Cloned (Comment) | Organism |
---|---|
expression of His6-tagged wild-type and E99Q/E143Q mutant Ca2+ binding domain, residues 1-169, of NOX5 in Escherichia coli strain BL21(DE3) | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
E99Q/E143Q | site-directed mutagenesis, mutation in the Ca2+ binding domain of NOX5 | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | the activity of NOX5 appears to be regulated by a self-contained Ca2+ binding domain, residues 1-169, the conformational change of the domain upon Ca2+ binding is essential for domain-domain interaction and superoxide production. Ca2+ binding to Ca2+ binding domain induces a conformational change that exposes hydrophobic patches and increases the quenching accessibilities of its Trp residues and 5-((((2-iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid at Cys107, no significant changes in the secondary structures of Ca2+ binding domain upon metal binding. The C-terminal half of the domain has a higher Ca2+ binding affinity, a higher chemical stability, and a slow Ca2+ dissociation. the N- and C-terminal halves of the domain are not completely structurally independent | Homo sapiens | |
additional information | Mg2+ cannot substitute for Ca2+, metal binding/dissociation kinetics, overview | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged wild-type and E99Q/E143Q mutant Ca2+ binding domain of NOX5 from Escherichia coli strain BL21(DE3) by nickel affinity and hydrophobic interaction chromatography, followed by ultrafiltration | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
NADPH oxidase 5 | - |
Homo sapiens |
NOX5 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | 8 | assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | the activity of NOX5 appears to be regulated by a self-contained Ca2+ binding domain, the conformational change of the domain upon Ca2+ binding is essential for domain-domain interaction and superoxide production | Homo sapiens |