The substrate specificity of LeuDH from Bacillus stearothermophilus an
d of PheDH from Rhodococcus sp. was investigated and found to be compl
ementary. LeuDH from different organisms have remarkably similar subst
rate specificity. During optimization of the synthesis of L-tert-leuci
ne, two byproducts (N-alpha-pivaloyl-tert-leucine amide (I) and 2,4-di
-tert-butyl-5-hydroxy-imidazol (II)) were found and identified which o
riginate from chemical reactions of keto acid and ammonia.