EC Number   |
Protein Variants |
Reference |
|---|
    6.3.3.3 | G169N |
Km value for (7R, 8S)-7,8-diaminopelargonic acid similar to wild-type, 3fold increase in Km value for carbonate |
-, 746545 |
| 6.3.3.3 | more |
construction of bio3 insertion mutants, which have a similar phenotype to the bio1 and bio2 auxotrophs identified using forward genetic screens for arrested embryos rescued on enriched nutrient medium. Genes bio3 and bio1 mutants define a single genetic complementation group, separate BIO3 and BIO1 transcripts and two different types of chimeric BIO3-BIO1 transcripts are produced. One of the fused transcripts is monocistronic and encodes a bifunctional fusion protein. A splice variant is bicistronic, with distinct but overlapping reading frames. Dual functionality of the monocistronic transcript is confirmed by complementing the orthologous auxotrophs of Escherichia coli strain. Allelism between bio1 and bio3 heterozygotes and phenotypes, overview |
694716 |
| 6.3.3.3 | N175A |
2.7fold decrease in Km value for CTP |
746545 |
| 6.3.3.3 | N175G |
no significant effects on Km value for ATP, CTP |
746545 |
| 6.3.3.3 | T11V |
active site mutant enzymes: T11V, E12A, E12D, K15Q, K37L, K37Q, K37R, S41A, S41C, T11V mutant shows a 24000fold increase in the Km for ATP with little or no change in the Km for 7,8-diaminononanoate and in turnover number. Mutants E12A and E12D show wild-type activity with slightly elevated turnover numbers. Unlike wild-type enzyme mutant enzyme E12A has the same apparent Km at subsaturating and saturating ATP concentrations. Mutant enzymes K15Q, K37Q, and K37R have no catalytic activity. Mutant enzymes S41A and S41C have the same turnover number as the wild-type enzyme and a moderate increase in Km for ATP and 7,8-diaminononanoate |
1350 |
