Article Abstract:
The opine dehydrogenase gene from Arthrobacter sp. strain 1C was cloned and expressed in Escherichia coli. The protein product of the gene appears to be the only known enzyme in bacteria that can catalyze the reversible oxidation-reduction reaction involving secondary amine dicarboxylic acids. The gene, called odh, was overexpressed in E. coli using the lac promoter in the plasmid pBluescript KS(-). The NAD+-dependent protein product appears to be a homodimer.
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Article Abstract:
The effect of borate on enhancing 5'-position selectivity of enzymatic transglucosylation to pyridoxine (PN) and the possibility that this effect could be applied to practical formation of PN-5'-alpha-Glc is described. A decrease in the formation of pyridoxine 5'-alpha-D-glucoside was observed in the reaction with borate, but this decrease was overcome by optimizing the pH and increasing the amount of cells in the reaction mixture.
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Article Abstract:
The quantitatively significant stereoselective microbial production of D-malate from maleate is discussed. An intact cell system was used to screen various maleate-utilizing microorganisms for enzyme activity. D-malate was best produced by an Anthriobacter sp. strain. Reaction activity formation and cell growth were facilitated by the addition of amino acids. A very good yield of D-malate was derived.
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