* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.
Reference：
[1] Angewandte Chemie - International Edition, 2001, vol. 40, # 10, p. 1948 - 1951
2
[ 328-51-8 ]
[ 106819-03-8 ]
[ 116783-26-7 ]
Reference：
[1] Journal of the American Chemical Society, 2006, vol. 128, # 33, p. 10923 - 10929
[2] Organic Letters, 2016, vol. 18, # 15, p. 3658 - 3661
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[ 644-90-6 ]
[ 106819-03-8 ]
[ 116783-26-7 ]
Reference：
[1] Journal of the American Chemical Society, 1988, vol. 110, # 2, p. 561 - 567
With pyridoxal 5'-phosphate; recombinant Lactobacillus salivarius UCC118 D-amino acid aminotransferase; In aq. phosphate buffer; at 30.0℃; for 0.0166667h;pH 7.5;Enzymatic reaction;
General procedure: Amino acceptor specificity was determined using a modification of the salicylaldehyde method by measuring the rate of pyruvate formation from D-alanine in the presence of an alpha-keto acid. The standard reaction mixture contained 100 mM potassium phosphate buffer (pH 7.5), 50 mM D-alanine, 20 mM alpha-keto acid, 0.05 mM pyridoxal-5?-phosphate and purified D-AAT. The reaction was run at 30 C for 1 min in a total volume of 1 ml, and the reaction was stopped by adding 1 ml of 60% potassium hydroxide, after which 0.5 ml of 2% salicylaldehyde dissolved in 99% ethanol was added, and the mixture was incubated for 30 min at 30 C. Thereafter, 1.5 ml of cold distilled water was added to the orange colored reaction mixture and absorbance at 480 nm was measured. The reaction mixture was also incubated for 1 min without the purified enzyme. The enzyme concentration was determined using the Bradford method with Bio-Rad Protein Assay Dye Reagent Concentrate (Bio-Rad, CA, USA). All enzyme assays were performed more than 3 times.
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