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Merck

N3665

Sigma-Aldrich

Pyrimidine Nucleoside Phosphorylase from Bacillus subtilis

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

Sinónimos:

PynP

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About This Item

Comisión internacional de enzimas:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

form

lyophilized powder

specific activity

≥70 units/mg protein

storage temp.

−20°C

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.

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.

Unit Definition

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_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
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
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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