EC Number |
Protein Variants |
Reference |
---|
1.1.1.282 | D107A |
site-directed mutagenesis |
656292 |
1.1.1.282 | K71G |
site-directed mutagenesis |
656292 |
1.1.1.282 | more |
construction of a gene qsuD deletion mutant. Cell cultures of the qsuD-deficient strain in glucose-containing medium are light yellow, whereas those of the wild-type in shikimate or quinate-containing medium are brown |
-, 724089 |
1.1.1.282 | more |
construction of an enzyme ydiB- knockout mutant JM101 strain. Fermentation processes for the production of shikimate in overproducing strains of Escherichia coli result in the simultaneous synthesis of quinic acid and 3-dehydroshikimic acid. The production of high amounts of these byproducts significantly reduces the yield of shikimate, and more importantly, the presence of quinate impairs the efficiency of shikimate extraction from supernatant cultures, reducing its purity and increasing downstream processing costs. The inactivation of the ydiB gene increases the molar proportion of shikimate and 3-dehydroshikimate with respect to quinate, showing a molar ratio of 0.81/0.05/0.14 (mol/mol/mol) of shikimate/quinate/3-dehydroshikimate. In this derivative strain, quinate production is 6.17% relative to shikimate (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce quinate production below 10% (mol/mol) relative to ahkimate in culture fermentations for shikimate production |
-, 740881 |
1.1.1.282 | more |
ydiB-encoded enzyme knockout in Escherichia coli strain PB12 |
-, 761708 |
1.1.1.282 | N193D |
site-directed mutagenesis, inactive mutant |
-, 740100 |
1.1.1.282 | N193L |
site-directed mutagenesis, inactive mutant |
-, 740100 |
1.1.1.282 | N193Q |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
-, 740100 |
1.1.1.282 | N193S |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
-, 740100 |
1.1.1.282 | N92A |
site-directed mutagenesis |
656292 |