Application | Comment | Organism |
---|---|---|
medicine | identification of mutations E244V and A551T and splice site mutation IVS11+1G to T in patients with complete loss of enzymic activity | Sus scrofa |
medicine | identification of mutations E244V and A551T and splice site mutation IVS11+1G to T in patients with complete loss of enzymic activity | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
mutants E244V and A551T | Sus scrofa |
Protein Variants | Comment | Organism |
---|---|---|
A551T | natural mutation identified in a human with complete loss of enzymic activity. Crystallization data of Sus scrofa recombinant mutant, mutation might prevent binding of the prosthetic group FMN and affect folding of the enzyme protein | Sus scrofa |
A551T | natural mutation identified in a patient with complete loss of enzymic activity | Homo sapiens |
E244V | natural mutation identified in a human with complete loss of enzymic activity. Crystallization data of Sus scrofa recombinant mutant, mutation interferes with the electron flow between NADPH and the pyrimidine binding site of the enzyme | Sus scrofa |
E244V | natural mutation identified in a patient with complete loss of enzymic activity | Homo sapiens |
additional information | natural mutant IVS11+1G to T leads to a cryptic splice site within exon 11 that results in loss of amino acid residues 400-446 in enzyme primary sequence | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q12882 | - |
- |
Sus scrofa | - |
recombinant enzyme | - |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | - |
Sus scrofa | |
NADPH | - |
Sus scrofa |