EC Number |
Application |
Reference |
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3.5.4.6 | analysis |
assessment of synthetic nitro- and polycyclic musks, imidazolium ionic liquids and N-glucopyranosyl ammonium salts |
668434 |
3.5.4.6 | biotechnology |
multicopy integrants of crt genes and co-expression of AMP deaminase improve lycopene production in Yarrowia lipolytica. It is possible to make use of the obtained strains to meet the industrial demand of lycopene production on the basis of further genetic and process optimization |
757279 |
3.5.4.6 | food industry |
noting the use of the enzyme from Aspergillus oryzae in food intended for human consumption and potential presence at trace levels in finished goods, a series of safety studies including an in vitro Ames test and chromosome aberration assay with Chinese hamster lung fibroblasts are conducted along with a 90-day oral toxicity study in rats. AMP deaminase shows no evidence of genotoxicity in the in vitro tests. Following gavage administration of Sprague-Dawley rats at dosages of 19.8, 198.4, or 1984 mg total organic solids (TOS)/kg body weight (bw)/day for 90 days, no adverse effects on body weight gain, food consumption, hematology, clinical chemistry, urinalysis, ophthalmological and histopathological examinations are observed. The no-observed-adverse-effect level is considered to be 1984 mg TOS/kg bw/day, the highest dose tested. Results of the genotoxicity studies and subchronic rat study support the safe use of AMP deaminase produced from Aspergillus oryzae in food production |
-, 756761 |
3.5.4.6 | food industry |
production of 5'-IMP as food additives and pharmaceutical intermediate, important enzyme for the food industry |
-, 756756 |
3.5.4.6 | medicine |
AMPD3 is a potential candidate for a pharmacological therapeutic strategy for remote reperfusion lung injury |
686111 |
3.5.4.6 | medicine |
the C34T T allele of the adenosine monophosphate deaminase-1 gene is associated with improved outcome in patients with cardiac dysfunction. Possession of the adenosine monophosphate deaminase-1 T allele is associated with decreased inotropic requirements before heart donation |
710799 |
3.5.4.6 | synthesis |
the recombinant enzyme is rapidly inactivated below pH 6.0 and at temperatures above 35 °C but under optimal conditions catalysed the highly efficient transformation of AMP to IMP with minimal by-products, suggesting that it could be used for IMP production following protein engineering |
-, 755821 |