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biotechnology
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evaluation of biotin overproduction, biotin production by Bacillus subtilis fermentation can be optimized by addition of exogenous lysine or mutational deregulation of lysine in the producing strain
pharmacology
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enzyme is a potential drug target in tuberculosis treatment
analysis
radiochemical assay for the bifunctional enzyme that monitors the formation of acid stable [14C]-DTB from acid-labile 14CO2 in the presence of appropriate substrates and cofactors
analysis
simple, cheap, and sensitive microplate fluorescence assay for 7,8-diaminopelargonic acid aminotransferase activity, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The method relies on the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol. The assay was validated with the known inhibitor desmethyl-KAPA, i.e. 8-amino-7-oxopelargonic acid, and adapted to microplate for high-throughput screening
analysis
analytical method to measure the enantiomeric excess of substrate 8-amino-7-oxononanoic acid, based on the derivatization of its amine function, by orthophtalaldehyde and N-acetyl-L-cysteine, followed by high pressure liquid chromatography separation. Using this methodology and enantiopure samples of 8-amino-7-oxononanoic acid, it appears that racemization of 8-amino-7-oxononanoic acid occurs rapidly with half-lives from 1 to 8 h, not only in 4 M HCl but also in the usual pH range, from 7 to 9
analysis
simple, cheap, and sensitive microplate fluorescence assay, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The principle of the method is the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol. The assay is validated with inhibitor 8-amino-7-oxopelargonic acid and adapted to microplate
analysis
microplate fluorescence assay for 7,8-diaminopelargonic acid aminotransferase that is simple, cheap, and sensitive, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The principle of the method is the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol
analysis
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analytical method to measure the enantiomeric excess of substrate 8-amino-7-oxononanoic acid, based on the derivatization of its amine function, by orthophtalaldehyde and N-acetyl-L-cysteine, followed by high pressure liquid chromatography separation. Using this methodology and enantiopure samples of 8-amino-7-oxononanoic acid, it appears that racemization of 8-amino-7-oxononanoic acid occurs rapidly with half-lives from 1 to 8 h, not only in 4 M HCl but also in the usual pH range, from 7 to 9
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analysis
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simple, cheap, and sensitive microplate fluorescence assay, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The principle of the method is the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol. The assay is validated with inhibitor 8-amino-7-oxopelargonic acid and adapted to microplate
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analysis
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microplate fluorescence assay for 7,8-diaminopelargonic acid aminotransferase that is simple, cheap, and sensitive, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The principle of the method is the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol
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