Characterization of a novel type homoserine dehydrogenase with high oxidation activity from Arthrobacter nicotinovorans

• A novel homoserine dehydrogenase ( An HSD) from A. nicotinovorans was identified. HSD not homologous to HSDs enzymes which are part of the aspartate pathway. insensitive feedback inhibition l -threonine and -methionine. This study provided possibility for biosynthesis -aspartate-β-semialdehyde. Homoserine (HSD) is a key enzyme in synthesis pathway family amino acids. can catalyze reversible reaction -aspartate-β-semialdehyde -Asa) -homoserine -Hse). In this study, one putative Arthrobacter , named HSD, different those that aspartic acid metabolic pathway, might be responsible specific oxidation -Hse. Surprisingly, analysis showed purified exhibited high activity At pH 10.0 40 °C, K m k cat 5.97 ± 1.10 mM 3.61 s −1 respectively. terms cofactor reliance, preferred NAD + than NADP as cofactor. The physiological role under natural also discussed . Collectively, these findings provide insight better understanding possible biotransformation method preparing -Asa.