TY - JOUR
T1 - Monoselenophosphate
T2 - Its hydrolysis and its ability to phosphorylate alcohols and amines
AU - Kamiński, Rafal
AU - Glass, Richard S.
AU - Schroeder, T. Benjamin
AU - Michalski, Jan
AU - Skowrońska, Aleksandra
N1 - Funding Information:
This material is based upon work supported by the National Science Foundation under Grant INT-9311868.
PY - 1997/8
Y1 - 1997/8
N2 - The rate of hydrolysis of monoselenophosphate, the labile selenium donor compound required for the synthesis of selenium-dependent enzymes and seleno-tRNAs, was determined by 31P NMR spectroscopy. The rate depended on the pH of the solution and was maximal at a pH ~7. This suggests that the dianion is the species that reacts fastest. Added alcohols and amines do not significantly affect the rate of hydrolysis but are phosphorylated. The entropy of activation is positive for the hydrolysis of monoselenophosphate. These data suggest a dissociative in nature mechanism for the hydrolysis of monoselenophosphate involving a monomeric metaphosphate-like transition state in the rate-determining step.
AB - The rate of hydrolysis of monoselenophosphate, the labile selenium donor compound required for the synthesis of selenium-dependent enzymes and seleno-tRNAs, was determined by 31P NMR spectroscopy. The rate depended on the pH of the solution and was maximal at a pH ~7. This suggests that the dianion is the species that reacts fastest. Added alcohols and amines do not significantly affect the rate of hydrolysis but are phosphorylated. The entropy of activation is positive for the hydrolysis of monoselenophosphate. These data suggest a dissociative in nature mechanism for the hydrolysis of monoselenophosphate involving a monomeric metaphosphate-like transition state in the rate-determining step.
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U2 - 10.1006/bioo.1997.1070
DO - 10.1006/bioo.1997.1070
M3 - Article
AN - SCOPUS:0031204361
VL - 25
SP - 247
EP - 259
JO - Bioorganic Chemistry
JF - Bioorganic Chemistry
SN - 0045-2068
IS - 4
ER -