15475-13-5

Usage

InChI:InChI=1/C10H10N4O6/c15-4-5(16)9(20-6(4)10(18)19)14-2-13-3-7(14)11-1-12-8(3)17/h1-2,4-6,9,15-16H,(H,18,19)(H,11,12,17)

Upstream product

• 58-63-9 inosine 
• 58-63-9 Inosine 
• 118101-43-2 inosine-5'-aldehyde 
• 28440-13-3 (3aS,4S,6R,6aR)-2,2-dimethyl-6-(6-oxo-1,6-dihydro-9H-purin-9-yl)tetrahydrofuro[3,4-d][1,3]dioxole-4-carboxylic acid 
• 2140-11-6 2',3'-O-isopropylideneinosine 

Downstream Products

• 75930-32-4 N-<2-(3-cyclohexylureido)ethyl>-1-deoxy-1-(1,6-dihydro-6-oxo-9H-purin-9-yl)-β-D-ribofuranuronamide 
• 75930-30-2 1-deoxy-1-(1,6-dihydro-6-oxo-9H-purin-9-yl)-N-<2-(3-methylureido)ethyl>β-D-ribofuranuronamide 
• 68-94-0 Allopurinol 
• 58-63-9 Inosine 
• 75930-23-3 1-deoxy-1-(1,6-dihydro-6-oxo-9H-purin-9-yl)-N-<2-(3-methyl-3-nitrosoureido)ethyl>β-D-ribofuranuronamide 
• 75930-25-5 N-<2-(3-cyclohexyl-1-nitrosoureido)ethyl>-1-deoxy-1-(1,6-dihydro-6-oxo-9H-purin-9-yl)-β-D-ribofuranuronamide 

Relevant academic research and scientific papers

A versatile procedure for the generation of nucleoside 5'- carboxylic acids using nucleoside oxidase

The nucleoside oxidase from Stenotrophomonas maltophilia (FERM BP-2252) has been used to generate 5'-carboxylic acid derivatives of nucleoside analogues. The enzyme, which has a surprisingly broad substrate specificity for unnatural nucleosides, has been

RUTHENIUM TETRAOXIDE: A MILD REAGENT FOR THE OXIDATION OF 2',3'-O-ISOPROPYLIDENE PURINE NUCLEOSIDES

2',3'-O-Isopropylidene purine nucleosides have been oxidized with ruthenium tetraoxide to provide the corresponding 5'-carboxylic acids in quantitative yields under neutral conditions.

Purification and Reaction of a New Enzyme, Nucleoside Oxidase

Nucleoside oxidase, a novel nucleoside oxidizing enzyme has been purified from a crude extract of Pseudomonas maltophilia LB-86 by a ammonium sulfate fractination, heat treatment, column chomatography on DEAE-Toyopearl, and gel filtration twice on Sephacryl S-200.The overall purification was approximately 60-fold with a yield of 35 percent.The purified enzyme gave a single protein band on acrylamide gel electrophoresis.Reaction products from inosine were identified as inosine-5'-aldehyde and inosine-5'-carboxylic acid.The enzyme catalyzed the oxidation of inosine to inosine-5'-carboxylic acid via inosine-5'-aldehyde using molecular oxygen as a primary electron acceptor with no formation of hydrogen peroxide.