Evidence for two distinct conformations of the Escherichia coli mannitol permease that are important for its transport and phosphorylation functions
Evidence for two distinct conformations of the Escherichia coli mannitol permease that are important for its transport and phosphorylation functions
复制标题
大肠杆菌甘露醇渗透酶的两种不同构象对其转运和磷酸化功能很重要的证据
DOI:
--
复制
发表时间:
1989
影响因子:
4
通讯作者:
G. Jacobson
中科院分区:
文献类型:
--
作者:
S. Khandekar;G. Jacobson
Column chromatography of the Escherichia coli mannitol permease (mannitolspecific enzyme II of the phosphotransferase system) in the presence of deoxycholate has revealed that the active permease can exist in at least two association states with apparent molecular weights consistent with a monomer and a dimer. The monomeric conformation is favored by the presence of mannitol and by the phosphoenolpyruvate (PEP)‐dependent phosphorylation of the protein. The dimer is stabilized by inorganic phosphate (Pi), which also stimulates phospho‐exchange between mannitol and mannitol 1‐phosphate (a partial reaction in the overall PEP‐dependent phosphorylation of mannitol). Kinetic analysis of the phospho‐exchange reaction revealed that Pi stimulates phospho‐exchange by increasing the Vmax of the reaction. A kinetic model for mannitol permease function is presented involving both conformations of the permease. The monomer (or a less‐stable conformation of the dimer) is hypothesized to be involved in the initial mannitol‐binding and PEP‐dependent phosphorylation steps, while the stably associated dimer is suggested to participate in later steps involving direct phosphotransfer between the permease, mannitol and mannitol 1‐phosphate.
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DOI:
--
发表时间:
1983
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Jacobson,GR;Lee,CA;Leonard,JE;SaierJr,MH
通讯作者:
SaierJr,MH
影响因子:
2.9
作者:
Stephan,MM;Jacobson,GR
通讯作者:
Jacobson,GR
影响因子:
2.9
作者:
Stephan,MM;Jacobson,GR
通讯作者:
Jacobson,GR
DOI:
10.1002/jss.400140303
发表时间:
1980
期刊:
Journal of supramolecular structure
影响因子:
--
作者:
SaierJr,MH
通讯作者:
SaierJr,MH