ISSN:
1573-5079
Keywords:
Cysteine modification
;
Maize leaf
;
Phosphoenolpyruvate carboxylase
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract Purified maize leaf phosphoenolpyruvate carboxylase (EC 4.1.1.31) was completely inactivated by several thiol-modifying reagents, including, CuCl2, CdCl2 and N-ethylmaleimide. The inactivation by CuCl2 could be reversed by dithiothreitol, suggesting the involvement of vicinal dithiols in the inactivation process. Complete inactivation of phosphoenolpyruvate carboxylase was correlated with the incorporation of two mol (3H)N-ethylmaleimide per 100-kilodalton subunit. The total protection of the enzyme against N-ethylmaleimide inactivation afforded by the substrate, phosphoenolpyruvate, was correlated with the protection of one mol (3H)N-ethylmaleimide reactive residue per mol subunit. The complete inactivation of phosphoenolpyruvate carboxylase by N-ethylmaleimide and the protection afforded by phosphoenolpyruvate against modification suggest the presence of an essential cysteine residue in the catalytic site of the C4 leaf enzyme.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00030021
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