EC Number   |
Protein Variants |
Reference |
|---|
    6.3.2.8 | C230A |
activity completely lost at 42°C |
651239 |
| 6.3.2.8 | C426A |
Km increased 3fold for ATP and 10fold for UDP-MurNAc and L-alanine, with respect to the wild-type |
651239 |
| 6.3.2.8 | H199A |
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates |
1292 |
| 6.3.2.8 | K130A |
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates |
1292 |
| 6.3.2.8 | more |
mutation of the phosphorylation site threonine residues highly impairs enzyme activity |
693199 |
| 6.3.2.8 | more |
screening and identification of a transposon mutant impaired in diazotrophic growth, the mutant strain contains a transposon insertion at nucleotide position -476 relative to the annotated translational start site of gene alr5065. The mutant, designated C6, is unable to grow diazotrophically and displays a deficit in heterocyst differentiation, producing 4.5% heterocysts compared to the 9% produced by the wild type. Proper heterocyst production is restored in mutant C6 when the mutation is complemented with both alr5065 and alr5066, encoding enzymes MurC and MurB, as PpetE-murC/B (pPJAV328) in the presence of copper, but not when either gene is introduced individually, which suggests that alr5065 and alr5066 may be in an operon and the transposon insertion affectes the expression of both genes. After repeated rounds of subculturing, C6 loses viability and ceases to grow in culture. Generation of murC mutant strain UHM351, in which murC is inactivated by pPJAV309, phenotype, overview |
-, 745220 |
| 6.3.2.8 | N293A |
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates |
1292 |
| 6.3.2.8 | N296A |
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates |
1292 |
| 6.3.2.8 | R151W |
site-directed mutagenesis |
-, 743924 |
| 6.3.2.8 | R327A |
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates |
1292 |
