Abstract:
:Uridine phosphorylase is one of the critical enzymes in the pyrimidine salvage pathway. Cells regenerate uridine for nucleotide metabolism by incorporating uracil with ribose-1-phosphate with this enzyme. Recent studies indicate that Escherichia coli uridine phosphorylase is destabilized in the presence of ATP. However, the mechanism underlying the destabilization process and its influence on uridine phosphorylase function remain to be established. Here, we comprehensively investigated the effects of ATP on protein folding and function of Escherichia coli uridine phosphorylase. Our results demonstrate that ATP apparently decreases the stability of uridine phosphorylase in a concentration-dependent manner. Additionally, simply increasing the level of ATP led to a reduction of enzymatic activity to complete inhibition. Further studies showed that uridine phosphorylase accumulates as a partially unfolded state in the presence of ATP. Moreover, ATP specifically accelerated the unfolding rate of uridine phosphorylase with no observable effects on the refolding process. Our preliminary findings suggest that ATP can alter the protein folding and function of enzymes via apparent destabilization. This mechanism may be significant for proteins functioning under conditions of high levels of ATP, such as cancer cell environments.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Liu YK,Lin TH,Liu PFdoi
10.1016/j.abb.2017.09.007subject
Has Abstractpub_date
2017-11-15 00:00:00pages
11-20eissn
0003-9861issn
1096-0384pii
S0003-9861(17)30446-0journal_volume
634pub_type
杂志文章abstract::Iodotyrosine deiodinase (IYD) is unusual for its reliance on flavin to promote reductive dehalogenation under aerobic conditions. As implied by the name, this enzyme was first discovered to catalyze iodide elimination from iodotyrosine for recycling iodide during synthesis of tetra- and triiodothyronine collectively k...
journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章,评审
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pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1994-05-15 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:2009-07-15 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1998.1036
更新日期:1999-02-15 00:00:00
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pub_type: 杂志文章
doi:10.1006/abbi.1993.1184
更新日期:1993-04-01 00:00:00
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pub_type: 杂志文章
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更新日期:2014-09-15 00:00:00
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1995-03-10 00:00:00
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abstract::Horseradish peroxidase (EC 1.11.1.7) is shown to catalyze the aerobic oxidation of lysozyme, bovine serum albumin, and protamine adducts with glycolaldehyde at physiological pH. This reaction is accompanied by light emission, which is attributed to the generation of triplet species. The intensity of chemiluminescence ...
journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1986-07-01 00:00:00