SRE0006
Thymidine Phosphorylase, recombinant from Escherichia coli
recombinant, expressed in E. coli, Suitable for manufacturing of diagnostic kits and reagents, buffered aqueous solution, ≥500 units/mL
Synonym(s):
Gliostatins, PD-ECGF, Thymidine:orthophosphate deoxy-D-ribosyltransferase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Product Name
Thymidine Phosphorylase, recombinant from Escherichia coli, recombinant, expressed in E. coli, Suitable for manufacturing of diagnostic kits and reagents, buffered aqueous solution, ≥500 units/mL
recombinant
expressed in E. coli
form
buffered aqueous solution
concentration
≥500 units/mL
technique(s)
inhibition assay: suitable
color
colorless to yellow
solubility
soluble
water: soluble
NCBI accession no.
UniProt accession no.
application(s)
diagnostic assay manufacturing
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Gene Information
Escherichia coli ... deoA(948901)
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Application
Thymidine phosphorylase has been used:
- in a study to evaluate biomarkers for advanced breast cancer patients treated with capecitabine-based first-line chemotherapy.
- in a study to investigate implications for the clinical efficacy of nucleoside analogues.
Biochem/physiol Actions
An enzyme that catalyzes the reversible conversion of thymidine to thymine. Thymidine phosphorylase is part of the pyrimidine nucleoside salvage pathway.
An enzyme that catalyzes the reversible conversion of thymidine to thymine. Thymidine phosphorylase is part of the pyrimidine nucleoside salvage pathway. This pathway allows pyrimidine bases to be recycled for nucleotide biosynthesis, while the pentose 1-phosphates are converted to intermediates of the pentose phosphate shunt and glycolysis. The E. coli thymidine phosphorylase shares 40% sequence homology with the human sequence, which has been found to be identical to the angiogenic agent platelet-derived endothelial growth factor. The purified E. coli enzyme has been shown to stimulate blood vessel growth in chick chorioallantoic membrane assays.
Thymidine phosphorylase catalyzes the reversible conversion of thymidine to thymine. Thymidine phosphorylase is part of the thymidine salvage pathway and pyrimidine nucleoside salvage pathway. This pathway allows pyrimidine bases to be recycled for nucleotide biosynthesis, while the pentose 1-phosphates are converted to intermediates of the pentose phosphate shunt and glycolysis. The enzyme inhibits apoptosis and induces angiogenesis thereby promoting tumor growth and metastatic process. Moreover, thymidine phosphorylase inhibits vascular smooth muscle cell proliferation.
General description
Research area: CELL SIGNALING
The E. coli thymidine phosphorylase shares 40% sequence homology with the human sequence, which is identical to the angiogenic agent platelet-derived endothelial growth factor. The purified E. coli enzyme has been shown to stimulate blood vessel growth in chick chorioallantoic membrane assays.
The E. coli thymidine phosphorylase shares 40% sequence homology with the human sequence, which is identical to the angiogenic agent platelet-derived endothelial growth factor. The purified E. coli enzyme has been shown to stimulate blood vessel growth in chick chorioallantoic membrane assays.
Other Notes
One unit will convert 1.0 μmole each of thymidine and phosphate to thymine and 2-deoxyribose 1-phosphate per min at pH 7.4 at 25°C.
Preparation Note
Cloned from E. coli and produced in overexpressing E. coli
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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The dual role of thymidine phosphorylase in cancer development and chemotherapy
Bronckaers A, et al.
Medicinal Research Reviews, 29(6), 903-953 (2009)
Thymidine kinase 1 and thymidine phosphorylase expression in non-small-cell lung carcinoma in relation to angiogenesis and proliferation
Brockenbrough J S, et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 57(11), 1087-1097 (2009)
Structures of native human thymidine phosphorylase and in complex with 5-iodouracil
Mitsiki E, et al.
Biochemical and Biophysical Research Communications, 386(4), 666-670 (2009)
Clinical and biochemical improvements in a patient with MNGIE following enzyme replacement.
Bridget E Bax et al.
Neurology, 81(14), 1269-1271 (2013-08-24)
Sheng-hua Zhang et al.
Cancer chemotherapy and pharmacology, 72(4), 777-788 (2013-08-27)
Capecitabine (CAP), a prodrug, needs to be converted to 5-fluorouracil by several key enzymes, including thymidine phosphorylase (TP). To improve the therapeutic index, potentiation of antitumor activity of CAP is required. In this study, we explored whether lidamycin (LDM), an
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