Ljudmila Kulakova

TL;DR: A simple method for enzymatic synthesis of L and D amino acids from alpha-keto acids with Escherichia coli cells which express heterologous genes is described and optic pure D enantiomers of glutamate and leucine were obtained.

TL;DR: Observations could be explained in terms of a decrease in active-site flexibility brought about by the mutation and were consistent with the hypothesis that cold activity and thermolability arise from local flexibility around the active site of the enzyme.

TL;DR: The recombinant SapSh (rSapSh) was found to have a molecular weight of about 44,000 and to be highly active in the alkaline region (optimum pH, around 9.0) when azocasein and synthetic peptides were used as substrates, but was far less stable than the subtilisin.

TL;DR: The gene of NAD+-dependent formate dehydrogenase (FDH) from Mycobacterium vaccae N10 was cloned into Escherichia coli by hybridization with digoxigenin-labeled DNA probes, which were prepared by amplification of the chromosomal DNA from the bacterium by the polymerase chain reaction with degenerate primers.

TL;DR: A new procedure for stereospecific conversion of various α-keto acids to the corresponding d -amino acids with four thermostable enzymes was developed, obtaining Optically pure d -enantiomers of glutamate, phenylalanine and tyrosine.