EC Number   |
Natural Substrates |
|---|
    2.4.2.4 | more |
thymidine phosphorylase is identical with platelet-derived endothelial cell growth factor, PD-ECGF, which promotes angiogenesis. The mechanism of endometrial angiogenesis involves thymidine phosphorylase and stimulation by ovarian steroids of production of angiogenic regulators by endometrial epithelium and stroma which then act on the endothelium |
| 2.4.2.4 | thymidine + phosphate |
intact platelets degrade thymidine but are not able to synthesize thymidine from thymine |
| 2.4.2.4 | thymidine + phosphate |
the enzyme confers resistance to apoptosis induced by hypoxia. The enzymatic degradation of thymidine by thymidine phosphorylase is required for the inhibition of hypoxia-induced apoptosis. The enzyme can confer resistance to apoptosis in addition to its angiogenic activity. The enzyme must play some role in the development or malignancy of tumors. Involved in invasion and metastasis of some solid tumors |
| 2.4.2.4 | thymidine + phosphate |
the enzyme plays a crucial role in intratumoral angiogenesis, which occurs in the early phase of ovarian cancer, or influences angiogenesis indirectly |
| 2.4.2.4 | thymidine + phosphate |
- |
| 2.4.2.4 | thymine + 2-deoxy-alpha-D-ribose 1-phosphate |
- |
| 2.4.2.4 | thymine + 2-deoxy-D-ribose 1-phosphate |
- |
| 2.4.2.4 | thymine + 2-deoxy-D-ribose 1-phosphate |
enzyme is enantioselective, acts only on the naturally occurring D-thymidine and some D-thymidine analogs, but not on their L-counterparts |
| 2.4.2.4 | thymine + 2-deoxy-D-ribose 1-phosphate |
in Escherichia coli and Salmonella typhimurium thymidine phosphorylase plays an important role in metabolism of thymine auxotrophs and is necessary for the conversion of exogenous thymine to thymidine |
| 2.4.2.4 | thymine + 2-deoxy-D-ribose 1-phosphate |
enzyme also catalyzes the nucleoside deoxyribosyltransferase reaction with pyrimidine deoxyribonucleosides, ec2.4.2.6 |
