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Literature summary for 3.4.21.53 extracted from

  • Patterson-Ward, J.; Tedesco, J.; Hudak, J.; Fishovitz, J.; Becker, J.; Frase, H.; McNamara, K.; Lee, I.
    Utilization of synthetic peptides to evaluate the importance of substrate interaction at the proteolytic site of Escherichia coli Lon protease (2009), Biochim. Biophys. Acta, 1794, 1355-1363.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
investigation of the mode of peptide interaction with the proteolytically inactive Lon mutant S679A in the absence and presence of ADP or AMPPNP shows that the binding interaction between protein and peptide varies with the nucleotide bound to the enzyme Escherichia coli

Protein Variants

Protein Variants Comment Organism
S679A proteolytically inactive Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Reaction

Reaction Comment Organism Reaction ID
hydrolysis of proteins in presence of ATP reaction may involve a substrate translocation step limiting the turnover rate Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lambda phage N protein + H2O generation of a panel of fluorescent peptides based on the cleavage profile of substrate lambda phage N protein indicates that protease Lon recognizes numerous discontinouos substrate determinants throughout lambda N protein to achieve substrate promiscuity Escherichia coli ?
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