EC Number   |
Protein Variants |
Reference |
|---|
    5.1.1.10 | H152S |
ratio of elimination reaction to racemization is 1.4 compared to 3.7 in wild-type |
662359 |
| 5.1.1.10 | I384M |
I384M mutant BAR shows the highest activity for Trp. Using I384M mutant BAR the proportion of D-Trp reaches 43% while wildtype BAR racemizes only 6% of initial L-Trp |
671544 |
| 5.1.1.10 | I384M |
specific activity: 0.124 (substrate Trp), 0.0744 (substrate Phe), 0.223 (substrate Lys), 0.026 (substrate Ala) |
671544 |
| 5.1.1.10 | I83L/D361V/Y396C |
specific activity: 0.0303 (substrate Trp), 0.0257 (substrate Phe), 0.473 (substrate Lys), 0.0121 (substrate Ala) |
671544 |
| 5.1.1.10 | K233A |
site-directed mutagenesis |
-, 747857 |
| 5.1.1.10 | L126H/Y396C |
specific activity: 0.0524 (substrate Trp), 0.0436 (substrate Phe), 0.477 (substrate Lys), 0.0144 (substrate Ala) |
671544 |
| 5.1.1.10 | more |
for D-lysine production, a two-step process for D-lysine production from L-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase is developed. Enzyme AAR is not a suitable candidate compared to enzyme Lyr (EC 5.1.1.5) from Proteus mirabilis |
-, 747470 |
| 5.1.1.10 | more |
random mutagenesis on bar gene is performed to obtain mutant BAR derivates with high activity for Trp. Five positive mutant are isolated after the two-step-screening of the randomly mutated BAR |
671544 |
| 5.1.1.10 | more |
substitutions at Y396 and I384 increases the Trp specific racemization activity and the racemazation activity for overall amino acids, respectively |
671544 |
| 5.1.1.10 | N154F |
ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type |
662359 |
