Literature summary for 3.4.21.53 extracted from

Patterson, J.; Vineyard, D.; Thomas-Wohlever, J.; Behshad, R.; Burke, M.; Lee, I.
Correlation of an adenine-specific conformational change with the ATP-dependent peptidase activity of Escherichia coli Lon (2004), Biochemistry, 43, 7432-7442.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
hydrolysis of proteins in presence of ATP	binding of ATP induces a conformational change that facilitates the coupling of nucleotide hydrolysis with peptide substrate delivery to the peptidase activs site	Escherichia coli	a

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kcat-value of peptide cleavage decreases with the reduction in the nucleotide binding affinity in the following order: ATP, CTP, GTP, UTP. Both nucleotide binding and hydrolysis contribute to peptidase turnover	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	binding of ATP induces a conformational change that facilitates the coupling of nucleotide hydrolysis with peptide substrate delivery to the peptidase active site	Escherichia coli

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Release 2023.1 (January 2023)