The substrate range of leucine dehydrogenase and phenylalanine dehydrogenase isolated from different organisms was investigated using a range of hydrophobic alpha-keto acids. Several aliphatic L-amino acids with bulky side chains were synthesized by reductive amination, L-neopentylglycine was produced on 30 kg scale. Besides the reductive amination of the alpha-keto acids these compounds were also investigated as substrates for hydroxyisocaproate dehydrogenase from Lactobacillus confusus and Lactobacillus casei, respectively. (C) 1997 Elsevier Science B.V.