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<< < Results 11 - 20 of 47 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16M152E inactive 742276
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16M152H the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and no activity towards pyruvate compared to the wild type enzyme 742276
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16M152K the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme 742276
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16M152L the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and pyruvate compared to the wild type enzyme 742276
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16M152N the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme 742276
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16M152Q site-directed mutagenesis, the mutant shows altered activity levels with meso-2,6-diaminoheptanedioate and pyruvate as substrates 724026
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16M152S the mutant shows increased activity towards meso-2,6-diaminoheptanedioate and reduced activity towards pyruvate compared to the wild type enzyme 742276
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16M152W inactive 742276
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16more 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
Show all pathways known for 1.4.1.16Display the word mapDisplay the reaction diagram Show all sequences 1.4.1.16more 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
<< < Results 11 - 20 of 47 > >>