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Literature summary for 1.6.3.1 extracted from

  • Wei, C.C.; Motl, N.; Levek, K.; Chen, L.Q.; Yang, Y.P.; Johnson, T.; Hamilton, L.; Stuehr, D.J.
    Conformational States and kinetics of the calcium binding domain of NADPH oxidase 5 (2010), Open Biochem. J., 4, 59-67.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.6.3.1

Cloned(Commentary)

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

Protein Variants Comment Organism
E99Q/E143Q site-directed mutagenesis, mutation in the Ca2+ binding domain of NOX5 Homo sapiens

Metals/Ions

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

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

Synonyms Comment Organism
NADPH oxidase 5
-
 Homo sapiens
NOX5
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8 assay at Homo sapiens

General Information

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