EC Number   |
Protein Variants |
Reference |
|---|
    2.1.2.1 | A206C |
the mutation yields an enzyme that forms a 3-bromopyruvate-enzyme complex and is completely inactivated |
756098 |
| 2.1.2.1 | C203S |
no loss of activity |
657811 |
| 2.1.2.1 | D227N |
nearly complete loss of activity, enzyme exists as dimer |
657811 |
| 2.1.2.1 | E53Q |
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity |
719472 |
| 2.1.2.1 | E74K |
specific activities drastically reduced with serine as substrate, but D-alanine transamination and allothreonine cleavage at rates comparable with wild-type enzyme |
441430 |
| 2.1.2.1 | E74Q |
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity |
719472 |
| 2.1.2.1 | E74Q |
specific activities drastically reduced with serine as substrate, but D-alanine transamination and allothreonine cleavage at rates comparable with wild type enzyme |
441430 |
| 2.1.2.1 | E75L |
no activity with L-Ser and tetrahydrofolate. The mutant enzyme does not catalyze the formation of 5,10-methenyl-tetrahydropteroylglutamate or N5-hydroxymethylene-tetrahydropteroylglutamate |
658083 |
| 2.1.2.1 | E75L |
site-directed mutagenesis, mutation of a substrate binding residue, the mutant retains tetrahydrofolate-independent aldolase activity |
719472 |
| 2.1.2.1 | E75Q |
500fold decrease in activity with L-Ser and tetrahydrofolate compared to wild-type enzyme, the KM-value for L-allothreonine is 10fold increased compared to wild-type value, the turnover-number for reaction with L-allothreonine is 4.3fold increased compared to wild-type enzyme |
658083 |
