EC Number   |
Application |
Reference |
|---|
    1.4.1.21 | analysis |
development of a genetically encoded fluorescent protein construct for monitoring of L-Asp in vitro, and employment of aspartate dehydrogenase scaffold as a biorecognition element |
724614 |
| 1.4.1.21 | analysis |
usage of AspDH in the quantitative measurement of amino acids, 2-oxo acids, and ammonia or urea in studies involving clinical settings, bioprocess control, and nutrition |
-, 724068 |
| 1.4.1.21 | more |
first report of an archaeal L-aspartate dehydrogenase, within the archaeal domain, homologues in many methanogenic species, but not in Thermococcales or Sulfolobales species |
672387 |
| 1.4.1.21 | synthesis |
individual overexpression of ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli, and diaminopimelate dehydrogenase from Pseudothermotoga thermarum in Corynebacterium glutamicum LC298, a basic lysine producer, increases the production of lysine by 30.7%, 32.4%, 17.4%, and 36.8%, respectively. The highest increase of lysine production (30.7%) is observed for a triple-mutant strain (27.7 g/L, 0.35 g/g glucose) expressing ASPDH, aspartate-semialdehyde dehydrogenase from Tistrella mobilis, dihydrodipicolinate reductase from Escherichia coli. A quadruple-mutant strain expressing all of the four NADH-utilizing enzymes allows high lysine production (24.1 g/l, 0.30 g/g glucose) almost independent of the oxidative pentose phosphate pathway |
763424 |
| 1.4.1.21 | synthesis |
potential application of AspDH for cost-effective and efficient L-Asp production via both fermentative and enzymatic systems. The ability to catalyze stereospecific reactions has also stimulated research interest in amino acid dehydrogenases as biocatalysts to produce synthons for pharmaceutical and food industries, e.g., enantiomerically pure non-natural amino acids as drug precursors |
-, 724068 |
