EC Number   |
Protein Variants |
Reference  |
|---|
    1.4.1.16 | more |
systems-wide metabolic pathway engineering in Corynebacterium glutamicum for bio-based production of diaminopentane. Superior strains with desirable properties such as (i) the release from unwanted feedback regulation at the level of aspartokinase and pyruvate carboxylase by introducing the point mutations lysC311 and pycA458, (ii) an optimized supply of the key precursor oxaloacetate by amplifying the anaplerotic enzyme, pyruvate carboxylase, and deleting phosphoenolpyruvate carboxykinase which otherwise removes oxaloacetate, (iii) enhanced biosynthetic flux via combined amplification of aspartokinase, dihydrodipicolinate reductase, diaminopimelate dehydrogenase and diaminopimelate decarboxylase, and (iv) attenuated flux into the threonine pathway competing with production by the leaky mutation hom59 in the homoserine dehydrogenasegene |
712938 |
| 1.4.1.16 | F146W |
site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates |
724026 |
| 1.4.1.16 | F146W/M152Q |
site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates |
724026 |
| 1.4.1.16 | M152Q |
site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates |
724026 |
| 1.4.1.16 | H227C |
site-directed saturation mutagenesis, the mutant shows 15.1fold increased activity with phenylpyruvate compared to the wild-type enzyme |
724034 |
| 1.4.1.16 | H227V |
site-directed saturation mutagenesis, the mutant shows 35.1fold increased activity with phenylpyruvate compared to the wild-type enzyme |
724034 |
| 1.4.1.16 | more |
in order to enlarge the substrate binding pocket of the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum to accommodate larger 2-keto acids, e.g. phenylalanine, four amino acid residues, Phe146, Thr171, Arg181, and His227, are targeted for site saturation mutagenesis |
724034 |
| 1.4.1.16 | R181F |
site-directed saturation mutagenesis, the mutant shows 6.4fold increased activity with phenylpyruvate compared to the wild-type enzyme |
724034 |
| 1.4.1.16 | R181F/H227V |
site-directed saturation mutagenesis, the mutant shows 19.3fold increased activity with phenylpyruvate compared to the wild-type enzyme |
724034 |
| 1.4.1.16 | T171P |
site-directed saturation mutagenesis, the mutant shows 2.2fold increased activity with phenylpyruvate compared to the wild-type enzyme |
724034 |
