1997
DOI: 10.1006/bioo.1997.1070
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Monoselenophosphate: Its Hydrolysis and Its Ability to Phosphorylate Alcohols and Amines

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Cited by 10 publications
(5 citation statements)
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“…At present we cannot offer any experimentally verified explanation for that observation, although one may consider inhibition of the geranylation by the selenophosphate component, which may interact with certain contact points inside the SelU active site debilitating in that way proper accommodation of ppGe. The other explanation, which may be more trivial, is connected with low stability of selenium phosphate in the reaction conditions (its decomposition before the geranyl‐derivative is formed) .…”
Section: Resultsmentioning
confidence: 99%
“…At present we cannot offer any experimentally verified explanation for that observation, although one may consider inhibition of the geranylation by the selenophosphate component, which may interact with certain contact points inside the SelU active site debilitating in that way proper accommodation of ppGe. The other explanation, which may be more trivial, is connected with low stability of selenium phosphate in the reaction conditions (its decomposition before the geranyl‐derivative is formed) .…”
Section: Resultsmentioning
confidence: 99%
“…20 It is interesting to note that SecS and the Nifslike protein both belong to the fold type I, PLPdependent enzyme superfamily. Considering the toxicity and lability of SeP, 21,22 we suggest that direct inter-enzyme product/substrate handover of SeP from hSPS1 to SecS might exist. The direct handover of selenium-containing molecules including selenide and SeP in the Nifs-like protein-SPS-SecS network might allow the cell to conquer the toxicity of selenium.…”
Section: Possible Protein-protein Interaction Networkmentioning
confidence: 93%
“…SeP, the active form of selenium, is toxic, labile and highly reactive. 21,22 Thus, it is unlikely that SeP will diffuse freely to SeP utilizing enzymes such as selenocysteine synthase (SecS) in vivo. Our enzymatic assays have confirmed that phosphate is able to accelerate ADP hydrolysis, which might support this hypothesis.…”
Section: Reactionmentioning
confidence: 99%
“…Further chemical reactions of monoseleno-phosphate were studied as well. 9 Chemically prepared monoselenophosphate and the enzymatically synthesized selenium donor compound were shown to be identical by 31 P NMR spectroscopy, chromatographic behavior and biological activity. Monoselenophosphate was also shown to be the source of the selenium in the metalloid modified base (2-seleno-5-methylaminouracil) that occurs in some tRNAs found in anaerobic bacteria.…”
Section: Ooo-trimethylselenophosphate 2 With Trimethylsilyl Iodide mentioning
confidence: 98%