Literature summary for 1.14.14.3 extracted from

Gnuchikh, E.; Baranova, A.; Schukina, V.; Khaliullin, I.; Zavilgelsky, G.; Manukhov, I.
Kinetics of the thermal inactivation and the refolding of bacterial luciferases in Bacillus subtilis and in Escherichia coli differ (2019), PLoS ONE, 14, e0226576 .

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Application

Application	Comment	Organism
synthesis	upon expression in Bacillus subtilis cells, luciferase is substantially more thermostable than in Escherichia coli. Thermal inactivation in Bacillus subtilis at 48.5#°C behaves as a first-order reaction. In Escherichia coli, the first order rate constant of the thermal inactivation exceeds that observed in B. subtilis cells 2.9 times. In dnaK-negative strains of Bacillus subtilis, both the rates of thermal inactivation and the efficiency of refolding are similar to that observed in wild-type strains	Photorhabdus luminescens
synthesis	upon expression in Bacillus subtilis cells, luciferase is substantially more thermostable than in Escherichia coli. Thermal inactivation in the cells of Escherichia coli and Bacillus subtilis may be described by first and third order kinetics, respectively. In dnaK-negative strains of Bacillus subtilis, both the rates of thermal inactivation and the efficiency of refolding are similar to that observed in wild-type strains	Photobacterium leiognathi

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Bacillus subtilis and in Escherichia coli	Photorhabdus luminescens
expression in Bacillus subtilis and in Escherichia coli	Photobacterium leiognathi

Organism

Organism	UniProt	Comment	Textmining
Photobacterium leiognathi	P09140 and P09141	P09140 i.e. alpha subunit LuxA, P09141 i.e. beta subunit LuxB	-
Photorhabdus luminescens	P23146 and P19840	P23146 i.e. alpha subunit LuxA, P19840 i.e. beta subunit LuxB	-

Synonyms

Synonyms	Comment	Organism
LuxA	-	Photorhabdus luminescens
LuxA	-	Photobacterium leiognathi
LuxB	-	Photorhabdus luminescens
LuxB	-	Photobacterium leiognathi

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Release 2023.1 (January 2023)