EC Number   |
Protein Variants |
Reference |
|---|
    5.4.99.1 | C15A |
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive |
3459 |
| 5.4.99.1 | C15N |
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive |
3459 |
| 5.4.99.1 | C15S |
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive |
3459 |
| 5.4.99.1 | E171A |
turnover number for glutamate is reduced 27.6fold, KM-value is increased 1.1fold, Km-value for adenosylcobalamin is reduced 1.23fold |
650824 |
| 5.4.99.1 | E171D |
turnover number for glutamate is reduced 1.8fold, KM-value is reduced 1.54fold, Km-value for adenosylcobalamin is reduced 2.7fold |
650824 |
| 5.4.99.1 | E171N |
turnover number for glutamate is reduced 232fold, KM-value is increased by 1.8fold, Km-value for adenosylcobalamin is reduced 1.4fold |
650824 |
| 5.4.99.1 | E171Q |
turnover number for glutamate is reduced 53fold, KM-value is reduced 2.4fold, Km-value for adenosylcobalamin is reduced 2fold, mutant enzyme is independent of pH |
650824 |
| 5.4.99.1 | more |
fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit |
3458 |
| 5.4.99.1 | more |
production of mesaconate in Escherichia coli by engineered glutamate mutase pathway, establishment of mesaconate pathway in Escherichia coli. First, glutamate is synthesized from glucose via glycolysis and TCA cycle.Then glutamate is converted into 3-methylaspartate by glutamate mutase. Finally, mesaconate is formed by elimination of ammonia from 3-methylaspartate via MAL. Since Escherichia coli does not contain glutamate mutase and 3-methylaspartate ammonia lyase, the two enzymes from Clostridium tetanomorphum are heterologously expressed. To increase the flux from glutamate to mesaconate, two effective strategies are employed to optimize the critical enzyme activity in the pathway: one is regenerating inactive mutase. The other is enhancing the availability of glutamate mutase (stability) and coenzyme B12 (regeneration). For the highest mesaconate production strain EM9, the consumed glutamate is 6.91 g/l (40.9 mM) and mesaconate titer is 7.81 g/l (60 mM). The GlmE from Clostridium cochlearium shows best performance in mesaconate titer because GlmE is more stable than MutE |
-, 748550 |
| 5.4.99.1 | more |
the S subunit is genetically fused to the C-terminus of the E subunit through an 11 amino acid 5-Gly linker segment. The affinity of adenosylcobalamine is unchanged, but the turnover-number and the Km-value for Glu in the conversion of L-Glu to (2S,3S)-3-methylaspartate are decreased by about a third |
3455 |
