EC Number   |
Protein Variants |
Reference |
|---|
    1.5.1.2 | E221A |
affinity for substrates is increased |
675382 |
| 1.5.1.2 | E221G |
insoluble protein |
675382 |
| 1.5.1.2 | more |
identification of a single homozygous region near the telomere of chromosome 17 in a cohort of patients with cutis laxa type 2. The single nucleotide change leads to a missense mutation adjacent to a slice junction in the gene encoding pyrroline-5-carboxylate reductase 1 which results in exon skipping and leads to deletion of reductase functional domain-coding region and an obligatory downstream frameshift |
695442 |
| 1.5.1.2 | more |
N-truncation results in an insoluble protein, C-truncation does not alter the activity |
675382 |
| 1.5.1.2 | R119C |
a naturally occuring mutation in patients with microcephaly and hypomyelination. The mutant is catalytically impaired, depending on whether NADPH or NADH is used, the catalytic efficiency of the R119C protein variant is 40 or 366 times lower than that of the wild-type enzyme |
762678 |
| 1.5.1.2 | R119C |
mutation identified in patient with microcephaly and hypomyelination, mutant is catalytically impaired |
762678 |
| 1.5.1.2 | R251C |
a naturally occuring mutation in patients with microcephaly and hypomyelination. The mutant is catalytically impaired, depending on whether NADPH or NADH is used, the catalytic efficiency of the R119C protein variant is 7 or 26 times lower than that of the wild-type enzyme. The R251C protein variant has a pronounced folding defect. The R251C variant displays the least overall regular alpha-helical character of the PYCR2 proteins, yet the R251C variant also displays strong overall regular beta-strand or beta-sheet character |
762678 |
| 1.5.1.2 | R251C |
mutation identified in patient with microcephaly and hypomyelination, mutant is catalytically impaired and has a pronounced folding defect |
762678 |
| 1.5.1.2 | T238A |
mutation in conserved residue, about 10fold decrease in catalytic efficiency |
740763 |
