by 3-bromopyruvate

[1]  A. Iglesias,et al.  Interaction of divalent metal ions with the NADP+-malic enzyme from maize leaves , 1991 .

[2]  A. Bhagwat,et al.  Chemical modification of the functional arginine residue(s) of malic enzyme from Zea mays , 1991 .

[3]  A. Iglesias,et al.  NADP-dependent malate dehydrogenase (decarboxylating) from sugar cane leaves. Kinetic properties of different oligomeric structures. , 1990, European journal of biochemistry.

[4]  A. Iglesias,et al.  Calcium ion interaction with NADP-malic enzyme from maize leaves , 1990 .

[5]  T. Nelson,et al.  Primary structure of the maize NADP-dependent malic enzyme. , 1989, The Journal of biological chemistry.

[6]  A. Iglesias,et al.  Purification of NADP-Malic Enzyme and Phosphoenolpyruvate Carboxylase from Sugar Cane Leaves , 1989 .

[7]  R. Wedding,et al.  pH Effects on the Activity and Regulation of the NAD Malic Enzyme. , 1987, Plant physiology.

[8]  N. Jawali,et al.  Presence of essential histidine residues in nadp-malic enzyme from maize , 1987 .

[9]  A. Iglesias,et al.  Active-site-directed inhibition of phosphoenolpyruvate carboxylase from maize leaves by bromopyruvate. , 1986, Archives of biochemistry and biophysics.

[10]  R. Perham,et al.  Bromopyruvate as an active-site-directed inhibitor of the pyruvate dehydrogenase multienzyme complex from Escherichia coli. , 1984, Biochemistry.

[11]  N. Carrillo,et al.  An essential carboxyl group at the nucleotide binding site of ferredoxin-NADP+ oxidoreductase. , 1981, The Journal of biological chemistry.

[12]  K. Izui,et al.  Phosphoenolpyruvate carboxylase of Escherichia coli. Affinity labeling with bromopyruvate. , 1979, Journal of biochemistry.

[13]  H. Penefsky.  Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase. , 1977, The Journal of biological chemistry.

[14]  M. D. Hatch,et al.  Association of NADP- and NAD-linked malic enzyme acitivities in Zea mays: relation to C4 pathway photosynthesis. , 1977, Archives of biochemistry and biophysics.

[15]  W. Cleland,et al.  Inhibition and alternate-substrate studies on the mechanism of malic enzyme. , 1977, Biochemistry.

[16]  G. Chang,et al.  Mechanism of pigeon liver malic enzyme: kinetics, specificity, and half-site stoichiometry of the alkylation of a cysteinyl residue by the substrate-inhibitor bromopyruvate. , 1977, Biochemistry.

[17]  M. Fonda.  Bromopyruvate inactivation of glutamate apodecarboxylase. Kinetics and specificity. , 1976, The Journal of biological chemistry.

[18]  R. Y. Hsu,et al.  Mechanism of pigeon liver malic enzyme. Modification of sulfhydryl groups by 5,5'-dithiobis(2-nitrobenzoic acid) and N-ethylmaleimide. , 1974, The Journal of biological chemistry.

[19]  Y. Morino,et al.  Affinity labeling of aspartate aminotransferase isozymes by bromopyruvate. , 1973, Journal of Biological Chemistry.

[20]  Meloche Hp.  Reaction of the substrate analog bromopyruvate with two active-site conformers of 2-keto-3-deoxy-6 phosphogluconic aldolase. , 1970 .

[21]  M. Utter,et al.  Pyruvate carboxylase. V. Interaction of the enzyme with adenosine triphosphate. , 1965, The Journal of biological chemistry.

[22]  H. Lindley.  The reaction of thiol compounds and chloroacetamide. 2. The reaction between chloroacetamide and cysteine peptides. , 1962, The Biochemical journal.

[23]  G. Ellman,et al.  Tissue sulfhydryl groups. , 1959, Archives of biochemistry and biophysics.

[24]  O. H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.