Literature summary for 3.6.4.10 extracted from

Schaupp, A.; Marcinowski, M.; Grimminger, V.; Boesl, B.; Walter, S.
Processing of proteins by the molecular chaperone Hsp104 (2007), J. Mol. Biol., 370, 674-686.

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Activating Compound

Activating Compound	Comment	Organism	Structure
ATP	ATP binding to nucleotide-binding domain 1 serves as a central regulatory switch for the chaperone, it triggers binding of polypeptides and stimulates ATP hydrolysis in the C-terminal nucleotide-binding domain 2 by more than 2 orders of magnitude	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
E285Q	impaired hydrolysis of ATP at nucleotide-binding domain 1	Saccharomyces cerevisiae
E285Q/E687Q	impaired hydrolysis of ATP at nucleotide-binding domains 1 and 2	Saccharomyces cerevisiae
E687Q	impaired hydrolysis of ATP at nucleotide-binding domain 2	Saccharomyces cerevisiae
K218T	impaired binding and hydrolysis of ATP at nucleotide-binding domain 1	Saccharomyces cerevisiae
K620T	impaired binding and hydrolysis of ATP at nucleotide-binding domain 2	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	isoform Hsp104	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	Hsp104 actively unfolds its substrates during processing	Saccharomyces cerevisiae	?	-	?

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Release 2023.1 (January 2023)