Reversible disaggregation of Escherichia coli succinyl-CoA synthetase. / Grinnell, Frederick Lawrence; David Stollar, B.; Nishimura, Jonathan S.In: BBA - Enzymology, Vol. 185, No. 2, 19.08.1969, p. 471-474.
Research output: Contribution to journal › Article › peer-review
TY - JOUR
T1 - Reversible disaggregation of Escherichia coli succinyl-CoA synthetase
AU - Grinnell, Frederick Lawrence
AU - David Stollar, B.
AU - Nishimura, Jonathan S.
N1 - Funding Information: Merthiolate, when incubated with the enzyme, resulted in losses of enzymatic actlvlty (Fig 3) The reaction of Merthiolate with the ealzyme reaches equlhbrlum after IO rain Thus, it would appear that Merthiolate dissociates the enzyme Into subunlts, and that the subumts are not active i mole of thlosahcylate (RSH) is formed when I mole of Merthiolate (R-S-Hg Et) reacts with a protein sulihydryl group The reaction follows the course shown in Eqn I R-S-Hg-Et + enzyme-SH-+ IRSH -4-(subumt(s)) S Hg-Et (i) Reversal of this reaction by sulfhydryl groups would be predicted To test this possl-blhty, excess dlthlothreltol was added after prelncubatlon of the enzyme with Merthiolate The data In Table I and Fig 4 indicate that the reaction of succlnyl-CoA synthetase with Merthiolate was reversible The subunlts reassoclated to an active form (Table I) that was serologlcally similar to the native enzyme (Fig 4) The fact that full activity was not restored may simply indicate that the rate of reaggregatlon was very slow under the conditions employed The effect of Merthiolate on succlnyl-CoA synthetase may be similar to that of p-mercurlbenzoate It has been observed that p-mercurlbenzoate dissociates the phosphorylated form of the enzyme into phosphorylated and nonphosphorylated subumts 5, although details describing this finding are not yet at hand It is important now to estabhsh whether the Merthiolate subunlt of tool wt 7 ° ooo is unique or IS a dlmer of subunlts of tool wt 35 ooo, and it will be of Interest to determine which of these subunlts is (are) phosphorylated The authors wish to thank Dr Louis Shuster for helpful discussions while this work was in progress The support of the National Institutes of Health (Grant GM AM-I3742 ) and the National Science Foundation (Grant GB-8o64) is acknowledged
PY - 1969/8/19
Y1 - 1969/8/19
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U2 - 10.1016/0005-2744(69)90443-4
DO - 10.1016/0005-2744(69)90443-4
M3 - Article
C2 - 4980136
AN - SCOPUS:0014452125
VL - 185
SP - 471
EP - 474
JO - BBA - Enzymology
JF - BBA - Enzymology
SN - 0005-2744
IS - 2