TY - JOUR
T1 - The effects of various n-substituted maleimides on succinic thiokinase of Escherichia coli
AU - Matula, J. Michael
AU - Nishimura, Jonathan S.
N1 - Funding Information:
Acknowledgem&ts-The authors with to thank Theresa Mitchell for assistance in the preparation of the enzyme. This work was supported in part by the United States Public Health Service, grant GM-17534, from the Institute of General Medical Sciences, and by the Robert A. Welch Foundation, grant AQ-458.
PY - 1978
Y1 - 1978
N2 - 1. 1. Even-chained N-alkyl maleimides, up to 10 carbon atoms in chain length, were tested for their ability to inactivate Escherichia coli succinic thiokinase. 2. 2. The pseudo-second-order inactivation constant, k2, was proportional to the chain length of the maleimides. 3. 3. However, the specificity with respect to sulfhydryl groups of the protein attacked appeared to be the same. 4. 4. The presence of ATP or CoA protected the enzyme partially against inactivation by both N-ethylmaleimide and N-hexylmaleimide.
AB - 1. 1. Even-chained N-alkyl maleimides, up to 10 carbon atoms in chain length, were tested for their ability to inactivate Escherichia coli succinic thiokinase. 2. 2. The pseudo-second-order inactivation constant, k2, was proportional to the chain length of the maleimides. 3. 3. However, the specificity with respect to sulfhydryl groups of the protein attacked appeared to be the same. 4. 4. The presence of ATP or CoA protected the enzyme partially against inactivation by both N-ethylmaleimide and N-hexylmaleimide.
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U2 - 10.1016/0020-711X(78)90151-9
DO - 10.1016/0020-711X(78)90151-9
M3 - Article
C2 - 348519
AN - SCOPUS:0017839491
VL - 9
SP - 213
EP - 215
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
SN - 1357-2725
IS - 3
ER -