N3665
Pyrimidine Nucleoside Phosphorylase from Bacillus subtilis
recombinant, expressed in E. coli, ≥70 units/mg protein
别名:
PynP
产品名称
Pyrimidine Nucleoside Phosphorylase from Bacillus subtilis, recombinant, expressed in E. coli, ≥70 units/mg protein
recombinant
expressed in E. coli
form
lyophilized powder
specific activity
≥70 units/mg protein
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
Pyrimidine nucleoside phosphorylase functions in the nucleotide synthesis salvage pathway by catalyzing the reversible phosphorolysis of pyrimidines. Both uridine and thymidine are substrates.
General description
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.
Other Notes
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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
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
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
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