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Enzymatic characterization of a NADH-dependent diaphorase from Lysinibacillus sp. strain PAD-91.
Kianmehr A, Oladnabi M, Mahrooz A, Ansari J, Mahdizadeh R. Kianmehr A, et al. Protein Expr Purif. 2018 Jun;146:1-7. doi: 10.1016/j.pep.2018.01.005. Protein Expr Purif. 2018. PMID: 29414067
The optimum pH and temperature for the catalytic activity of the enzyme was about pH 7.5 and 30 C. The K(m) and V(max) values were estimated to be 0.025 mM and 1.33 mumol/min, respectively. ...
The optimum pH and temperature for the catalytic activity of the enzyme was about pH 7.5 and 30 C. The K(m) and V(max) values were es …
Recombinant expression, characterization and application of a dihydrolipoamide dehydrogenase with diaphorase activity from Bacillus sphaericus.
Kianmehr A, Mahdizadeh R, Oladnabi M, Ansari J. Kianmehr A, et al. 3 Biotech. 2017 Jun;7(2):153. doi: 10.1007/s13205-017-0763-0. Epub 2017 Jun 8. 3 Biotech. 2017. PMID: 28597164 Free PMC article.
Different metal ions and inhibitors showed no influence on the activity of target enzyme. The K (m) and V (max) values for NADH were estimated to be 0.33 mM and 200.0 U/ml, respectively. ...
Different metal ions and inhibitors showed no influence on the activity of target enzyme. The K (m) and V (max) values for NADH were …