N3665
Pyrimidine Nucleoside Phosphorylase from Bacillus subtilis
recombinant, expressed in E. coli, ≥70 units/mg protein
Sinônimo(s):
PynP
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About This Item
Produtos recomendados
recombinante
expressed in E. coli
forma
lyophilized powder
atividade específica
≥70 units/mg protein
temperatura de armazenamento
−20°C
Descrição geral
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.
Ações bioquímicas/fisiológicas
Pyrimidine nucleoside phosphorylase functions in the nucleotide synthesis salvage pathway by catalyzing the reversible phosphorolysis of pyrimidines. Both uridine and thymidine are substrates.
Definição da unidade
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.
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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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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