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从磷酸化丙酮酸、磷酸二激酶中分离3-磷酸组氨酸。

Isolation of 3-phosphohistidine from phosphorylated pyruvate, phosphate dikinase.

作者信息

Spronk A M, Yoshida H, Wood H G

出版信息

Proc Natl Acad Sci U S A. 1976 Dec;73(12):4415-9. doi: 10.1073/pnas.73.12.4415.

DOI:10.1073/pnas.73.12.4415
PMID:12506
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC431479/
Abstract

Pyruvate, phosphate dikinase (EC 2-7-9-1) catalyzes formation of phosphoenolpyruvate, AMP, and inorganic pyrophosphate from pyruvate, ATP, and orthophosphate. A pyrophosphoryl and phosphoryl form of the enzyme is involved in this transfer. The [32P]phosphoryl form of pyruvate, phosphate dikinase was prepared with enzyme isolated from Bacteroides symbiosus. The [32P]phosphoryl enzyme was found to have properties corresponding to a phosphoramidate linkage and this was confirmed by isolation of 3-[32P]phosphohistidine from alkaline hydrolysates of the enzyme. The histidyl residue is considered to be the pyrophosphoryl- and phosphoryl-carrier between the three substrate sites of this enzyme.

摘要

丙酮酸磷酸双激酶(EC 2-7-9-1)催化由丙酮酸、ATP和正磷酸盐形成磷酸烯醇丙酮酸、AMP和无机焦磷酸盐。该酶的焦磷酸化和磷酸化形式参与了这种转移。用从共生拟杆菌中分离的酶制备了丙酮酸磷酸双激酶的[32P]磷酸化形式。发现[32P]磷酸化酶具有与氨基磷酸酯键相对应的性质,并且通过从该酶的碱性水解产物中分离出3-[32P]磷酸组氨酸得到了证实。组氨酸残基被认为是该酶三个底物位点之间的焦磷酸化和磷酸化载体。

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本文引用的文献

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