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Merck

N3665

Sigma-Aldrich

Pyrimidine Nucleoside Phosphorylase from Bacillus subtilis

recombinant, expressed in E. coli, ≥70 units/mg protein

别名:

PynP

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About This Item

分類程式碼代碼:
12352204
NACRES:
NA.54

重組細胞

expressed in E. coli

品質等級

形狀

lyophilized powder

比活性

≥70 units/mg protein

儲存溫度

−20°C

一般說明

The roles of the residues in the catalytic active site of pyrimidine nucleoside phosphorylase from Bacillis subtilis have been elucidated using hybrid quantum-mechanical/molecular-mechanical methods.

生化/生理作用

Pyrimidine nucleoside phosphorylase functions in the nucleotide synthesis salvage pathway by catalyzing the reversible phosphorolysis of pyrimidines. Both uridine and thymidine are substrates.

單位定義

One unit will convert 1 μmole each of 2′-deoxyuridine and phosphate to uracil and 2-deoxyribose 1-phosphate per minute at pH 7.4 and 37 °C.

象形圖

Health hazard

訊號詞

Danger

危險聲明

防範說明

危險分類

Resp. Sens. 1

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Xue-Feng Gao et al.
Journal of structural biology, 154(1), 20-26 (2006-02-14)
Pyrimidine nucleoside phosphorylase (PYNP) catalyzes the reversible phosphorolysis of pyrimidines in the nucleotide synthesis salvage pathway. We have built a model of a closed active conformation of the three-dimensional structure of PYNP from Bacillus subtilis. Using docking, molecular dynamics, and
A Danchin
DNA research : an international journal for rapid publication of reports on genes and genomes, 4(1), 9-18 (1997-02-28)
Genome comparison permits identification of chromosome regions conserved during evolution. Bacillus subtilis and Escherichia coli are so distant that there exists very few conserved landmarks in their genome organisation. Analysis of the conserved cmk rpsA cluster pinpointed the importance of
M J Pugmire et al.
Structure (London, England : 1993), 6(11), 1467-1479 (1998-11-18)
Pyrimidine nucleoside phosphorylase (PYNP) catalyzes the reversible phosphorolysis of pyrimidines in the nucleotide synthesis salvage pathway. In lower organisms (e.g. Bacillus stearothermophilus) PYNP accepts both thymidine and uridine, whereas in mammalian and other higher organisms it is specific for thymidine
T Hamamoto et al.
Bioscience, biotechnology, and biochemistry, 60(7), 1179-1180 (1996-07-01)
The purine nucleoside phosphorylase (Pu-NPase) and the pyrimidine nucleoside phosphorylase (Py-NPase) have been purified from Bacillus stearothermophilus TH 6-2. The Pu-NPase is a trimer of 30-kDa subunits and the Py-NPase is a dimer of 46-kDa subunits. The isoelectric points of
K Okuyama et al.
Bioscience, biotechnology, and biochemistry, 60(10), 1655-1659 (1996-10-01)
The pyrimidine nucleoside phosphorylase (Py-NPase) of Bacillus stearothermophilus TH 6-2 is a dimer of 46-kDa subunits and catalyzes the reversible phosphorolysis of uridine and thymidine. The gene encoding this pyrimidine nucleoside phosphorylase (pyn gene) has been cloned and sequenced from

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