Literature summary for 1.13.12.24 extracted from

Jafarian, V.; Sajedi, R.H.; Hosseinkhani, S.; Sariri, R.; Taghdir, M.; Khalifeh, K.; Vafa, M.; Aghamaali, M.R.
Structural and functional consequences of EF-hand I recovery in mnemiopsin 2 (2018), Int. J. Biol. Macromol., 118, 2006-2013 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
recombinantly expressed in Escherichia coli with Hexa-His-tag tail at N-terminal	Mnemiopsis leidyi

Protein Variants

Protein Variants	Comment	Organism
E50G	the luminescence activity of the variant is about 17times greater than that of wild-type photoprotein. The activity of E50G variant increases as a result of more flexibility that is brought about by Gly essential for adopting the correct conformation for functional activity. In comparison with wild-type protein, the variant shows higher optimum temperature and calcium sensitivity as well as slower rate of luminesx02cence decay	Mnemiopsis leidyi

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	calcium-regulated photoprotein	Mnemiopsis leidyi

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
27000	-	SDS-PAGE	Mnemiopsis leidyi

Organism

Organism	UniProt	Comment	Textmining
Mnemiopsis leidyi	E0X987	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Mnemiopsis leidyi

Subunits

Subunits	Comment	Organism
?	x * 27000, SDS-PAGE	Mnemiopsis leidyi

Synonyms

Synonyms	Comment	Organism
mnemiopsin 2	-	Mnemiopsis leidyi

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	9.5	mutant enzyme E50G	Mnemiopsis leidyi
9	-	wild-type enzyme	Mnemiopsis leidyi

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Release 2023.1 (January 2023)