The transfer of sulfate among phenolic compounds with 3',5'-diphosphoadenosine as coenzyme.
The transfer of sulfate among phenolic compounds with 3',5'-diphosphoadenosine as coenzyme.
复制标题
以3,5-二磷酸腺苷为辅酶的硫酸盐在酚类化合物之间的转移。
DOI:
10.1016/s0021-9258(19)63710-5
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发表时间:
1957
期刊:
影响因子:
--
通讯作者:
F. Lipmann
中科院分区:
文献类型:
--
作者:
J. D. Gregory;F. Lipmann
Nitrophenyl esters have been used extensively for the determination of hydrolases, the phosphate having been introduced by Huggins and Smith (1) for phosphatase assay. The sulfate has been used lately in particular by Roy (2) for arylsulfatase determination. Sulfate activation and transfer, however, have been studied with various phenols as sulfate acceptors (3-5). When work on sulfate activation was started in this laboratory, it seemed of advantage to use p-nitrophenol, which behaves as a transfer indicator because of the disappearance of the colored anion on esterification. In the course of these experiments, a number of observations were made which indicated a reversible reaction between active sulfate (PAPS) l (6) and nitrophenol. The present paper deals in detail with various aspects of this reversibility. The enzyme, phenol sulfokinase, which catalyzes this reaction, appears to have a rather broad activity covering a large variety of phenolic compounds. It is, however, specific with regard to PAPS. If reasonably high concentrations of p-nitrophenyl sulfate are used, the reverse reaction can be observed in which sulfate is returned to the residue PAP. This system may be used for assay of PAP and is particularly effective if supplied with an additional sulfate acceptor, the sulfate potential of which is far below that of p-NPS, and the enzyme then catalyzes a transfer of sulfate from p-NPS to phenol, which is dependent on the presence of PAP as sulfate carrier. sulfokinase p-NPS+ phenol _____f PAP p-NP+ phenyl sulfate