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SRE0006

Sigma-Aldrich

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

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Synonym(s):
Gliostatins, PD-ECGF, Thymidine:orthophosphate deoxy-D-ribosyltransferase
CAS Number:
9030-23-3
Enzyme Commission number:
2.4.2.4 (BRENDA, IUBMB)
MDL number:
MFCD00132426
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

400

form

buffered aqueous solution

concentration

≥500 units/mL

technique(s)

inhibition assay: suitable

color

colorless to yellow

solubility

soluble
water: soluble

NCBI accession no.

NP_418799.1

UniProt accession no.

P07650

application(s)

diagnostic assay manufacturing

shipped in

wet ice

storage temp.

2-8°C

Gene Information

Escherichia coli ... deoA(948901)

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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.

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. 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.

Unit Definition

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 Code

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)
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
Akihiko Hatano et al.
Organic & biomolecular chemistry, 11(40), 6900-6905 (2013-09-24)
Herein, we describe β-selective coupling between a modified uracil and a deoxyribose to produce functionalized nucleosides catalyzed by thymidine phosphorylase derived from Escherichia coli. This enzyme mediates nucleobase-exchange reactions to convert unnatural nucleosides possessing a large functional group such as
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