Nucleoside Phosphorylase bacterial lyophilized powder, ≥10 units/mg protein

Properties

Related Categories	2.4.x.x Glycosyltransferases, 2.x.x.x Transferases, Application Index, Biochemicals and Reagents, Chemical Synthesis, Enzyme Class Index, Enzyme-Mediated Synthesis, Enzymes for Diagnostic Kit Manufacturing, Enzymes, Inhibitors, and Substrates, General Metabolic Enzymes, Metabolomics, Nucleotide Metabolism, Specialty Synthesis, Transferases More...
form	lyophilized powder
mol wt	mol wt ~120 kDa
composition	Protein, 40-80%
storage temp.	−20°C

Description

Application

Nucleoside phosphorylase is used in coupled enzyme systems to measure protein dephosphorylation.

This enzyme is useful for enzymatic determination of inorganic phosphorus, 5′-nucleotidase and adenosine deaminase when coupled with xanthine oxidase (XTO-212) and uricase (UAO-201, UAO-211). Purine nucleoside phosophorylase has shown the ability to perform both phosphorylosis and synthesis of purine deoxy- and ribonucleosides. ¹ It has also been found that membrane-associated nucleoside phosphorylases may have a transmembranal orientation with their base and ribose-1-P binding sites on opposite sides of the membrane. ²

Biochem/physiol Actions

Catalyzes the following reaction: purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate

General description

Nucleoside phosphorylase is an enzyme important for the biosynthesis of nucleosides. ³

Unit Definition

One unit will cause the phosphorolysis of 1.0 μmole of inosine to hypoxanthine and ribose 1-phosphate per min at pH 7.4 at 25 °C.

Physical form

Lyophilized powder containing potassium gluconate, mannitol and EDTA

Physical properties

Isoelectric point : 4.1 +/- 0.1
Michaelis constants : 6.4 x 10^-5M (Inosine), 3.2x10^-4M (Pi)
Inhibitors : p-Chloromercuribenzoate, SDS, Hg⁺⁺, Ag⁺Optimum pH : 7.5 - 8.0
Optimum temperature : 65o^C
pH Stability : pH 6.0 - 9.0 (30o^C, 16hr)
Thermal stability : below 60o^C (pH 7.7, 30min)

Price and Availability

Related Papers

2. Regulation of purine utilization in bacteria. VII. Involvement of membrane-associated nucleoside phosphorylase in the uptake and the base-mediated loss of the ribose moiety of nucleosides by Salmonella typhimurium membrane vesicles Rader, R. and J. Hochstadt J. Bacteriol. 128, 290-301, (1976)

Documents

Certificate of Analysis

Certificate of Origin

Enzyme Explorer

Metabolic Pathways Chart (784 KB )

N8264 - Enzyme Assay (15 KB)

Safety Information

Personal Protective Equipment	Eyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter
WGK Germany	3

Technical information & documentation associated with this product is available in the Safety & Documentation tab.

Protocols

Assay Procedure for Nucleoside Phosphorylase Bacterial

One unit causes the formation of one micromole of uric acid per minute under the conditions described below.
Keywords: Extinction coefficient

Papers

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1. A second purine nucleoside phosphorylase in Escherichia coli K-12. II. Properties of xanthosine phosphorylase and its induction by xanthosine Hmmer-Jespersen, K. Mol. Genet. Genomics 179, 341-8, (1980)

2. Regulation of purine utilization in bacteria. VII. Involvement of membrane-associated nucleoside phosphorylase in the uptake and the base-mediated loss of the ribose moiety of nucleosides by Salmonella typhimurium membrane vesicles Rader, R. and J. Hochstadt J. Bacteriol. 128, 290-301, (1976)

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3. Enzymatic synthesis of nucleosides by nucleoside phosphorylase co-expressed in Escherichia coli Ding, Q., et al. J. Zhejiang Univ. Sci. 11, 880-8, (2010)

Golimumab, a human antibody to tumour necrosis factor {α} given by monthly subcutaneous injections, in active rheumatoid arthritis despite methotrexate therapy: the GO-FORWARD Study. Keystone E.C., et al Ann. Rheum. Dis. 68(6), 789-96, (2009)

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Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis. Drake, E.J., et al Biochemistry 49(43), 9292-305, (2010)

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A Continuous Kinetic Assay For Adenylation Enzyme Activity And Inhibition. Wilson, D.J., et al. Anal. Biochem. 404, 56-63, (2010)

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