40809
Purine nucleoside phosphorylase
recombinant, expressed in E. coli, ≥120 U/mL
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Servicio técnico
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Permítanos ayudarlerecombinant
expressed in E. coli
form
buffered aqueous solution (100 mM phosphate buffer with 1 mM MgCl2)
specific activity
≥120 U/mL
storage temp.
−20°C
InChI
1S/C10H12N4O4/c15-2-6-7(16)8(17)10(18-6)14-4-13-5-1-11-3-12-9(5)14/h1,3-4,6-8,10,15-17H,2H2/t6-,7-,8-,10-/m1/s1
InChI key
MRWXACSTFXYYMV-FDDDBJFASA-N
Application
Purine nucleoside phosphorylase is used to study nucleotide salvage pathways and purine metabolism. It is used to study purine nucleoside phosphorylase deficiency and responsible PNP genetic mutations.
Biochem/physiol Actions
Purine nucleoside phosphorylase is an enzyme involved in purine metabolism. PNP metabolizes adenosine into adenine, inosine into hypoxanthine, and guanosine into guanine. Mutations in the PNP gene are responsible for purine nucleoside phosphorylase deficiency.
Other Notes
1 U will cause the phosphorolysis 1 μmol of inosine to hypoxanthine and ribose 1-phosphate per minute at pH 7.4 at 25°C
Clase de almacenamiento
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Purine nucleoside phosphorylase deficiency with a novel PNP gene mutation: a first case report from India
Manisha Rajan Madkaikar, et al.
BMJ Case Reports, DOI:10-DOI:10 (2011)
Fernanda Canduri et al.
Biochemical and biophysical research communications, 313(4), 907-914 (2004-01-07)
Human purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effect on B-cell function. PNP
Candida Deves et al.
Bone, 52(1), 167-175 (2012-10-03)
Purine nucleoside phosphorylase (PNP) is a purine-metabolizing enzyme that catalyzes the reversible phosphorolysis of 6-oxypurine (deoxy)nucleosides to their respective bases and (deoxy)ribose-1-phosphate. It is a key enzyme in the purine salvage pathway of mammalian cells. The present investigation sought to