Literature summary for 3.6.4.B10 extracted from

Shin, E.J.; Lee, J.W.; Kim, J.H.; Jeon, S.J.; Kim, Y.H.; Nam, S.W.
Overexpression, purification, and characterization of beta-subunit group II chaperonin from hyperthermophilic Aeropyrum pernix K1 (2010), J. Microbiol. Biotechnol., 20, 542-549.

Search for more literature for 3.6.4.B10

Application

Application	Comment	Organism
synthesis	ApCpnB has both foldase and holdase activities and can be used as a powerful molecular machinery for the production of recombinant proteins as soluble and active forms in Escherichia coli	Aeropyrum pernix K1

Cloned(Commentary)

Cloned (Comment)	Organism
subcloned into vector pET21a. The constructed pET21a-ApCpnB is transformed into Escherichia coli BL21 Codonplus (DE3)	Aeropyrum pernix K1

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
61200	-	x * 61200, SDS-PAGE	Aeropyrum pernix K1

Organism

Organism	UniProt	Comment	Textmining
Aeropyrum pernix K1	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Aeropyrum pernix K1

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	in the presence of ATP, ApCpnB effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Specifically, the activity of malate dehydrogenase (MDH) at 85°C is greatly stabilized by the addition of ApCpnB and ATP	Aeropyrum pernix K1	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
?	x * 61200, SDS-PAGE	Aeropyrum pernix K1

Synonyms

Synonyms	Comment	Organism
ApCpnB	-	Aeropyrum pernix K1
chaperonin B	-	Aeropyrum pernix K1

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Release 2023.1 (January 2023)