Literature summary for 1.13.12.24 extracted from

Eremeeva, E.; Vysotski, E.
Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin (2017), J. Photochem. Photobiol. B, 174, 97-105 .

Search for more literature for 1.13.12.24

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Aequorea victoria
expression in Escherichia coli	Obelia longissima

Protein Variants

Protein Variants	Comment	Organism
additional information	mutation of all 3 Cys resiudes to Ser. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild-type aequorin. Mutant aequorin shows increased conformational flexibility	Aequorea victoria
additional information	mutation of all 5 Cys resiudes to Ser. Cys-free obelin retains only about 10% of the bioluminescence activity of wild-type obelin and binds coelenterazine and forms active photoprotein much less effectively. The mutation drastically changes the bioluminescence kinetics of obelin completely eliminating a fast component from the light signal decay curve. Replacement of Cys residues increases conformational flexibility	Obelia longissima

Organism

Organism	UniProt	Comment	Textmining
Aequorea victoria	P07164	isoform aequorin-1	-
Obelia longissima	Q27709	-	-

Synonyms

Synonyms	Comment	Organism
obelin	-	Obelia longissima

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
28.8	-	Cys-free mutant, melting temperature	Obelia longissima
44.6	-	Cys-free mutant, melting temperature	Aequorea victoria
49.1	-	wild-type, melting temperature	Obelia longissima
53.3	-	wild-type, melting temperature	Aequorea victoria

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Release 2023.1 (January 2023)